Term
| What is intracellular signaling |
|
Definition
| Signals arise within the cell due to allosteric regulation and substrate concentrations |
|
|
Term
| What is intercellular signaling |
|
Definition
| Signaling between differs cells, coordinate developmental and survival activities |
|
|
Term
| What are the types of intercellular signaling |
|
Definition
| Direct contact, synaptic signaling, endocrine signaling |
|
|
Term
| What occurs during direct contact signaling |
|
Definition
| Signals sent between layers of cells at periphery of tissues via gap junctions |
|
|
Term
| When is direct contact signaling used |
|
Definition
| Wen cells are not in good contact with vessels |
|
|
Term
| What does direct contact signaling share with the other cells |
|
Definition
| mRNA, cell cycle regulators, evidence of pathogen invasion, etc |
|
|
Term
| What occurs in synaptic signaling |
|
Definition
| Signaling is carried out using neurotransmitters |
|
|
Term
| What occurs in endocrine signaling |
|
Definition
| Hormone is released in one location and travels to a receptor in another location |
|
|
Term
| War is the function of endocrine signaling |
|
Definition
| Coordinate multiple tissues, regulate and coordinate metabolism |
|
|
Term
| I general, what is a g-protein coupled receptor classified as |
|
Definition
| Integral membrane protein |
|
|
Term
| What is a g-protein coupled receptor specific |
|
Definition
| Because it can only interact with one ligand |
|
|
Term
| How is a g-protein coupled receptor structured? How many units does it have? |
|
Definition
| It has 7 transmembrane domains |
|
|
Term
| What does it mean when said that a g-protein is heterochromatic |
|
Definition
| It has 3 subunits: alpha, beta, gamma |
|
|
Term
| Wen is the G protein alpha subunit located when it is inactive |
|
Definition
| At the beta gamma subunit docking station |
|
|
Term
| How can G protein be stimulatory or inhibitory? |
|
Definition
| It can interact with the G protein coupled receptor to inhibit the process (Gi) or it can interact with the adenylyl cyclase to stimulate the process (Gs) |
|
|
Term
| When the Alpha subunit binds adenylyl cyclase, where does it bind |
|
Definition
| On the guanosine nucleotide |
|
|
Term
| What qualifies the alpha subunit of the G protein to be stimulator or inhibitor |
|
Definition
| If it is working with a stimulating G protein it is stimulating (Gas) when working with a inhibiting G protein it is and inhibitor (Gai) |
|
|
Term
| Once protein kinase A is activated, how does it actually effect the cell |
|
Definition
| It phosphorlyates target proteins which regulates flow of ions across membranes, regulates metabolic pathways using enzymes, acts as DNA binding protein and promotes or inhibits gene expression |
|
|
Term
| What are the steps in the first path we learned to initiate cellular response to intercellular signals |
|
Definition
1. Ligand binds G protein coupled receptor
2. Receptor changes conformation on its inner cellular surface
3. G protein that is interacting with the receptor changes conformation
4. G protein changes GDP to GTP
5. G protein alpha subunit dissociates from the beta gamma dock
6. Alpha subunit changes conformation of adenylyl cyclase
7. Adenylyl cyclase generates cAMP using free ATP
8. cAMP activates protein kinase A by binding to its 2 regulatory subunits and release the two catalytic subunits
9. Protein kinase A phosphorlyates target proteins
10. Alpha subunit hydrolysis GTP to GDP
11. Alpha subunit dissociates from adenylyl cyclase
12. Alpha subunit docks with beta gamma dock |
|
|
Term
| In general, what is a adenylyl cyclase considered to be |
|
Definition
| An integral membrane enzyme |
|
|
Term
| In general, what is cAMP considered to be |
|
Definition
|
|
Term
| When a ligand binds a G protein coupled receptor, what changes occur in the G protein |
|
Definition
| It changes conformation changing GDP to GTP, the alpha subunit dissociates from the beta gamma subunit dock and goes off to find adenylyl cyclase |
|
|
Term
| What tools do adenylyl cyclase need to generate cAMP |
|
Definition
| G protein alpha subunit, ATP |
|
|
Term
| How does cAMP activate protein kinase a |
|
Definition
| It binds to its two regulatory subunits and causes the release of its two catalytic subunits |
|
|
Term
| What hydrolysis GTP back to GDP |
|
Definition
|
|
Term
| Way are the three ways to stop the first path of intercellular signaling |
|
Definition
| Remove the hormone (or other extra cellular signaling molecule), dephosphorlyate proteins, hydrolysis of cAMP |
|
|
Term
| What do protein phosphatses do |
|
Definition
| Hydrological lay cleave phosphate esters and remove effector proteins that are phosphorlyated by protein kinase |
|
|
Term
| What do cAMP phosphodiesterases do |
|
Definition
| Hydrolysis of cAMP, cleaves the phosphodiester bond turning it into 5'-AMP which is inactive |
|
|
Term
| Wy is removing the extra cellular signaling molecule not the most effective way of stopping a intercellular signaling chain |
|
Definition
| The effect can still keep going inside the cell |
|
|
Term
| Explain the process of cholerae infection |
|
Definition
1. It enters the gut and releases cholera toxin
2. Toxin enters the epithelium and is endocytosed, only the elephant subunit enters the cell
3. Alpha subunit is clipped
4. Alpha subunit interacts with ADP ribosylation factor
5. The factor activates adenylyl cyclase permanently
6. Lots of cAMP is made so lots of protein kinase is made
7. Ca is released from the ER opening Cl channels
8. Cl drags positive ions (Na) and water out of the cell into large intestines
9. This much water cannot be absorbed so it causes dirreaha and denydration |
|
|
Term
| How is a cholerae infection treated |
|
Definition
| Water and electrolytes to replace the water lost, there isn't a problem absorbing the water just retaining it |
|
|
Term
| What causes the build up of water in the intestines in a cholerae infection |
|
Definition
| Ca release opens Cl channels and drags after and positive ions and water into the large intestines |
|
|
Term
| What are the steps in the second path we learned to initiate cellular response to intercellular signals |
|
Definition
1. Ligand binds receptor
2. Receptor conformation changes activates Gq protein
3. Gq protein releases GDP and binds GTP
4. Gaq subunit detaches and activates phospholipid C
5. Phospholipid c cleaves the lipid bi layer into IP2, IP3, DAG
6. IP3 binds ER activating Ca channels releasing Ca into cytosol
7. DAG stays in the membrane, activating protein kinase C with the help of Ca
8. Ca and protein kinase C work together as a secondary messenger to turn on phosphorylation proteins |
|
|
Term
| Where is phospholipase C located |
|
Definition
|
|
Term
| What does phospholipase C do when activated |
|
Definition
| Cleaves the lipid bi layer into IP2, IP3, and DAG |
|
|
Term
| If in the liver and the ligand is epinephrine, what intracellular signaling process is activated, how does it happen |
|
Definition
| Glycogen degradation when epinephrine binds a1 adrenic receptor. Calcium binds cal moulin, this new complex changes conformation of enzymes in metabolism |
|
|
Term
| how do organs of metabolism communicate |
|
Definition
| nervous system, circulating substrates, hormones |
|
|
Term
| in metabolism, what do hormones signal for |
|
Definition
|
|
Term
| what is coordination of the metabolism primairly regulated by |
|
Definition
|
|
Term
| what is coordination of the metabolism secondairly regulated by |
|
Definition
| epinepherine and norepinepherine |
|
|
Term
| where is insulin produced |
|
Definition
| beta cells of the islets of langerhan in the pancreas |
|
|
Term
| what is insulin stored in |
|
Definition
|
|
Term
| where is glucagon produced |
|
Definition
| alpha cells of the islets of langerhan in the pancreas |
|
|
Term
| what type of effetor is insulin |
|
Definition
|
|
Term
| what type of effector is glucagon |
|
Definition
|
|
Term
| in general what does insulin affect, what does this cause |
|
Definition
| it affects glycogen, TAGs, and proteins. promotes glucose uptake |
|
|
Term
| in general, what does glucagon affect, what does this cause |
|
Definition
| affects glucose release from the liver. it causes gluconeogenesis and glycogenolysis |
|
|
Term
| what stimulates insulin to be released |
|
Definition
| increased blood glucose, amino acids, peptide hormones, glucagon decreases |
|
|
Term
| what do peptide hormones have to do with insulin |
|
Definition
| when produced due to response to food ingestion, they cause insulin to be released |
|
|
Term
|
Definition
| decreased amino acids, epinepherine |
|
|
Term
|
Definition
| decrease in glucose or amino acids (fasting), increase in epinepherine |
|
|
Term
| what can causes increases in epinepherine in the body |
|
Definition
|
|
Term
| what effect does epinepherine have on the body |
|
Definition
| increases glucagon, decreases glucose, affects mobilization of glucose from the liver and fatty acids from adipose |
|
|
Term
| in general, what inhibits glucagon |
|
Definition
| increasing glucose or insulin levels |
|
|
Term
| what are the types of glucose receptors |
|
Definition
| insulin sensitive and insulin insensitive |
|
|
Term
| what type of tissues are insulin insensitive receptors located |
|
Definition
| in tissues that require uptake of glucose but do not have a role in blood sugar regulation |
|
|
Term
| what tissues have insulin insensitive receptors and use active transport |
|
Definition
| epithelia of intestine, renal tubules, choroid plexus, |
|
|
Term
| what tissues have insulin insensitive receptors and use facilitative transport |
|
Definition
| RBC, WBC, lens of eye, cornea, liver, brain |
|
|
Term
| what type of transport do tissues with insulin sensitive receptors use |
|
Definition
|
|
Term
| what tissues have insulin sensitive receptors |
|
Definition
| most tissues: skeletal muscle, adpipose.. |
|
|
Term
| what is the general cause of hypoglycemia |
|
Definition
| low glucose causes elevated glucagon and epinepherine and low insulin |
|
|
Term
| what are the adrenergic symptoms of hypoglycemia |
|
Definition
| anxiety, papitation, sweating, tremor |
|
|
Term
| what causes the adrenergic symptoms of hypoglycemia |
|
Definition
| epinepherine, ACTH, and growth hormone release from the hypothalamus in response to decreased glucose levels |
|
|
Term
| what are the neuroglycopenia symptoms of hypoglycemia |
|
Definition
| headache, confusion, slurred speech, seizures, coma, death |
|
|
Term
| what causes the neuroglycopenia symptoms of hypoglycemia |
|
Definition
| impaired delivery of glucose to the brain |
|
|
Term
| what is the treatment of hypoglycemia |
|
Definition
| resolved in minutes of glucose intake |
|
|
Term
| what is the main worry of someone who is experiencing hypoglycemia |
|
Definition
| CNS only fuel is glucose, without glucose for too long nerves die, could cause death |
|
|
Term
| what does transient hypoglycemia cause |
|
Definition
|
|
Term
| what are the types of hypoglycemia |
|
Definition
| insulin injected, postparandial, fastine |
|
|
Term
| what type of patients usually have insulin injected hypoglycemia |
|
Definition
|
|
Term
| what are symptoms of insulin injected hypoglycemia |
|
Definition
| unconsious, no coordiinated swallow reflex |
|
|
Term
| how do you treat insulin injected hypoglycemia |
|
Definition
| subcutanous or intramuscular glucagon injection |
|
|
Term
| what is the second most common hypoglycemia |
|
Definition
|
|
Term
| what causes postparandial hypoglycemia |
|
Definition
| exaggerated insulin release following a meal |
|
|
Term
| how do you treat postparandial hypoglycemia |
|
Definition
| auto corrects itself, eat frequent small meals |
|
|
Term
| what is the most rare hypoglycemia |
|
Definition
|
|
Term
| what are the most serious symptoms involved in fasting hypoglycemia |
|
Definition
|
|
Term
| what causes fasting hypoglycemia |
|
Definition
| low liver glucose production, fasting and alcohol, pancreatic tumors that make lots of insulin |
|
|
Term
| what are the three paths you could take to try and inhibit glucagon signaling |
|
Definition
| regulate glyconeogenesis, increase glycogen storage, decrease glycogen storage |
|
|
Term
| how can glycogenesis be regulated to stop glucagon signaliing |
|
Definition
| dephosphorlyate glycogen synthase |
|
|
Term
| how can glycogen storage be increased to stop glucagon signaliing |
|
Definition
| add insulin which decreases cAMP with phosphodiesterase and activates protein phosphatase 1. dephosphorlyate glycogen synthase to activate it |
|
|
Term
| how can glycogen storage be decreased to stop glucagon signaliing |
|
Definition
| glycagon and epinepherine induce cAMP production, protein kinase A phosphorlyates glycogen synthase, phosphorlyated glycogen synthase is inactivated |
|
|
Term
| in gulcagon signaling once the associated enzymes are phosphorlyated, what occurs in the liver |
|
Definition
| break don of glycogen and increased gluconeogenesis, ketogenesis, amino acid uptake to make carbon skeletons for gluconeogenesis |
|
|
Term
| in gulcagon signaling once the associated enzymes are phosphorlyated, what occurs in the adipose |
|
Definition
| activation of lipolysis, free fatty acids are used by the liver to make acetyl coenzyme A to do ketogenesis |
|
|
Term
| what are the steps of glucagon signaliing |
|
Definition
1. glucagon binds glucagon receptor
2. receptor activates g-protein which activates adenylyl cyclase
3. adenylyl clcyase generates cAMP
4. protein kinase phosphorlyates and activates metabolic enzymes |
|
|
Term
| what are the steps of insulin signaling |
|
Definition
1. insulin binds receptor tyrosine kinase on the insulin receptor
2. tyrosine kinase phosphorlyates beta subunit of insulin receptor and insulin receptor substrates
3. substrates promote activation of protein kinases and phosphatases
4. proteins affect gene expression, cell metabolism, and cell growth |
|
|
Term
| once insulin binds to the membrane, what changes occur in the membrane |
|
Definition
| insulin promotes recruitment of insulin sensitive glucose transporters in so more transporters come to the membrane and increase insulin mediated glucose uptake |
|
|
Term
| what changes occur in the membrane after insuliin levels are reduced |
|
Definition
| glucose transporters are taken out of the membrane and stored in the cell as endosome |
|
|
Term
| after signaling, what does insulin cause to happen to carbohydrate metabolism (explain what goes on in each tissue) |
|
Definition
| glycogen synthesis in the liver, increases glucose transporters in muscle (GLUT-4), in adipose it causes glycerol-3-phosphate synthesis for TAG production |
|
|
Term
| after signaling, what does insulin cause to happen to lipid metabolism |
|
Definition
| takes fatty acids out of the blood to increase TG synthesis in adipose, uses glucose to make glycerol-3-phosphage and FA for TAG synthesis |
|
|
Term
| after signaling, what does insulin cause to happen to protein metabolism |
|
Definition
| stimulates amino acid uptake by most tissues and protein synthesis |
|
|
Term
| How do beta cells sense changes in glucose levels, explain the process |
|
Definition
| Sugar is phosphorlyated by glucokinase and converted to ATP, the increase in ATP closes K channels, depolarizing the membrane, calcium voltage gated ion channels open, calcium flows in, fusion and secretion of insulin granules that are inside the cell |
|
|
Term
| what is the purpose of a metabolic map |
|
Definition
| shows big picture of meatbolic pathways, helps you visualize intermediates, helps you figure out what happens if you block a step |
|
|
Term
| what does catabolism mean |
|
Definition
| degredation or break down of complex molecules |
|
|
Term
| what are examples of what catabolism might break down |
|
Definition
| proteins, polysaccharides, lipids, CO2, NH3, H20 |
|
|
Term
|
Definition
| synthesis. reactions form complex products from simple precursors |
|
|
Term
| what is an example of a reaction of anabolism |
|
Definition
|
|
Term
| what role does catabolism play in metabolism |
|
Definition
| captures energy from ATP, NADH, or NADPH via degregation of energy rich fuels, allows us to reduce complex molecules from storage or diet into useful building blocks for other compounds |
|
|
Term
| what does catabolism do to proteins |
|
Definition
| breaks them into amino acids |
|
|
Term
| what does catabolism do to carbohydrates |
|
Definition
| breaks them into monosaccharides |
|
|
Term
| what does catabolism do to fat |
|
Definition
| breaks it into fatty acids and glycerol |
|
|
Term
| once catabolism makes amino acids, monosaccharides, fatty acids, and glycerol, in general, what happens to them |
|
Definition
| they are converted to acetylyl CoA, put into the TCA cycle which oxidizes it, and makes fatty acids, cholesterol, ketones, and other complex molecules |
|
|
Term
| what does anabolism do to amino acids |
|
Definition
|
|
Term
| what does anabolism need to work |
|
Definition
| energy: ATP or reduced compounds (NADH or NADPH) |
|
|
Term
| what is the time span of the well fed state |
|
Definition
|
|
Term
| what is another word for the well fed state |
|
Definition
|
|
Term
| what basic changes occur in the well fed state in the body |
|
Definition
1. increase in blood glucose, AA, TAG (as chylomicrons) from the food
2. pancreas releases insulin secretion and decreases glucagon release
3. glycogen and TAG synthesis increases to replenish fuel storage
4. protein synthesis increased to replenish what was used in fasting (protein isnt stored) |
|
|
Term
| what factors control metabolism (control the enzymes) |
|
Definition
| avability of substrates, allosteric regulation, covalent modification, induction or repression of enzyme synthesis |
|
|
Term
| in what pathways of metabolism does gene expression regulation occur |
|
Definition
| in ones that are only active in certian physiological conditions, influences enzyme avability not how well the enzyme works |
|
|
Term
| on what molecules does covalent modification of enzymes occur |
|
Definition
|
|
Term
| at what point do allosteric enzymes usually regulate |
|
Definition
|
|
Term
| what organ is considered to be the nutrient distribution center for the metabolism |
|
Definition
|
|
Term
| what does the venous drainage of the portal vein do for the nutrients in the body |
|
Definition
| it makes them all enter the liver first to be stored, rerouted, or metabolized |
|
|
Term
| in general, what is the function of the liver in metabolism |
|
Definition
| allow smoothing of broad fluxuations of nutrients. stores what you have too much of or breaks down molecules to get the nutrients you need more of |
|
|
Term
| what is the only organ that releases glucose |
|
Definition
|
|
Term
| what can the liver do with glucose |
|
Definition
| release it when blood glucose is low, store it if it is high |
|
|
Term
| what type of insulin receptors does the liver have |
|
Definition
| GLUT 2 non-insulin sensitive |
|
|
Term
| what happens to glucose once it enters the liver cell |
|
Definition
| it is phosphorlyated by glucokinase |
|
|
Term
| what can the liver do with glycogen |
|
Definition
| increase glycogen synthesis to store sugars, glycolysis |
|
|
Term
| describe the carbohydrate metabolism of the liver when well fed |
|
Definition
| when glucose is taken it it causes glycogen synthesis, increases activity of hexos monophosphate pathway providing NADPH and NADH for FA synthesis, increases glycolysis, decreases glyconeogenesis |
|
|
Term
| describe the role of liver in fat metabolism when well fed |
|
Definition
| increases fatty acid synthesis, turns chylomicrons into fatty acids then TAG which are transported to adipose in VLDL |
|
|
Term
| describe the role of the liver in amino acid metabolism when well fed |
|
Definition
| increases amino acid degration sending amino acids to the blood, tissues, or to be deaminated, uses AA in the tCA cycle for fat synthesis, increase protein synthesis |
|
|
Term
| describe the role of the adipose tissue in well fed metabolism |
|
Definition
| increases glycolysis to give energy, makes glycerol and uses VLDL FA to make fat, stores FA brought by VLDL |
|
|
Term
| why does adipose have to make glycerol |
|
Definition
| because the glycerol brought with the FA it stores, from the VLDL from the liver cannot enter the cell so to store TAG it needs to make its own glycerol to pair with the FA |
|
|
Term
| how does insulin inhibit TAG degredation |
|
Definition
| insulin causes phosphorlyzation of hormone sensitive lipase which inactivates it stopping TAG break down |
|
|
Term
| for what reason does muscle change its role in metabolism |
|
Definition
| changes in demand for ATP from muscle contraction |
|
|
Term
| what glucose receptors does adipose tissues have |
|
Definition
|
|
Term
| what glucose receptors does skeletal muscle have |
|
Definition
|
|
Term
| what role does the skeletal muscle have in carbohydrate metabolism when well fed |
|
Definition
| increases glucose transport due to increased blood glucose levels or insulin and does glycolysis with it, or increases glyogen synthesis |
|
|
Term
| what role does skeletal muscle play in amino acid metabolism when well fed |
|
Definition
| increases protein synthesis, increases uptake of branched chain AA to do protein synthesis |
|
|
Term
| what is the primary site for amino acid degredation |
|
Definition
|
|
Term
| how does heart muscle store glycogen or lipids |
|
Definition
|
|
Term
| does the heart need glucose storage? why |
|
Definition
| no, it is aerobic and needs oxygen at all times |
|
|
Term
| what does the heart muscle use for energy |
|
Definition
| fatty acids, glucose, ketone bodies |
|
|
Term
| for what reason does muscle change its role in metabolism |
|
Definition
| changes in demand for ATP from muscle contraction |
|
|
Term
| what glucose receptors does adipose tissues have |
|
Definition
|
|
Term
| what glucose receptors does skeletal muscle have |
|
Definition
|
|
Term
| what role does the skeletal muscle have in carbohydrate metabolism |
|
Definition
| increases glucose transport due to increased blood glucose levels or insulin and does glycolysis with it, or increases glyogen synthesis |
|
|
Term
| what role does skeletal muscle play in amino acid metabolism when well fed |
|
Definition
| increases protein synthesis, increases uptake of branched chain AA to do protein synthesis |
|
|
Term
| what is the primary site for amino acid degredation |
|
Definition
|
|
Term
| how does heart muscle store glycogen or lipids |
|
Definition
|
|
Term
| does the heart need glucose storage? why |
|
Definition
| no, it is aerobic and needs oxygen at all times |
|
|
Term
| what does the heart muscle use for energy |
|
Definition
| fatty acids, glucose, ketone bodies |
|
|
Term
| why does the brain need to use only glucose for fuel |
|
Definition
| FA cannot get across blood brain barrier |
|
|
Term
| when does the fasting state occur |
|
Definition
|
|
Term
| what type of reactions occur in the fasting state |
|
Definition
|
|
Term
| what is the first thing to happen when fasting that triggers the other fasting processes |
|
Definition
| blood glucose, AA, and TAG fall |
|
|
Term
| what does the pancreas do in response to low blood glycose, AA, or TAG |
|
Definition
| decreases insulin release, increases glucagon synthesis |
|
|
Term
| when fasting, what are the two main concerns the body has before all other |
|
Definition
| maintain blood glucose level for tissues (especially RBC and brain), mobilize FA and ketone |
|
|
Term
| what are the types of stored fuel in the body, how much energy can they provide relative to eachother |
|
Definition
| glycogen (provides little energy), protein (provides medium energy), TAG (provides most energy) |
|
|
Term
| how much protein can be lost in fasting before there are fatal complications |
|
Definition
|
|
Term
| what is the main function of the liver in fastin |
|
Definition
|
|
Term
| how is the liver involved in carbohydrate metabolism when fasting |
|
Definition
| degrades glycogen into glucose, once glycogen depletes it does gluconeogenesis |
|
|
Term
| how is the liver involved in fat metabolism when fasting |
|
Definition
| it takes the products of fatty acid oxidation and uses them for gluconeogenesis. it takes in ketones and does ketoneogenesis |
|
|
Term
| what is the role of adipose in carbohydrate metabolism when fasting |
|
Definition
| decreased insulin causes endocytosis of GLUT 4 insulin sensitive receptors, this decreases enterance of glucose and decreases glycolysis |
|
|
Term
| what role does adipose tissue have in fat metabolism in fasting |
|
Definition
| degrades TAG for fuel. releases FA for fuel and glycerol to be used in gluconeogenesis in the liver, decreases FA uptake |
|
|
Term
| what role does skeletal muscle have in carbohydrate metabolism when fasting |
|
Definition
| decreased insulin causes endocytosis of GLUT 4 insulin sensitive receptors, this decreases enterance of glucose and decreases glycolysis |
|
|
Term
| what role does skeletal muscle have in lipid metabolism when fasting, what changes occur over time |
|
Definition
| uses ketone bodies and FA as fuel, at 2 weeks it uses FA almost exclusivly |
|
|
Term
| whty does the skeletal muscle change to only using FA when fasting |
|
Definition
| because they brain needs the ketone bodies |
|
|
Term
| what is the role of skeletal muscle in protein metabolism during fasting |
|
Definition
| breas down providing protein for gluconeogensis |
|
|
Term
| in the first few days of fasting what does the brain use as food |
|
Definition
|
|
Term
| after prolonged fasting what does the brain use for food, why |
|
Definition
| mostly keytone bodies to conserve muscle protein |
|
|
Term
| what is the role of kidney in metabolism |
|
Definition
| can make or release glucose, metabolizes glutamein reasing ammonia which picks up H+ put into blood by ketone bodies (ketoacidosis), ammonia pickes up the acid and is excreted in urine |
|
|
Term
| what is the most abundent organic molecule |
|
Definition
|
|
Term
| what are the functions of carbohydrates |
|
Definition
| calories, energy source via glycogen, membrane compooents that mediate communication, structural components |
|
|
Term
| what types of structural membrane components do carbohydrates make |
|
Definition
| bacteria cell wall, exoskeleton of insects, fibrous cellulose of plants |
|
|
Term
| what is the basic structural unit of a carb |
|
Definition
|
|
Term
| how are monosacchardies named / classified. give examples |
|
Definition
| by number of carbons (triose, tetroses, pentoses, hexoses |
|
|
Term
| what functional groups can a carb have (how does this also change the name of the molecule) |
|
Definition
| aldehyde (aldoses), ketone (ketoses) |
|
|
Term
| what are the names of the polymeres of carbs, how many monomoeres do they specify |
|
Definition
| disaccharide 2, oligosaccharide 3-10, polysaccharide > 10 |
|
|
Term
|
Definition
| same formula, different structure |
|
|
Term
| what is an example of an isomere |
|
Definition
|
|
Term
| when numbering carbons on a carb, what do you begin with |
|
Definition
|
|
Term
| what type of monosaccharides are usually cyclic |
|
Definition
|
|
Term
| what interaction causes cyclic carbs |
|
Definition
| aledhyde or keytone reacts with -OH of same sugar |
|
|
Term
|
Definition
| 6 membered ring with 5 C and 1 O |
|
|
Term
|
Definition
| 5 membered right with 4 C and 1 O |
|
|
Term
| when a carb is cyclic what does this do to the structure |
|
Definition
| causes there to be an anomeric C (isomere) that is in alpha or beta form |
|
|
Term
| how is the anomeric carbon on a carb physiologically relivent |
|
Definition
| enzymes only react with one of the anomeric conformations |
|
|
Term
| what bond joins monosaccharides |
|
Definition
|
|
Term
| what are the different types of glycidic bonds |
|
Definition
| alpha and beta (depending on isomere of the sugar) |
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
| describe the structure of glycogen |
|
Definition
| many glucose alpha linked and branched |
|
|
Term
| where does starch come from |
|
Definition
|
|
Term
| where does glycogen come from |
|
Definition
|
|
Term
| where does cellulose come from |
|
Definition
|
|
Term
| describe the structure of starch |
|
Definition
| glucose alpha linked and branched |
|
|
Term
| describe the structure of cellulose |
|
Definition
|
|
Term
| how are glycocidic bonds named |
|
Definition
| according to connected carbons: C1 to beta-galactose = B1-4 glycocidic bond |
|
|
Term
| what are complex carbohydrates |
|
Definition
| carbs attached to non-carb structures |
|
|
Term
| gives some examples of complex carbohydrates |
|
Definition
| purines and pyrimidines, aromatic rings in steriods, glycoproteins, glycolipids |
|
|
Term
| what is the bond called when a sugar is attached to a non carb with the NH2 group |
|
Definition
|
|
Term
| what is the bond called when a sugar is attached to a non carb with the -OH group |
|
Definition
|
|
Term
| explain the process of digestion of carbs |
|
Definition
1. mouth: salivary amalyase breaks a1-4 of starch and glycogen
2. low stomach pH inactivates salivary amalyase
3. SI: pancreatic amalyase, similar to salivary amalyase
4. luminal side of brush border membrane intestinal cells secrete different enzymes
4. monosaccharidestaken up by transporter |
|
|
Term
| what enzymes does the lumenal side of the brush border membrane intestinal mucosa cells release |
|
Definition
| sucrase isomaltase complex, maltase, lactase |
|
|
Term
| what does the sucrase portion of the sucrase isomaltase complex do |
|
Definition
| digests sucrose into glucose and fructose |
|
|
Term
| what does the isomaltase portion of the sucrase isomaltase complex do |
|
Definition
| cleaves maltose into 2 glucose. cleaves a1-6 bonds |
|
|
Term
|
Definition
| cleaves maltose and maltotriose a1-4 bonds |
|
|
Term
|
Definition
|
|
Term
| what happens in the large intestines when there is abnormal digestion of carbs |
|
Definition
| disaccharides end up in LI causing osmotic pressure leading to diarrhea. bacteria in the LI ferment carbs into CO2, H2, and methane. they also make 1-3 C compounds increasing osmotic imbalance leading to diarrhea |
|
|
Term
| what conditions can cause abnormal digestion of carbs |
|
Definition
| inflammatory bowel disease (chron's disease), malnutrition, drugs (chemotherapeutics), dietary intolerances |
|
|
Term
| what is defficient in a lactose intolerance, how do you treat it |
|
Definition
| lactase. avoid milk, suppliment with Ca |
|
|
Term
| what mutation causes a lactose intolerance |
|
Definition
| none! the people with the intolerance are normal |
|
|
Term
| when someone has a sucrase-isomaltase complex deficiency, what is the result |
|
Definition
|
|
Term
| how do you treat a sucrose intolerance |
|
Definition
| avoid sucrose, take replacement enzymes |
|
|
Term
| how can you diagnose dietary intolerances |
|
Definition
| oral tolerance test, takes a H+ breath measurement. H+ is proportional to sugar metabolized |
|
|
Term
| what does glycolysis produce if you have oxygen and mitochondroa |
|
Definition
| makes intermediates for other pathways, ATP, pyuvate |
|
|
Term
| what does glycolysis produce if you dont have oxygen or mitochondria |
|
Definition
| intermediates for other pathways, ATP, lactate |
|
|
Term
| what are the ways to transport glycose into a cell |
|
Definition
| Na independent facilitated diffusion, Na monosaccharide cotransporter |
|
|
Term
| what occurs in sodium independent facilitated diffusion |
|
Definition
| high glucose out of the cell and low in makes a gradient glucose 1-14 transporters span mambrane and change conformation when glucose binds transporting it across the membrane |
|
|
Term
| where are glut 1 and 3 transporters located |
|
Definition
| in most tissues, especially brain (1) and neurons (3) |
|
|
Term
| what do glue 1 and 3 transporters function in |
|
Definition
|
|
Term
| where are glut 2 transporters located |
|
Definition
| liver, pancreatic beta cells |
|
|
Term
| what do glut 2 transporters function in, what conditions do they need |
|
Definition
| uptake and release, glucose sensors, low affinity, need lots of glucose to work |
|
|
Term
| where are glut 4 transporters located |
|
Definition
| skeletal muscle and adipose |
|
|
Term
| what do glut 4 transporters function in, what conditions do they need |
|
Definition
| stimulated by glucose uptake and exercise. insulin sensitive. come to surface when insulin is present |
|
|
Term
| how does sodium monosaccharide cotransport work |
|
Definition
| uses energy to transport glucose against its gradient by cotransporting it with sodium down sodium's gradient |
|
|
Term
| where does sodium monosaccharide cotransport happen |
|
Definition
| epithelial cells of intestine, renal tubules, choroid plexus, sodium dependent glucose transporter |
|
|
Term
| what does sodium monosaccharide cotransport do in epithelial cells |
|
Definition
|
|
Term
| what does sodium monosaccharide cotransport do in renal tubules |
|
Definition
|
|
Term
| wha does sodium monosaccharide cotransport do in the choroid plexus |
|
Definition
| allows glucose to cross blood brain barrier into CSF using glut 1 |
|
|
Term
| what is the role of sodium monosaccharide cotransport in sodium dependent glucose transporters |
|
Definition
| needs tissue specific isoforms |
|
|
Term
| what are the first 5 reactions of glycolysis function in |
|
Definition
| energy investment, provides phosphorlyated forms of intermediates |
|
|
Term
| what do the first 5 reactions use |
|
Definition
|
|
Term
| what do subsequent generations of glycolysis make |
|
Definition
| 4 ATP, glucose 2 NADH, pyruvate |
|
|
Term
| in glycolysis what does glucose turn into next, what enzymes help |
|
Definition
| glycose-6-phosphate, hexokinase or glucokinase |
|
|
Term
| where is hexokinase active in glycolysis |
|
Definition
|
|
Term
| in glycolysis describe rate and affinity of hexokinase |
|
Definition
| low affinity, low Vmax. can be easily saturated |
|
|
Term
| in glycolysis what inhibits hexokinase |
|
Definition
|
|
Term
| in glycolysis where is glucokinase used |
|
Definition
| liver, pancreatic B cells |
|
|
Term
| in glycolysis describe rate and affinity of glucokinase |
|
Definition
|
|
Term
| what isglucokinase stimulated by |
|
Definition
|
|
Term
| in glycolysis what does glucose-6-phosphate turn into |
|
Definition
|
|
Term
| what enzymes tunrs glucose-6-phoshate into fructose-6-phoshate |
|
Definition
|
|
Term
| what is the rate limiting step in glycolysis |
|
Definition
| fructose-6-phosphate to fructose-1,6-biphosphate |
|
|
Term
| what is the committed step in glycolysis |
|
Definition
| fructose-6-phosphate to fructose-1,6-biphosphate |
|
|
Term
| what enzyme catalyzes fructose-6-phosphate to fructose-1,6-biphosphate |
|
Definition
| phosphofructokinase 1 (PFK 1) |
|
|
Term
| what inhibits PFK 1, what do these forms of inhibition suggest physiologically |
|
Definition
| ATP (you have enough energy), citrate (TCA is backed up) |
|
|
Term
| what stimulates PFK 1, what do these forms of stimulation suggest physiologically |
|
Definition
| AMP (you have low energy, ATP was used up), fructose-2,6-Bisphosphate (there is insulin present |
|
|
Term
| what are the irreversible reactions in glycolysis |
|
Definition
| phosphoralyzation of glucose, fructose-6-phosphate to fructose 1,6-bisphosphate, phosphoenolpyruvate to pyruvate |
|
|
Term
| where does fructose-2,6-bisphosphate regulates glycolysis |
|
Definition
|
|
Term
| what needs to happen for fructose-2,6-bisphosphate to be produced |
|
Definition
| insulin needs to be present which causes PFK-2 to be DEphosphorlyated |
|
|
Term
| what needs to happen for fructose-2,6-bisphosphate to not be produced |
|
Definition
| glucagon needs to be present causing PFK-2 to be phosphorlyated |
|
|
Term
| what does fructose-2,6-bisphosphate do for regulation of glycolysis |
|
Definition
| when insulin is present it is made and it activates PFK-1 |
|
|
Term
| what enzyme helps make fructose-2,6-bisphosphate |
|
Definition
|
|
Term
| in what state is PFK-2 when it is active |
|
Definition
|
|
Term
| are PFK-1 and PRK-2 usually active at the same time, why would this be |
|
Definition
| yes, because they both help glycolysis go forward. PFK-2 creates a product that helps PFK-1 |
|
|
Term
| in glycolysis, what does fructose-1,6-bisphosphate turn into, how? |
|
Definition
| the 6 C molecule splits into 2x 3 C molecules: dehydroxyacetone phosphate and glyceraldehyde-3-phosphate |
|
|
Term
| are dehydroxyacetone phosphate and glyceraldehyde-3-phosphate both used in glycolysis? what happens in glycolysis between these molecules? how? |
|
Definition
| dehydroxy acetone phosphate is turned into glyceraldehyde-3-phosphate for glycolysis to continue via triose-phosphate-isomerase |
|
|
Term
| what catalyzes the conversion of fructose-1,6-bisphosphate to dehydroxyacetone phosphate and glyceraldehyde-3-phosphate? |
|
Definition
| aldolase (not aldolase B!) |
|
|
Term
| in glycolysis, what does glyceraldehyde-3-phosphate turn into? what major changes occur during this step to the molecule? why? |
|
Definition
| 1,3-BPG. an inorganic phosphate is added for future ATP creation. NAD+ is converted to NADH which is high energy |
|
|
Term
| what enzyme catalyzes the conversion of glyceraldehyde-3-phosphate into 1,3-BPG? |
|
Definition
| glyceraldehyde-3-phosphate dehydrogenase |
|
|
Term
| in glycolysis what does 1,3-BPG turn into? what major event takes place assisting the formation of the product? |
|
Definition
| the inorganic phosphate is removed from 1.3-BPG and given to ADP making ATP! the product of this is 3-phosphoglycerate |
|
|
Term
| what is substrate level phosphorlyation |
|
Definition
| energy for phosphorlyation comes from substrate |
|
|
Term
| what enzyme catalyzes the conversion of 1,3-BPG to 3-phosphoglycerate |
|
Definition
|
|
Term
| what reactions in glycolysis participate in substrate level phosphorlyation |
|
Definition
| 1,3-BPG to 3-phosphoglycerate, phosphoenolpyruvate to pyruvate |
|
|
Term
| in glycolysis what does 3-phosphopglycerate turn into? what enzyme helps this? |
|
Definition
| 2-phosphoglycerate via phosphoglycerate mutase |
|
|
Term
| in glycolysis what does 2-phosphoglycerate turn into? what enzymes helps this? |
|
Definition
| phosphoenolpyruvate (PEP), via enolase |
|
|
Term
| what is the final step in glycolysis |
|
Definition
|
|
Term
| what catalyzes the final step in glycolysis |
|
Definition
|
|
Term
| what atom interchange facilitates the conversion of PEP to pyruvate, what is the product of this |
|
Definition
| an inorganic phosphate from PEP is removed and given to ADP making ATP! the result is pyruvate |
|
|
Term
| what stimulates pyruvate kinase |
|
Definition
| in the liver insulin activates it, fructose-1,6-bisphosphate |
|
|
Term
| what inhibits pyruvate kinase |
|
Definition
| in the liver glucagon inactivates it |
|
|
Term
| how is pyruvate kinase really controlled by the PFK-1 reaction (which is the true regulatory reaction) |
|
Definition
| pyruvate kinase is controlled by the product of this reaction, fructose-1,6-bisphosphate, so pyruvate kinase is in turn controlled by the same stuff PFK-1 is controlled by because it needs to be working to make fructose-1,6-bisphosphate |
|
|
Term
| in what state is pyruvate kinase turned on |
|
Definition
|
|
Term
| in what state is pyruvate kinase turned off |
|
Definition
|
|
Term
| what moleule can be turned into 2,3-BPG |
|
Definition
|
|
Term
| what enzyme turns 1,3-BPG into 2,3-BPG |
|
Definition
|
|
Term
|
Definition
| lowers Hb affinity, increasing O2 drop off in the tissues |
|
|
Term
| how can 2,3-BPG be lowered |
|
Definition
| phosphatase can turn it into 3-phosphoglycerate which can be sent back into glycolysis |
|
|
Term
| if there is oxygen and mitochondria, what is pyruvate turned into |
|
Definition
|
|
Term
| if there is no oxygen or mitochondria, what is pyruvate turned into |
|
Definition
|
|
Term
| what enzyme helps turn pyruvate into lactate |
|
Definition
|
|
Term
| what does pyruvate turning into lactate produce, what function does this product have |
|
Definition
| it turns NADH into NAD+ which allows glycolysis to keep going because it is a needed product |
|
|
Term
| what is the fate of some of the lactate after produced due to an anaerobic enivornment |
|
Definition
| it goes to the blood then to the liver where it can be used in gluconeogenesis where its reversabe enzyme (lactate dehydrognase) can turn it back into pyruvate to make glucose |
|
|
Term
| what os oxaloacatate made from |
|
Definition
|
|
Term
|
Definition
| replenish TCA intermediates, glucoenogenesis |
|
|
Term
| what is the net yield of glycolysis, why |
|
Definition
| 2 ATP and 2 NADH. a 6 C molecule split into 2x 3 C molecules. this created two pathways that each produced 2ATP and 1NADH. it cost 2 ATP to run glycolysis |
|
|
Term
| what is the net yield of glycolysis done in an anaerobic enivornment |
|
Definition
|
|
Term
| what changes occur in glycolysis if there are prolonged levels of insulin exposure in the body |
|
Definition
| it would increase in transciprion of proteins involved in glycolysis |
|
|
Term
| why would there be an decrease in transcription of proteins revolving around glucagon |
|
Definition
| fasting, untreated type 1 diabetes |
|
|
Term
| why would someone have prolonged exposure to insulin |
|
Definition
| increased carbohydrate diet, insulin therapy |
|
|
Term
| what happens when someone has a glucokinase mutation |
|
Definition
| increases Km or decreases Vmax. this increases blood sugar causing maturity onset diabetes of the young |
|
|
Term
| how does arsenic primairly poison the body |
|
Definition
| inhibition of enzymes that use lipoic acid (a coenzyme) |
|
|
Term
| what does arsenic disrupt in glycolysis |
|
Definition
| inserts into glyceraldehyde instead of an inorganic phosphate so in the next step, 1,3-BPG to 3-phosphoglycerate, no ATP is made. |
|
|
Term
| what occurs in a pyruvate kinase mutation |
|
Definition
| increases Km or decreases Vmax, in RBC pumps that maintain the shape fail because there is no ATP which causes damage to the RBC in vascular system and for them to be removed from circulation causing hemolytic anemia |
|
|
Term
| what is the second most common genetic enzyme deficiency that causes hemolytic anemia |
|
Definition
|
|
Term
| what is the first most common genetic enzyme deficiency that causes hemolytic anemia |
|
Definition
| glucose-6-phoshpate dehydrogenase deficiency |
|
|
Term
| what is different between a glucose-6-phoshpate dehydrogenase deficiency and a pyruvate kinase deficiency.. other than the ovbious different enzyme |
|
Definition
| in the glucose-6-phoshpate dehydrogenase deficiency there are Heinz bodies |
|
|
Term
|
Definition
|
|
Term
|
Definition
| RBC and exercising muscle |
|
|
Term
| in muscles, what does excess lactate cause |
|
Definition
|
|
Term
| after lactate is made in RBC and muscle, where does it go |
|
Definition
| into the plasma and is then taken up by the liver / tissues or other paths |
|
|
Term
| what happens if there is a lot of lactate in the blood |
|
Definition
| lactic acid acidosis (low blood pH) |
|
|
Term
| what happens when there is no oxygen and lactate builds up in a tissue |
|
Definition
|
|
Term
| where is fructose found in the diet |
|
Definition
| sucrose, fruit, table sugar |
|
|
Term
| how is fructose taken into the cell, how does this affect the chemical messengers in metabolism |
|
Definition
| by non-insuliin dependent transporters, does not promote insulin secretion |
|
|
Term
| what is the first (common) step in fructose metabolism |
|
Definition
| fructose to fructose-1-phosphate using ATP vua fructokinase |
|
|
Term
| where is fructokinase located |
|
Definition
| mostly in the liver, kidney, small intestine mucosal cells |
|
|
Term
| what is the first (uncommon) step in fructose metabolism. why is it uncommon |
|
Definition
| fructose to fructose-6-phosphate vua hexokinase. because hexokinase has a low affinity so you would need a lot of fructose |
|
|
Term
| what is fructose-1-phosphate turned into, by what |
|
Definition
| DHAP and glyceraldehyde by aldolase B |
|
|
Term
| what pathways can aldolase B be part of, why is it special |
|
Definition
| it can be part of glycolysis or fructose metabolism, but none of the other aldolases that can take part in glycolysys can do fructose metabolism. |
|
|
Term
| in fructose metabolism, what happens to glyceraldehyde |
|
Definition
| it is turned into glycerol. turned into glyceraldehyde-3-P and used for glycolysis or gluconeogenesis |
|
|
Term
| what happens to DHAP in fructose metabolism |
|
Definition
| it is used for glycolysis or glyconeogenesis |
|
|
Term
| why is fructose rapidly metabolized |
|
Definition
| because it skips the PFK-1 step in its metabolism, it is not regulated like glycolysis is |
|
|
Term
| what turns glucose into sorbitol |
|
Definition
|
|
Term
| what turns sorbitol into fructose |
|
Definition
|
|
Term
| where is aldose reductase located |
|
Definition
| lens, retina, schwann cells of peripherial nerves, liver, kidney, cells of ovaries, seminal vesicles |
|
|
Term
| where is sorbitol located |
|
Definition
| liver, kidney, ovaries, seminal vesicles |
|
|
Term
| what happens in an sorbitol dehydrogenase deficiency |
|
Definition
| glucose turns into sorbitol and it builds up making osmotic water uptake causing diabetes symptoms: cataracts, retinopathy, neuropathy |
|
|
Term
| what can cause glucose to turn into sorbitol |
|
Definition
| some tissues require the product of the next step, fructose. if there is a lot of glucos ein the blood this will just happen |
|
|
Term
| what is the name of the disease with a fructosekinase deficiency |
|
Definition
| essential fructoseuira / HFI |
|
|
Term
| what does a fructose kinase deficiency cause |
|
Definition
| elevated sugar levels in urine, benign |
|
|
Term
| why is cataracts not a symptom of fructose kinase deficiency |
|
Definition
| because fructose is not a substrate for aldolase reactions |
|
|
Term
| what does aldolase B deficiency cause |
|
Definition
| fructose intolerance, hepatomeaguly, jaundice, hypoglycemia, renal dysfunction |
|
|
Term
| how is aldolase b deficiency treated |
|
Definition
| avoid fructose, sucrose, and sorbitol |
|
|
Term
| what are the steps in an aldolase b deficiency causing hyperuricema |
|
Definition
| fructose enters the cell and is phosphorlyated trapping it in, it cannot be metabolized so it builds up, cellular phosphate is tied up trying to phosphorlyate fructose decreasing ATP levels, AMP builds up causing AMP degeneration leading to hyperuricema |
|
|
Term
| what is the first step in galactose metabolism |
|
Definition
| galactose to galactose-1-phosohate using galactose kinase and ATP. |
|
|
Term
| what does galactose-1-phosphate turn into, using what enzyme |
|
Definition
| galactose-1-phoshpate uridyltransverase helps it chane to UDP galactose and glucose-1-phosphate (using a UDP glucose made by the cell and exchanging UDP for P) |
|
|
Term
| what are the symptoms of a galactokinase deficiency |
|
Definition
|
|
Term
| how does a galactokinase deficiency cause cataracts |
|
Definition
| galactose is a substrate for aldose reductase so when it builds up it reacts with that as a catalyst to make galactiol which is trapped in the cell and causes an osmotic gradient |
|
|
Term
| what disease does a galactose-1-phosphate uritotransferase deficiency cause |
|
Definition
|
|
Term
| what are the symptoms of classic galactosemia |
|
Definition
| early cataracts, liver and kidney damage, nerve damage (retardation) |
|
|
Term
| what chemical process causes the symptom of cataracts in classic galactosemia |
|
Definition
| increased galactose-1-phosphate inhibits galactokinase which increases galactose causing cataracts |
|
|
Term
| what chemical process causes the symptoms of classic galactosemia |
|
Definition
| increased galactose-1-phosphate ties up the use of the cell phosphate causing decreased ATP |
|
|
Term
| how is classic galactosemia treated |
|
Definition
|
|
Term
|
Definition
| tricarboxcylic acid cycle |
|
|
Term
| what are other ways to say TCA cycle |
|
Definition
|
|
Term
| overall what does the TCA cycle do |
|
Definition
| metabolizes carbs, AA, FA into CO2 which is exhaled. ATP production. |
|
|
Term
| where does the TCA cycle occur |
|
Definition
| in mitochondria near the ETC |
|
|
Term
| what does the ETC do, in general |
|
Definition
| couples oxidation of reduced coenzymes made in TCA to production of ATP |
|
|
Term
| what is the TCA cycle dependent on, why |
|
Definition
| oxygen, it is aerobic. because O2 is the final e- acceprot in the ETC |
|
|
Term
| what origional ingredients are lost in the TCA cycle, explain |
|
Definition
| none, oxaloacetate is the rectant and the final product of the ccle |
|
|
Term
| what is the reaction that connects glycolysis to the TCA cycle |
|
Definition
| oxidative decarboxylation of purivate, pyruvate to acetyl CoA |
|
|
Term
| what are the reactantS and productS of oxidative decarbodylation of pyruvate |
|
Definition
| pyruvate + CoA + NAD+ --> NADH + CO2 + acetyl CoA |
|
|
Term
| what enzyme catalyzes oxidative decarboxylation of pyruvate |
|
Definition
| pyruvate dehydrogenase complex |
|
|
Term
| is oxidative decarboxylation of pyruvate a comitted step, what does that mean |
|
Definition
| yes, only goes in one direaction |
|
|
Term
| what activates pyruvate dehydrogenase |
|
Definition
| pyruvate, NAD+, ADP, Ca in muscle, CoA |
|
|
Term
| what deactivates pyruvate dehydrogenase |
|
Definition
|
|
Term
| before oxidative decarboxylation of pyruvate, but after glycolysis what needs to happen |
|
Definition
| pyruvate needs to be transported into the mitochondria via sepcific transporters |
|
|
Term
| what are the coenzymes included in the pyruvate dehydrogenase complex |
|
Definition
| thiamine pyrophosphate (TPP), lipoid acid, CoA, FAD, NAD+ |
|
|
Term
| where does lipoic acid come from |
|
Definition
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
| where does NAD+ come from |
|
Definition
|
|
Term
| how many ATP are made total per glucose in the TCA cycle |
|
Definition
|
|
Term
| what is the break down of true products that adds up to 12 ATP total made in TCA cycle |
|
Definition
3 NADH = 9 ATP,
1 FADH2 = 2 ATP,
1 GTP = 1 ATP |
|
|
Term
| after the TCA cycle, how many ATP have been made total |
|
Definition
|
|
Term
| explain how there are 38 total ATP after TCA per molecule of glucose |
|
Definition
glycolysis: 8
oxydative decarboxylation of pyruvate: 2 NADH = 6 ATP
TCA: 24 ATP |
|
|
Term
| explain how glycolysis produces 8 ATP per molecule of glucose |
|
Definition
|
|
Term
| in the TAC what does oxaloacetate turn into, what does it need to do this |
|
Definition
| citrate. it needs acetyl CoA and citrate synthase |
|
|
Term
| what regulates citrate synthase |
|
Definition
| substrate/product regulation |
|
|
Term
| what are the irreversible reaction enzymes of TCA |
|
Definition
| citrate synthase, isocitrate dehydrogenase, alpha-ketogluterate dehydrogenase complex |
|
|
Term
| what is the rate limiting step of TAC |
|
Definition
| isocitrate to alpha-ketogluterate via isocitrate dehydrogenase |
|
|
Term
| in the TAC what does citrate turn into |
|
Definition
| it can go inhibit PFK-1, it can do fatty acid synthesis, or turn into isocitrate |
|
|
Term
| what catalyzes citrate into isocitrate |
|
Definition
|
|
Term
| what type of reaction is citrate to isocitrateq |
|
Definition
|
|
Term
| what does isocitrate turn into in the TAC, what does it need to do this, what are all the products |
|
Definition
| isocitrate + NAD --> NADH + CO2 + alpha-ketogluterate |
|
|
Term
| what type of reaction is isocitrate to alpha-ketogluterate |
|
Definition
| oxidation and decarboxylation |
|
|
Term
| what inhibits isocitrate dehydrogenase |
|
Definition
|
|
Term
| what stimulates isocitrate dehydrogenase |
|
Definition
|
|
Term
| what enzymes of the TCA are involved in reactions that make NADH |
|
Definition
| isocitrate DH, alpha-ketogluterate DH, malate DH |
|
|
Term
| what enzymes of the TCA are involved in reactions that make CO2 |
|
Definition
| isocitrate DH, alpha-ketogluterate DH |
|
|
Term
| what enzymes of the TCA are involved in reactions that make GTP |
|
Definition
|
|
Term
| what enzymes of the TCA are involved in reactions that make FADH2 |
|
Definition
|
|
Term
| what does alpha-ketogluterate turn into in TCA, what are the other substrates and products |
|
Definition
| CoA + NAD + alpha-ketogluterate --> NADH + CO2 + succinyl CoA |
|
|
Term
| what enzyme turns alpha-ketogluterate into succinyl CoA |
|
Definition
|
|
Term
| what inhibits alpha-ketogluterate DH |
|
Definition
|
|
Term
| what stimulates alpha-ketogluterate DH |
|
Definition
|
|
Term
| what type of reaction does alpha-ketogluterate DH catalyze |
|
Definition
| oxidative decarboxylation |
|
|
Term
| what is alpha-ketogluterate DH simillar to |
|
Definition
| pyruvate kinase DH complex |
|
|
Term
| in the TCA what does succinyl-CoA turn into, what are they other products and reactants |
|
Definition
| succinyl CoA + GDP --> GTP + succinate |
|
|
Term
| what enzyme catalyzes succinyl Coa to succinate |
|
Definition
|
|
Term
| what type of reaction does succinate thiokinase catalyze |
|
Definition
| substrate level phosphorlyation |
|
|
Term
| what does GTP from the TCA turn into |
|
Definition
|
|
Term
| in the TCA what does succinate turn into, what are the other reactants and products |
|
Definition
| succinate + FAD --> fumurate + FADH2 |
|
|
Term
| what catalyzes succinate to fumerate |
|
Definition
|
|
Term
| where is succinate DH located |
|
Definition
|
|
Term
| what does succinate DH do |
|
Definition
| succinate to fumerase. complex II of ETC |
|
|
Term
| what does fumurate turn into in the TCA, what are the other products and reactants |
|
Definition
|
|
Term
| what is malate turned into in the TCA, what are the other products and reactants |
|
Definition
| malate + NAD --> NADH and oxaloacetate |
|
|
Term
| what does arsenic poisoning do in the TCA cycle |
|
Definition
| removes lipolic acid inhibiting PDH and alpha-ketogluterate DH |
|
|
Term
| how can blocking the ETC block the TCA |
|
Definition
| decreasing O2 for example, causes build up of products and inhibits TCA |
|
|
Term
| what does a niacin or thiamine deficiency cause |
|
Definition
| decreases the activity of PDH and alpha-ketogluterate DH, this leads to CNS problems because the brain needs glucose to survive |
|
|
Term
| what is another name for wernickle korsakoff syndrome |
|
Definition
| encephalopathy psycosis syndrome |
|
|
Term
| what occurs in wernickle korsakoff syndrome |
|
Definition
| decreaded thiamine causes decreased activity of PDH and alpha-ketogluterate DH |
|
|
Term
| who commonly has wernickle korsakoff syndrome |
|
Definition
|
|
Term
| what are the names of diseases with a PDH deficiency |
|
Definition
| leign syndrome, subacute necrotizing encephalomelopathy |
|
|
Term
| what occurs in a PDH deficiency |
|
Definition
| pyruvate cannot go into the TCA cycle so it goes to making lactic acid, leads do chronic lactic acid acidosis |
|
|
Term
| what are the symptoms of PDh deficiency |
|
Definition
| neuro degeneration, muscle spasticity, early death |
|
|
Term
| What is the general overall story of ETC |
|
Definition
| Glucose is oxidized to CO2 and water coupled to the transfer of electrons of coenzymes FAD and NAD to yield energy as NADH and FADH2. They donate electrons to electrons carriers which makes energy for a pump that creates a gradient that is coupled to ATP production |
|
|
Term
| What is an alternative route for the energy made from ETC, other than ATP production |
|
Definition
| Ancillary reactions (Ca transport in mitochondria making heat) |
|
|
Term
|
Definition
|
|
Term
| At what point does the ETC turn off |
|
Definition
| It only turns off when oxygen isn't present, it is Always running |
|
|
Term
| What is the outer membrane permeable to |
|
Definition
| Most ions and small molecules |
|
|
Term
| What is the inner membrane permeable to |
|
Definition
| Few ions or molecule.s need carriers |
|
|
Term
| What is the inner mitochondrial membrane made of |
|
Definition
| Lots of proteins (50% are ETC proteins), very convoluted forming cristae to increase surface area |
|
|
Term
| What is the mitochondrial matrix made of |
|
Definition
| 50% protein, gel like, enzymes for oxidating pyruvate amino acids, fatty acids beta-oxidation, and TCA. NAD, FAD, ADP, Pi. Mitochondrial DNA and replication / expression tools. |
|
|
Term
| What drives transfer of electrons in ETC |
|
Definition
| NADH is a good electron donor and oxygen a good acceptor |
|
|
Term
| What happens to the strength of the donors as you go through the etc |
|
Definition
| Each donor is weaker and acceptors are stronger |
|
|
Term
| What is the common intermediate between oxidation and oxidative phosphorylation |
|
Definition
|
|
Term
| Where does the NADH and H come form for etc |
|
Definition
|
|
Term
| Where does NADH enter into the etc chain |
|
Definition
|
|
Term
| What is another name for complex 1 |
|
Definition
|
|
Term
| What occurs in NADH dehydrogenase |
|
Definition
| FMN accepts 2H / 2e- making FMNH2 assisted by the Fe/S center |
|
|
Term
| Where does FADH2 enter the etc |
|
Definition
| It sends 2H / 2e to cytochrome c |
|
|
Term
|
Definition
| A non membrane bound lipid electron carrier |
|
|
Term
| Where does coenzyme q take electrons to |
|
Definition
| Complex 3: cytochrome BC1 |
|
|
Term
| What picks up electrons from cytochrome bc1 |
|
Definition
|
|
Term
| Where does cytochrome c take electrons do |
|
Definition
| Cytochrome c oxidase, complex 4 |
|
|
Term
| What does cytochrome c oxidase do |
|
Definition
| Uses Fe and Cu to help use 2H / 2e to reduce oxygen to water |
|
|
Term
| What complexes are not membrane bound in etc |
|
Definition
| Cytochrome c and coenzyme q, the electrons carris |
|
|
Term
| What complexes pump protons out in their electron transport exchange |
|
Definition
|
|
Term
| In regard to the gradient, what is the outside of the mitochondrial membrane like |
|
Definition
|
|
Term
| In regard to the gradient, what is the inside of the mitochondrial membrane like |
|
Definition
|
|
Term
| Describe the composition and role of a cytochrome |
|
Definition
| Has heme, involved in electron transport, reversible oxidized or reduced Fe |
|
|
Term
| Where is the Fo subunit of complex 5 located |
|
Definition
|
|
Term
| Explain the role of the F1 subunit of complex 5 |
|
Definition
| Rotation of the unit is driven by the gradient, this allows ADP and P to make ATP |
|
|
Term
| What is another name for complex 5 |
|
Definition
|
|
Term
| In general, what do etc inhibitors do |
|
Definition
| Prevent flow of electrons so NADH builds up leading to TCA inhibition, this causes anaerobic glycolysis, increasing lactic acid and decreasing oxygen consumption, aerobic tissues are most effected |
|
|
Term
| What does Amytal do, what is it classified as |
|
Definition
| Barbiturate that stops complex 1 of etc |
|
|
Term
|
Definition
|
|
Term
|
Definition
| Insecticide,pesticide, piscicide |
|
|
Term
|
Definition
|
|
Term
| What is antimycin found in |
|
Definition
|
|
Term
|
Definition
|
|
Term
|
Definition
| Irreversibly binds complex 4 in etc, binds iron tight in heme |
|
|
Term
| Why might someone be exposed to cyanide |
|
Definition
| House if re, industrial fire, burning polyurethane |
|
|
Term
| what does CN- bind to in ETC |
|
Definition
| Fe3+ in heme of complex 4 |
|
|
Term
|
Definition
| inhibits complex 4 reversibly |
|
|
Term
| what does sodium azide bind to in ETC |
|
Definition
| Fe3+ in cytochromes of complex 4 |
|
|
Term
| where is sodium azide found |
|
Definition
| propellent in airbags, explosives, lab as anti microbial preservitive in sera or other solutions |
|
|
Term
|
Definition
| binds to complex 5 in ETC closing proton channel leading back to matrix, stops ATP synthesis so also ETC |
|
|
Term
| where is oligomycin found |
|
Definition
| tool to study electron transport in lab |
|
|
Term
| where are coupling proteinsfound |
|
Definition
| inner mitochondrial membrane |
|
|
Term
| what do coupling proteins do |
|
Definition
| allow protons to flow back into matrix without going through complex 5, does not stop ETC but does not make ATP, energy is released as heat |
|
|
Term
| what are examples of coupling proteins |
|
Definition
| UPC 1 (thermogenin), synthetic uncouplers, salicylic acid |
|
|
Term
|
Definition
|
|
Term
| what are synthetic uncouplers |
|
Definition
| non-proteins that increase permability of inner mitochondrial membrane to protons which uncouple ETC from ATP production |
|
|
Term
| what is an example of a synthetic uncoupler, what does it cause |
|
Definition
| 2,4-dinitropherol: weight loss drug, overdose causes fatal hyperthermia |
|
|
Term
| what does salicylic acid do |
|
Definition
| uncouples ETC from ATP production, overdose leads to fever and sweating |
|
|
Term
| where is salicylic acid found |
|
Definition
|
|
Term
| what is a reactive O2 species formed by |
|
Definition
| oxygen improperly turning into water that the end of the ETC |
|
|
Term
| what are the reactive O2 species |
|
Definition
| superodixe (O2-), H2O2, hydroxyl radicals (OH) |
|
|
Term
| what do reactive O2 species do |
|
Definition
| damage proteins, lipids, DNA, RNA in mitochondria |
|
|
Term
| other than the fact that they damage sruff, why are reactive O2 species a problem |
|
Definition
| they mess up the ETC which increases the amount of reactive O2 species making a bad circle of life |
|
|
Term
| how does the body normally combat reactive O2 species |
|
Definition
|
|
Term
| what are the natural enzymes the body uses to combat reactive O2 species |
|
Definition
| lipid soluble vitamins in membrane (antioxident vitamins, vitamin E), water soluble vitamins in cytosol (vitamin C), superoxide dismutase, catalyase, gltathione peroxidase |
|
|
Term
| what is a reprefusion injury |
|
Definition
| decreased O2 > decreased ATP and NADH prodiction. then O2 is suddenly introducd. ETC activity is too much > reactive oxygen species produced |
|
|
Term
| where do the proteins from oxidative phosphorlyation come from |
|
Definition
| 13/120 are on mitochondrial DNA, the rest are transported into the mitochondria from the nucleus |
|
|
Term
| why does mitochondrial DNA have a higher mutation rate |
|
Definition
| reactive oxygen species generation |
|
|
Term
| what do mutations in mitochondrial DNA cause |
|
Definition
| oxidative phosphorlyation defects which hurts aerobic tissues causing neuropathies and myopthies |
|
|
Term
| what are examples of mitochondrial DNA mutations |
|
Definition
| LHON, MERRF, mitochondrial encephalomyopathy, lactic acidosis, stroke like episodes, leigh syndrome |
|
|
Term
| what is the role of the mitochondria in apoptosis |
|
Definition
| may be initiated through intrinsic (mitochondria mediated) path by outer pores of the outer mitochondrial membrane allowing cytochrome C into the cytosol, cytochrome c activates proapoptotic factors to activate proteolytic enzymes (capsases). capsases cleave key proteins leading to morphologicl and biochemical changes of apoptosis |
|
|
Term
| what happens in Fe deficient anemia |
|
Definition
| Fe is in the ETC so a defect would lead to faulty ETC and tiredness |
|
|
Term
| where does gluconeogensis occur |
|
Definition
| the liver, unless there has been prolonged fasting then the kidney helps |
|
|
Term
| how long can glycogen storage in the liver sustain you |
|
Definition
|
|
Term
| once the liver glycogen storage is depeleted, what kicks in to keep you going |
|
Definition
|
|
Term
| what is the challenge for the body in completing gluconeogenesis |
|
Definition
| need to reverse the three irreversible steps in glycolysis |
|
|
Term
| what are the substrates for gluconeogenesis |
|
Definition
| glycerol, lactate, amino acids |
|
|
Term
| how is glycerol involved in gluconeogenesis |
|
Definition
| adipocytes release FA by hydrolyzing TAG which also releases glycerol. it is converted to DHAP which can go into gluconeogenesis skipping the pyruvate challenge reaction |
|
|
Term
| why can we just keep using glycerol / gluconeogenesis for energy |
|
Definition
| there itsnt enough to give significant energy |
|
|
Term
| where is lactate produced |
|
Definition
| RBC and exercising skeletal muscle |
|
|
Term
| what can convert lactate to pyruvate |
|
Definition
|
|
Term
|
Definition
| lactate made in muscle travels to the liver. gluconeogenesis turns into into glucose, glucose travels to the muscle and is turned into lactate. rinse and repeat |
|
|
Term
| where are amino acids derived from |
|
Definition
|
|
Term
| what is the major amino acid that energy comes from |
|
Definition
|
|
Term
| what needs to happen to amino acids before they can be used for energy |
|
Definition
|
|
Term
| how many amino acids can be used for energy |
|
Definition
|
|
Term
| how are amino acids used for energy |
|
Definition
| they become TCA cycle intermediates which can yeild oxaloacetate which can turn into PEP which can be used in gluconeogenesis |
|
|
Term
| how is acetyl CoA used in glucoenogenesis |
|
Definition
| it isnt, you cannot convert acetyl CoA into pyruvate, PDH is irreversible |
|
|
Term
| how can actyl CoA provide energy if it canot go into gluconeogenesis |
|
Definition
| fatty acid oxidation gives the liver energy to complete gluconeogenesis |
|
|
Term
| what is the first step of gluconeogenesis, what catalyzes it |
|
Definition
| pyruvate to oxaloacetate via pyruvate carboxylase and biotin coenzyme |
|
|
Term
| where does the first step of gluconeogenesis take place |
|
Definition
|
|
Term
| where is pyruvate carboxylase located |
|
Definition
| in cells that dont do gluconeogenesis well (muscle) and need to replace TCA intermediates instead |
|
|
Term
| once produced via gluconeogenesis, what is the fate of oxaloacetate |
|
Definition
| TCA intermediate or further gluconeogenesis |
|
|
Term
|
Definition
| bind CO2 in pyruvate carboxylase |
|
|
Term
| what does pyruvate carboxykinase need to work |
|
Definition
|
|
Term
| what is thee malate shuttle |
|
Definition
| oxaloacetate is converted to malate and back to OAA to get through the mitochondrial membrane in gluconeogenesis |
|
|
Term
| what does OAA turn into if going through gluconeogenesis, what enzyme does it |
|
Definition
| malate via mitochondrial malate dehydrogenase |
|
|
Term
| after going through the membrane what does malate turn into in gluconeogenesis, using what enzyme? |
|
Definition
| OAA via cytosolic malate dehydrogenase |
|
|
Term
| after getting through the mitochondrial membrane, what does OAA turn into, what is needed for this reaction to occur |
|
Definition
|
|
Term
| what enzyme turns OAA into PEP |
|
Definition
|
|
Term
| in glycolysis PEP is turned into pyruvate, why does this not just happen after we reverse it in gluconeogenesis |
|
Definition
| because the enzyme that converts PEP to pyruvate, pyruvate kinase, is inhibited by glycogen |
|
|
Term
| what stimulates pyruvate carboxykinase |
|
Definition
|
|
Term
| what enzyme converts fructose-1,6-bisphosphate into fructose-6-phosphate |
|
Definition
| fructose-1,6-bisphosphatase |
|
|
Term
| what activates fructose-1,6-bisphosphatase, what does this indicate physiologically |
|
Definition
| ATP, the liver needs energy |
|
|
Term
| what inhibits fructose-1,6-bisphosphatase |
|
Definition
| AMP, fructose-2,6-bisphosphate |
|
|
Term
| explain how fructose-2,6-bisphosphate inhibits fructose-1,6-bisphosphatase |
|
Definition
| fructose-2,6-bisphosphate gets low glycolysis will shut off and gluconeogenesis will be able to turn on |
|
|
Term
| how does glycogen affect fructose-1,6-bisphosphatase |
|
Definition
| it inhibits PFK-2 which decreases fructose-2,6-bisphosphate and increases glucoenogenesis and decreases glycolysis |
|
|
Term
| what turns glucose-6-phosphate into glucose |
|
Definition
|
|
Term
| what is used in glyconeolysis to yield free glucose |
|
Definition
|
|
Term
| once productd via gluconeogenesis, where does glucose go |
|
Definition
| out of the liver into the blood to supply tissues |
|
|
Term
| what is the cause of von gierke disease |
|
Definition
| glucose-6-phosphatase deficience |
|
|
Term
| how does substrate avability regulate gluconeogenesis: muscle |
|
Definition
| muscle breaks down into amino acid and its sent to the liver and gluconeogenesis is stimulated by aa. |
|
|
Term
| how does substrate avability regulate gluconeogenesis: fatty acids |
|
Definition
| fatty acid oxidation yields ATP and NADH which go to the liver. this stimulates gluconeogenesis |
|
|
Term
| how do the reversible reactions regulate gluconeogenesis |
|
Definition
| direction of the reactions depend on substrate vs product regulation |
|
|
Term
| how does acetyl CoA regulate gluconeogenesis |
|
Definition
| it allosterically activates pyruvate carboxykinase. if it builds up there isnt enough OAA for it to combine with to make citrate so it activates gluconeogenesis. it inhibits PDH so pyruvate is used for gluconeogenesis so more acetyl CoA isnt made. |
|
|
Term
| how does AMP regulate gluconeogenesis |
|
Definition
| allosterically inhibits fructose-1,6-bisphosphate, it activates PRK 1 and makes sure enzymes are muturally exclusive |
|
|
Term
| why is glycogen used in metabolism |
|
Definition
| dietary glucose is unreliable, gluconeogenesis is slow so their is a gap it fills when glucose isnt taken in |
|
|
Term
| what parts of the body release sugar |
|
Definition
|
|
Term
| why isnt sugar released from the muscle |
|
Definition
| it is degraded when ecercising |
|
|
Term
| where is glycogen mainly stored |
|
Definition
| skeletal muscle and liver |
|
|
Term
|
Definition
| skeletal muscle, liver, kidney |
|
|
Term
| what is the only organ that does not use glycogen for itself |
|
Definition
|
|
Term
| how is glycogen involved in weight gain |
|
Definition
| it holds water which increases its weight |
|
|
Term
| describe the structure of glycogen |
|
Definition
| branched chain of a-D-glucose with a1-4 and a1-6 bonds that make large granules |
|
|
Term
| where are the enzymes to make or break glycogen located |
|
Definition
| associated with the glycogen granules |
|
|
Term
| give a general explination of how glycogen is made |
|
Definition
| glucose-1-p + UDP -> UDP glucose, UDP glucose adds onto glycogenin one at a time, every 8 residues there is a branch made |
|
|
Term
| what catalizes glucose-1-phosphate + UDP -> UDP glucose |
|
Definition
| UDP glucose phosphorlyase |
|
|
Term
| what catalizes the first 4 residues being put on glycogenin protein |
|
Definition
|
|
Term
| what catalizes more than 4 residies being added to glycogenin protein |
|
Definition
|
|
Term
| what type of bonds does glycogen synthase make |
|
Definition
|
|
Term
| why does glycogen have branches |
|
Definition
| to give more ends for synthesis that glucose can be liberated from |
|
|
Term
| how is a glycogen branch made |
|
Definition
| glycogen synthase puts on more than 8 branches, 6 are cleaved off and moved down the molecule by branching enzyme |
|
|
Term
| what type of bonds do branching enzyme make |
|
Definition
|
|
Term
| what is another name for branching enzyme |
|
Definition
|
|
Term
| what does glycogen phosphorlyase do |
|
Definition
| cleave a1-4 bonds of glycogen yielding glucose 1-phosphate |
|
|
Term
| what is the rate limiting step in glycogen degredation |
|
Definition
|
|
Term
| why and where does glycogen phosphorlyase stop cleaving (other than hormones and such) |
|
Definition
| it reaches steric hinderance near a branch approx 4 residues from it |
|
|
Term
| how are branches removed from glycogen |
|
Definition
| debranching enzyme uses 4/4 transferase and 1/6 glucosidase activity |
|
|
Term
| what does glycogen phosphrlyase need to work |
|
Definition
|
|
Term
|
Definition
|
|
Term
| what is the 4/4 transferase activity |
|
Definition
| debranching enzyme removes 3 of the 4 glucose and attaches them to another branch making a longer chain so glycogen phosphorlyase can act on it |
|
|
Term
| what is the 1/6 glucosidase activity |
|
Definition
| debranching enzyme cleaves the branch point of glucogen, yielding free glucose |
|
|
Term
| what turns glucose-1-phosphate into glucose-6-phosphate |
|
Definition
|
|
Term
| what turns glucose-6-phosphate into glucose |
|
Definition
|
|
Term
| what is an alternative way for glycogen to be broken down |
|
Definition
| lysosomal alpha glucosidase in the lysosome |
|
|
Term
| explain how, after degrading glycogen, it can be used for energy |
|
Definition
| the product of the degredation is glucose-1-phosphate, it can be converted to glucose-6-phosphate and into glucose |
|
|
Term
| what regulates glycogen metabolis, how |
|
Definition
| glycogen synthase and phosphorlyase regulators, they have tissue specific isoenzymes |
|
|
Term
| what activates glycogen synthase in the liver |
|
Definition
| insulin, glucose-6-phosphate |
|
|
Term
| what inhibits glycogen synthase in the liver |
|
Definition
|
|
Term
| what activates glycogen synthase in the muscle |
|
Definition
|
|
Term
| what inhibits glycogen synthase in the muscle |
|
Definition
|
|
Term
| what activates glycogen phosphorlyase in the liver |
|
Definition
|
|
Term
| what inhibits glycogen phosphorlyase in the liver |
|
Definition
|
|
Term
| what activates glycogen phosphorlyase in the muscle |
|
Definition
|
|
Term
| what inhibits glycogen phosphorlyase in the muscle |
|
Definition
|
|
Term
| what causes von gierke's disease |
|
Definition
| glucose-6-phosphate deficiency |
|
|
Term
| what does von greike's cause |
|
Definition
| severe fastin hypoglycemia, lactic acidosis, hepatomeagly, hyperlipidemia, hyperuricemia, short stature due to growth retardation |
|
|
Term
| what does sever fasting hypoglycemia cause in von gierke's disease |
|
Definition
| cannot release glucose from liver from gluconeogenesis or glycogenolysis |
|
|
Term
| what does lactic acidoses cause in von gierke's disease |
|
Definition
| glucose-6-phosphate builds up an stops at gluconeogenesis, PDH is inhibited, lactate production is favored, lactate from RBC does not go to gluconeogenesis |
|
|
Term
| what does hepatomeagly cause in von gierke's disease |
|
Definition
| glycoen metabolites accumulate in liver and FA synthesis is favored, the liver swells because glycogen likes water |
|
|
Term
| what does hyperlipidemia cause in von gierke's disease |
|
Definition
| increased fa synthesis in liver due to deraged glucose in the liver |
|
|
Term
| what does hyperuricemia cause in von gierke's disease |
|
Definition
| glucose-6-phosphate build up tieing up cellular phosphate leading to turn over of nucleotides |
|
|
Term
| what causes pompe disease |
|
Definition
| lysosomal a1-4 glucosidase deficiency, hurts lysosomal glycogen degredation |
|
|
Term
| what are the symptoms of pompe disease |
|
Definition
| like other lysosomal storage disease, accumulation of the compound that cannot be broken down |
|
|
Term
|
Definition
| debranching enzyme deficiency |
|
|
Term
| what are the symptoms of cori disease |
|
Definition
| mild hypoglycemia, liver enlargement, short outer branches of glycogen |
|
|
Term
| why is there mild hypoglycemia in cori disease |
|
Definition
| glucose is only released from glycogen until a branch is reached |
|
|
Term
| why is there liver enlargement in cori disease |
|
Definition
| accumulation of glycogen remains |
|
|
Term
| what is deficient in anderson disease |
|
Definition
|
|
Term
| what are the symptoms of andersen disease |
|
Definition
| infantile hypotonia, cirrhosis, early death |
|
|
Term
| what is infantile hypotonia |
|
Definition
| few branches in glycogen so few ends release glycogen for muscle contraction |
|
|
Term
|
Definition
| linear glycogen is much less soluble and percipitates, damaging liver cells |
|
|
Term
| why is there early death in andersen disease |
|
Definition
| liver and heart are severly affected by percipitated glycogen |
|
|
Term
| what is deficnent in mcCardle disease |
|
Definition
| muscle glycogen phosphorlyase |
|
|
Term
| what are the symptoms of McCardle disease |
|
Definition
| muscle cramps, cannot release glycogen for muscle contraction, myoglobinuria |
|
|
Term
|
Definition
| destruction of some some muscle cells due to exercise induced lack of ATP |
|
|
Term
| what is wrong in Hers disease |
|
Definition
| liver gluycogen phosphorlyase deficneicy |
|
|
Term
| what are the symptoms of Hers disease |
|
Definition
| mild fasting mypoglycemia, hepatomeagly |
|
|
Term
| what occurs in mild fasting hypoglycemia |
|
Definition
| no glucose from glycogen but gluconeogenesis still is function |
|
|
Term
| why does hepatomeagly occur in glycogen storage diseases |
|
Definition
| excess build up of glycogen in the liver |
|
|
Term
| describe the solubility of lipids |
|
Definition
| hydrophobic, non-polar, water insoluble |
|
|
Term
| what does the solubility of lipids cause the molecules to do |
|
Definition
|
|
Term
| how can you dissolve lipids |
|
Definition
|
|
Term
| what are the major functions of lipids |
|
Definition
| provide hydrophobic barriers for cell membranes and subcellular compartments, source of energy |
|
|
Term
| what are the minor functions of lipids |
|
Definition
| coenzyme or regulatory, regulating homeostasis |
|
|
Term
| what lipids have coenzyme functions |
|
Definition
|
|
Term
| what lipids have functions in regulation of homeostasis |
|
Definition
|
|
Term
| what has increased intake in saturated FA and cholesterol been shown to cause risk of, what form of fat does not |
|
Definition
|
|
Term
| what is the optimal pH for acid lipase |
|
Definition
|
|
Term
| what are the enzymes in the stomach that digest lipids |
|
Definition
| acid lipase, lingual lipase, gastric lipase |
|
|
Term
| what is an example of something that acid lipase digests |
|
Definition
|
|
Term
| what enzyme is important in neonates for milk digestion |
|
Definition
|
|
Term
| what does acid lipase target |
|
Definition
| short and medium chain FA (<12 C) |
|
|
Term
| where is lingual lipase secreted |
|
Definition
|
|
Term
| where is gastric lipase secreted |
|
Definition
|
|
Term
| in general what processes emulsify dietary lipids |
|
Definition
| complimentary actions: mechanical agitation and secretion of bile salts |
|
|
Term
| what causes mechanical digestion, what does it accomplish |
|
Definition
| peristalsis increases surface area of lipid droplets |
|
|
Term
|
Definition
| make smaller particles, detergent stablizes particles so they dont stick back together |
|
|
Term
| where are bile salts made |
|
Definition
|
|
Term
| where are bile salts stored |
|
Definition
|
|
Term
| where are bile salts secreted |
|
Definition
|
|
Term
| what do proteolytic enzymes in the small intestines digest |
|
Definition
| TAG, cholesterol esters, phospholipids |
|
|
Term
| what digests TAGs in the small intestine |
|
Definition
|
|
Term
| what does pancreatic lipase cleave TAGs into |
|
Definition
| 2-monoacylglycerol and FA |
|
|
Term
| what percent of the pancreatic secretion is pancreatic lipase |
|
Definition
|
|
Term
| what does pancreatic lipase need for it to work |
|
Definition
|
|
Term
|
Definition
| binds pancreatic lipase at a 1:1 ratio moving it to aqueous barrer where inhibitor bile acids are present so enzymes can get to the TAG |
|
|
Term
| ih what form is most dietary cholesterol |
|
Definition
|
|
Term
| what digests cholesterol esters in the small intestines |
|
Definition
| pancreatic cholesterol esterase |
|
|
Term
| what does pancreatic cholesterol esterase turn cholesterol esters into |
|
Definition
|
|
Term
| what activates pancreatic cholesterol esterase |
|
Definition
|
|
Term
| in general how are phosphilipids digested |
|
Definition
|
|
Term
| what is the process of phospholipid digestion |
|
Definition
1. phospholipase A2 removes FA from position 2 makes lysophorpholipid and FA
2. lisophospholipase removes FA from position one making glycerophosphoryl and FA
3. glycerylphosphorly base is absorbed, digested, or excreted |
|
|
Term
| what conteols pancreatic enzymes |
|
Definition
|
|
Term
| what is CCK secreted from |
|
Definition
| mucosal cells of lower duodenum and jejunum |
|
|
Term
| what is CCK released in response to |
|
Definition
| lipids, partially digested proteins |
|
|
Term
|
Definition
| contraction of gall bladder releasing bile salts, phospholipids, free cholesterol. exocrine cells of pancreas to secrete hydrolytic enzymes, decreases gastric motility, reducing release of gastric contents into the small intestines |
|
|
Term
| what type of hormone is secretin |
|
Definition
|
|
Term
|
Definition
|
|
Term
| what does secretin respond to |
|
Definition
| low pH of chime entering intestine |
|
|
Term
|
Definition
| bicarbonate release from liver and pancreas, gives appropirate pH for enzyme function |
|
|
Term
| after being digested what happens to the lipid particles |
|
Definition
| they form into micelles along with soluble vitamins and bile salts, micelles go to brush border of the membrane of enterocytes and are absorbed |
|
|
Term
| what does lipid digestion in the small intestines generate in the end |
|
Definition
| Fa, cholesterol, 2-monoacylglycerol |
|
|
Term
| how do long chain fatty acids get absorbed into brush border |
|
Definition
| broken down and put into micelles |
|
|
Term
| how do short and medium chain fatty acids get absorbed into brush border |
|
Definition
| they can go right through |
|
|
Term
| once in the enterocytes, what happens to long chain FA |
|
Definition
| converted to acyl-Coa at the ER |
|
|
Term
| once in the enterocytes, what happens to 2-monoacylglycerol, what helps |
|
Definition
| TAG synthase sequentially adds FA using acyltransferase activities |
|
|
Term
| once in the enterocytes, what happens to lysophospholipids |
|
Definition
| reacylated by acyltransferases to form phospholipids |
|
|
Term
| once in the enterocytes, what happens to cholesterol |
|
Definition
|
|
Term
| once in the enterocytes, what happens to short and medium chain FA |
|
Definition
| not activated, released into portal circulation and carried by serum albumin |
|
|
Term
| what needs to happen to TAG and cholesterol esters before the can leave the enterocyte |
|
Definition
| need to be packaged into chylomicrons |
|
|
Term
| what is a chylomicron made of |
|
Definition
| TAG and cholesterol esters with a layer of phospholipids, cholesterol, and Apo B48 around the outside |
|
|
Term
| where are chylomicrons made |
|
Definition
|
|
Term
| once made, what happens to the chylomicron |
|
Definition
| exocytosed into the lacteal making the lumph chyle |
|
|
Term
|
Definition
| lymph capillary in the SI villi |
|
|
Term
| what happens when the chylomicron makes chylo |
|
Definition
| it is passed into the lymphatic system to thoracic duct to left subclavian then blood |
|
|
Term
| what happens to a chylomicron once it reaches a tissue |
|
Definition
| lipoprotein lipase degrades TAG into FA and glycerol |
|
|
Term
| where is lipoprotein lipase secreted |
|
Definition
| mostly muscle and adipose but also heart, lung, kidney, liver |
|
|
Term
| what does lipoprotein lipase associate with |
|
Definition
| lumen endothelial cells of capillary bed |
|
|
Term
| what happens for FA in circulation |
|
Definition
| they are usually taken up immediatly by adjacent muscle or adipose if they dont, they will circulate on albumin until they are |
|
|
Term
| what happens to glycerol after being released into blood |
|
Definition
| it is taken up by liver and used to make glycerol-3-phosphate for glycolysis or gluconeogenesis |
|
|
Term
| what remains after the contents of a chylomicron are used by the tissues |
|
Definition
| phospholipids, cholesterol esters, apolipoproteins, fat soluble vitamins, TAG |
|
|
Term
| what happens to chylomicron reamins |
|
Definition
| interacti with liver cells and are endocytosed |
|
|
Term
| what happens to nitrogenous bases and phospholipids associated with FA transport to tissues |
|
Definition
|
|
Term
| how can you tell there is lipid malabsorption |
|
Definition
| fat soluble vitamins and essential fatty acids in excretion |
|
|
Term
| what diseases involve lipid malabsorption |
|
Definition
| cystic fibrosis and shortened bowl |
|
|
Term
| what type of inheritence is cystic fibrosis |
|
Definition
|
|
Term
| what is mutated in cystic fibrosis, what does this cause |
|
Definition
| CL ion channels CFTR that hydrate mucous in secretory ducts of pancreas mutations lead to viscous mucous tha blocks pancreatic enzymes needed for lipid digestion in si |
|
|
Term
| what are the symptoms, other than lipid malabsorption of cystic fibrosis related to lipids |
|
Definition
| delayed growth, energy deficient |
|
|
Term
| how is cystic fibrosis treated |
|
Definition
| with enzyme replacement and fat soluble vitamin supplements |
|
|
Term
| where and when are free FA most concentrated |
|
Definition
|
|
Term
|
Definition
|
|
Term
| where do free FA come from |
|
Definition
| TAG in adipose or circulating lipoproteins |
|
|
Term
| where can free FA be consumed |
|
Definition
|
|
Term
| where are free FA in low concentrations |
|
Definition
|
|
Term
| what are the functions of free fatty acids |
|
Definition
| membrane lipids (phospholipids, glycolipids), stored in adipose, major energy reseve |
|
|
Term
| what form at 90% of fatty acids in |
|
Definition
|
|
Term
| what part of a fatty acid is hydrophobic |
|
Definition
|
|
Term
| what part of a fatty acid is hydrophillic, why |
|
Definition
| carboxyl group, at physological pH it is COO- |
|
|
Term
| due to the carbon end and the COO- end of fatty acids the molecule is considered to be... |
|
Definition
|
|
Term
| when the fatty acid is longer what does this do to the solubility |
|
Definition
| more hydrophobic, must be carried with a protein for transport, decreasing fluidity |
|
|
Term
| what does it mean if a fatty acid is saturated |
|
Definition
|
|
Term
| what does it mean if a fatty acid is unsaturated |
|
Definition
| it has one or more double bonds |
|
|
Term
| what conformation and pattern are double bonds in an unsaturated fatty acid |
|
Definition
| cis spaced every # carbons |
|
|
Term
| what do double bonds do to the physical properities of the fatty acid |
|
Definition
| reduce Tm and increase fluidity |
|
|
Term
| when naming what carbon do you begin numbering with |
|
Definition
|
|
Term
| how do you name a fatty acid |
|
Definition
| number of carbons : number of double bonds (location of double bonds) |
|
|
Term
| where is the alpha carbon located |
|
Definition
| next to the carbonyl, carbon 2 |
|
|
Term
| where is the beta carbon located |
|
Definition
|
|
Term
| where is the gamma carbon located |
|
Definition
|
|
Term
| where is the omega carbon located |
|
Definition
|
|
Term
| what is an alternativie way of naming fatty acids |
|
Definition
| name from the omega carbon instead of carbonyl |
|
|
Term
| what does it mean if a fatty acid is essential |
|
Definition
|
|
Term
| what are the essential fatty acids |
|
Definition
| alpha-linolenic acid, linoleic acid, arachidonic acid |
|
|
Term
| what is the precursor for omega 3 fatty acid |
|
Definition
|
|
Term
| what is the function of omega 3 fatty acid |
|
Definition
|
|
Term
| what is the precursor for omega 6 fatty acid |
|
Definition
|
|
Term
| what is the function of omega 6 fatty acid |
|
Definition
|
|
Term
| what is the largest source of fatty acids in people |
|
Definition
|
|
Term
| what is the function o f arachadonic acid |
|
Definition
| becomes essential if linoleic acid is deficient in the diet |
|
|
Term
| what happens to excess dietary protein and carbs |
|
Definition
|
|
Term
| where are the common places of de novo synthesis |
|
Definition
| liver and lactating mammary glands, some in adipose |
|
|
Term
| where are fatty acids made |
|
Definition
|
|
Term
| what is the carbon source for fatty acid production |
|
Definition
|
|
Term
| where does energy for fatty acid production come from |
|
Definition
|
|
Term
| where does reduction power for fatty acids production come from |
|
Definition
|
|
Term
| how does the mitochondria make acetyl CoA |
|
Definition
| oxidizing pyruvate, beta-oxidation of long cahin CoA, catabolism of ketone bodies and some amino acids |
|
|
Term
| what causes FA to not be stored during FA synthesis |
|
Definition
| isocitrate dehydrogenase is inhibited by high ATP levels |
|
|
Term
| what is the first reaction in FA synthesis |
|
Definition
| citrate synthase turns acetyl CoA and OAA into citrate |
|
|
Term
| why is acetyl CoA turned into citrate in FA synthesis |
|
Definition
| because acetyl CoA cannot get through the mitochondrial membrane |
|
|
Term
| what happens to citrate after it crosses the membrane in fatty acid synthesis |
|
Definition
| ATP-citrate lyase cleaves it into acetyl-CoA and OAA |
|
|
Term
| after citrate gets turned into acetyl CoA what happens to it |
|
Definition
| ATP citrate lyase cleaves citrate into carboxylate acetyl using CO2 and ATP |
|
|
Term
| what causes short term activation of acetyl CoA carboxylase |
|
Definition
|
|
Term
| what causes short term deactivation of acetyl CoA carboxylase |
|
Definition
| long chain FA, AMP activated protein kinase |
|
|
Term
| what activates AMP activated protein kinase |
|
Definition
|
|
Term
| what inhibits AMP activated protein kinase |
|
Definition
| glucagon and epinepherine |
|
|
Term
| what is AMP activated protein kinase dependent on |
|
Definition
|
|
Term
| what stimulates acetyl CoA carboxylase long term |
|
Definition
| prolonged high calorie or carbohydrate diet |
|
|
Term
| wat inhibits acetyl CoA carboxylase long term |
|
Definition
|
|
Term
| what is the function of turning acetyl CoA into caeboxylate acetyl |
|
Definition
| provides energy or carbon to carbon condensations in elongation of the FA with the help of decarboxylation |
|
|
Term
| what is the rate limiting step of fatty acid synthesis |
|
Definition
|
|
Term
| how many things does fatty acid synthase do |
|
Definition
|
|
Term
| what are the domains of fatty acid synthase |
|
Definition
| domain for binding 4-phosphopantetheine, acyl carrier protein domain |
|
|
Term
| what occurs at the domain for binding 4-phosphopantetheine |
|
Definition
| it functions as an acyl carrier protein with acyl units on its terminal thiol group during fatty acid synthesis |
|
|
Term
| what happens at the acyl carrier protein domain |
|
Definition
| acetyl is transferred to it to CYS, malonate is transferred from malonyl CoA to it, acetyl CoA carboxylase adds CO2 to it |
|
|
Term
| what drives reaction between acyl CIS and malonyl CoA on acyl carrier protein |
|
Definition
| CO2 added by acetyl CoA carboxylase |
|
|
Term
| what remains attached to acyl carrier protein domain, what is produced |
|
Definition
| 4 carbon product is attached, 3-ketoacyl is made |
|
|
Term
| what happens for 3-ketoacyl |
|
Definition
| converted to saturated acyl by two reductions using NADPH and dehydration making alcohol |
|
|
Term
| once an alcohol is made in fatty acid synthesis, how is it modified |
|
Definition
| water is removed, double bonds form between carbon 2 and 3, butyryl is made and three terminal carbons are attached to acyl carrier protein by fatty acid synthase |
|
|
Term
| how is a fatty acid elongated |
|
Definition
| repeat actions of fatty acid synthase at transfer of butyryl to CiS at fatty acid |
|
|
Term
| how many carbons are added a round of elongation |
|
Definition
|
|
Term
| how many times can a fatty acid be elongated |
|
Definition
|
|
Term
| what is the product of the actions of fatty acid synthase |
|
Definition
|
|
Term
| what happens to palmitoyl-S-CoA |
|
Definition
| palmitoyl thioesterase cleaves thioester bond making palmitate (16:0) |
|
|
Term
| what happens if we need palmitate to be further elongated |
|
Definition
| palmitate goes to the smoother ER and 2 carbon units are added from malonyl CoA and reduction of NADPH, special enzymes are used for each addition |
|
|
Term
| where in the body are there very long chain fatty acids |
|
Definition
|
|
Term
| how are fatty acids desaturated |
|
Definition
| smoother ER has desaturases that desaturate long chain FA, introducing CIS usually between C9 and C10 |
|
|
Term
| how is fatty acid stored as TAG |
|
Definition
| esterified via carbonyl group to carbons of glycerol, acid loses its charge forming neutral TAG |
|
|
Term
| describe the structure of TAG, what is on each carbon |
|
Definition
carbon 1 is saturated FA
carbon 2 is unsaturated FA
carbon 3 is either |
|
|
Term
| describe the solubility of TAG |
|
Definition
| slightly soluble in water, cannot form micelles independently, can coalesce and form oil drops |
|
|
Term
| what are the building blocks in TAG synthesis |
|
Definition
| glycerol phosphate and acyl CoA |
|
|
Term
| what is the role of glycerol phosphate in TAG synthesis |
|
Definition
| initial acceptor of activated FA during TAG synthesis |
|
|
Term
| what is the role of acyl CoA in TAG sythesis |
|
Definition
| free FA must be converted to activated form |
|
|
Term
| what is the first step in TAG synthesis |
|
Definition
| synthesis of glycerol phosphate backbone |
|
|
Term
| how is glycerol phosphate made in adipose and liver |
|
Definition
| glucolytic path turns glucose into DHAP and DHAP is reduced to glycerol phosphate by glycerol kinase |
|
|
Term
| how is glycerol phosphate made in the liver only |
|
Definition
| glycerol kinase converts free glycerol into glycerol phosphate |
|
|
Term
| what is the second step in TAG synthesis |
|
Definition
| fatty acyl CoA synthase (thiokinases) turn free FA into acetyl CoA |
|
|
Term
| what attaches FA to backbone in TAG, what must then occur |
|
Definition
| acyl transferase, phosphatase removes phosphate |
|
|
Term
| what is the final step in fatty acid synthesis |
|
Definition
| acyl transferase adds third FA |
|
|
Term
| what is the difference between a chilomicron and a VLDL |
|
Definition
| chilomicron delivers exogenous dietary acquired lipids, VLDL delivers deo novo synthesized lipids |
|
|
Term
| where does NADPH for fatty acid synthesis come from |
|
Definition
| mostly hesosemonoophosphate (HMP) shunt, malate oxidation and decarboxylation by malic enzyme |
|
|
Term
| how does the hexosemonophosphate shunt work |
|
Definition
| G6P DH is rate limiting and irreversible, it uses NADP as a coenzyme acceptor to oxidize G6P |
|
|
Term
| for each hexosemonophosphate shunt round, how many NADPH are made |
|
Definition
|
|
Term
| what does the malic enzyme do |
|
Definition
| oxidizes and decarboxylates malate to pyruvate, NADP is a coenzyme acceptor to oxidize malate generating NADPH |
|
|
Term
| what does hormone sensitive lipase do |
|
Definition
| converts TAG to DAG releasing FA from TAG |
|
|
Term
| what does epinepherine do to hormone sensitive lipase, describe the process |
|
Definition
| it binds receptor, activates adenylyl cyclase which activates cAMP which turns on cAMP dependent protein kinase which phosphorlyates HSL activating it |
|
|
Term
| what does insulin do to hormone sensitive lipase, describe the process |
|
Definition
| it binds receptor, activates phosphatase which dephosphorlyates HSL, inactivating it |
|
|
Term
| when epinepherine is activating HSL what is it also doing in the cell |
|
Definition
| it sends cAMP to acetyl CoA carboxylase and deactivates it causing FA production from acetyl CoA to stop |
|
|
Term
| after HSL is activated, what happens before it can do its job with TAG |
|
Definition
| a perilipin (lipid droplet) binds to it and the lipase activity is now active |
|
|
Term
| what can happen to the fatty acid that is released via HSL from TAG |
|
Definition
| it can go into the tissues and be used for energy production, it can be re-esterified to lower free FA in plasma |
|
|
Term
| describe the path of FA from release from HSL to being used in a tissue for energy |
|
Definition
| it leaves adipocyte through wall, goes into blood, binds serum albumin, is transported to tissue, fatty acyl-CoA synthase (thypkinase) turns it into fatty acyl-CoA and it is used for energy |
|
|
Term
| what tissues can free FA on albumin not get dropped off at |
|
Definition
|
|
Term
| how is a free FA re-esterified |
|
Definition
| glyceroneogenesis produces glycerol-3-phoshpate DH which tunrs FA into esterified FA |
|
|
Term
| what disease is re-esterifying FA associated with |
|
Definition
| insulin resistance type 2 diabetes and obesity |
|
|
Term
| what is the fate of the glycerol left over after TAG degredation |
|
Definition
| it can go to the liver be phosphorlyated and used for TAG synthesis, it can be used for glyconeogenesis or glycolysis |
|
|
Term
| describe the path of a glycerol released from TAG to glycolysis |
|
Definition
| glycerol-3-phoshate DH turns it into DHAP which is used for glycolysis or gluconeogenesis |
|
|
Term
| why can't the adipocyte metabolize its glycerol back into TAG |
|
Definition
| because it has not glycerol kinase |
|
|
Term
| in beta oxidation, which end are fragments removed from |
|
Definition
|
|
Term
| where does beta oxidation occur |
|
Definition
|
|
Term
| how does a long chain fatty acid get inside the mitochondrial membrane after entering a cell for beta oxidation |
|
Definition
| LCFA CoA synthase (thiokinase) turns it into LCFA-CoA. CAT-1 turns it into acyl carnitine which is transported through by acyl carnitine translocate in exchange for carnitine |
|
|
Term
| once inside the mitochondria what happens to acyl carnitine |
|
Definition
| CAT II catalyzes it back to acyl-CoA |
|
|
Term
| how do short chain fatty acids and medium chain fatty acids get into the mitochondria |
|
Definition
| they can go through in their normal form and are changed by thiokinase into acyl CoA |
|
|
Term
|
Definition
|
|
Term
| what muscle relies on carnitine the most |
|
Definition
|
|
Term
| where does carnitine come from |
|
Definition
| diet (meat mostly), made by enzymatic path in liver and kidney with lys and met |
|
|
Term
| in general, what does a carnitine deficiency cause |
|
Definition
| decreased ability to use LCFA as fuel |
|
|
Term
| what are the congenital causes of carnitine deficiency |
|
Definition
| renal tubule reabsorption, decreased cell uptake, CAT I and II defect |
|
|
Term
| what occurs in a CAT I defect |
|
Definition
| decreased liver use of LCFA to make glucose in fasting |
|
|
Term
| what occurs in a CAT II defect |
|
Definition
| heart and skeletal m. cardiomyopathy, muscle weakness, myoglobinemia with exercise |
|
|
Term
| how can a carnitine deficiency be treated |
|
Definition
| avoid fastine, increase carbs, decrease LCFA in diet, eat MCFA and carnitine |
|
|
Term
| how many reactions are involved in beta oxidation |
|
Definition
|
|
Term
| how many carbons are dropped in each round of beta oxidation |
|
Definition
|
|
Term
| what is the first step in beta oxidation |
|
Definition
| acyl CoA DH oxidizes making FADH2 |
|
|
Term
| what is the second step in beta oxidation |
|
Definition
| enoyl CoA hydrolyase causes hydration |
|
|
Term
| what is the third step of beta oxidation |
|
Definition
| 3-hydroxyacyl CoA DH causes a second oxidation making NADH |
|
|
Term
| what is the forth step of beta oxidation |
|
Definition
| thiolytic clevage releasing acetyl CoA |
|
|
Term
| what links FA oxidation to gluconeogenesis |
|
Definition
| acetyl CoA is a positive allosteric effector of pyruvate carboxylase |
|
|
Term
| how many ATP are made from degrading 1 palmitoyl CoA |
|
Definition
|
|
Term
| what is the difference in beta oxidation with an even or odd nuumber of carbons |
|
Definition
| thyolytic clevage poduces a 3-carbon product, propionyl CoA |
|
|
Term
| what is the first step in metabolizing propionyl CoA |
|
Definition
| proponyl CoA is carboxylated by propinoyl CoA caroxylase making D-methylmalonyl CoA |
|
|
Term
| what is the second step in metabolizing propinoyl CoA |
|
Definition
| D-methylmalonyl CoA is converted to L-methylmalonyl CoA by methylmalonyl CoA racemase |
|
|
Term
| what is the last step in propinoyl CoA metabolization |
|
Definition
| l-methylmaolnyl-CoA is turned into succinyl CoA by methylmalonyl CoA mutase |
|
|
Term
| what does methylmaolnyl CoA mutase need to work |
|
Definition
|
|
Term
| how can a vitamin B12 deficiency be detected |
|
Definition
| excretion of propinoate and methylmalonate in the urine |
|
|
Term
| what causes heritable methylmalonic academia and acidurica |
|
Definition
| mutase is missing, deficient, or has poor affinity for B12, inability to convert B12 to coenzyme form |
|
|
Term
| what are the symptoms of methylmalonic academia and aciduria |
|
Definition
| metabolic acidosis and potential for retardation |
|
|
Term
| what type of FA have more energy, why |
|
Definition
| saturated because they are less highly reduced, fewer reducing equlivanents are made |
|
|
Term
| who do you need to oxidize monounsaturated fatty acids |
|
Definition
| additional isomerase enzyme |
|
|
Term
| what do you need to oxidize polyunsaturated fatty acids |
|
Definition
| isomerase and reductase enzyme |
|
|
Term
| where are FA 22 C or longer initially oxidized |
|
Definition
|
|
Term
| what happens in the perixisom in very long chain fatty acid oxidation different than normal |
|
Definition
|
|
Term
| what do genetic defects in peroxisome beta oxidation cause |
|
Definition
| failure to target matrix proteins to the peroxisome, Zelweger's syndrome |
|
|
Term
| what disease causes an inability to get VLCFA across peroxisome membrane |
|
Definition
| X-linked adrenoleukodystrophy |
|
|
Term
| what do all disorders with peroxisome beta oxidation cause |
|
Definition
| accumulation of VLCFA in blood and tissue |
|
|
Term
|
Definition
| branched chain 20 C FA phytanic acid cannot function as substrate for acetyl CoA DH because the methyl is at its beta carbon |
|
|
Term
| how does alpha oxidation of FA work |
|
Definition
| paytanoyl CoA a-hydrolase hydroxylates the alpha-carbon and carbon 1 and releases CO2 from phytanic acid, the 19 C pristanic acid is activated to CoA and undergoes beta oxidation |
|
|
Term
| what is the inheritance of refsum disease |
|
Definition
| rare, autosomal recessive |
|
|
Term
| what causes refsum disease |
|
Definition
| peroxisomal PhyH deficiency |
|
|
Term
| what occurs physiologically in refsum disease |
|
Definition
| phytanic acid accumulates in the blood and tissues |
|
|
Term
| what are the symptoms of refsum disease |
|
Definition
|
|
Term
| what is the treatment of regsum disease |
|
Definition
|
|
Term
| what occurs in a medium chain fatty acyl CoA DH deficiency |
|
Definition
| decreased oxidation of 6-10 C FA that then accumulate and show up in urine |
|
|
Term
| what are symptoms of medium chain fatty acyl CoA DH deficiency |
|
Definition
|
|
Term
| what is the treatment of medium chain fatty acyl CoA defiency |
|
Definition
|
|
Term
| what is the inheritance of medium chain fatty acyl CoA deficiency |
|
Definition
|
|
Term
| what are the ketone bodies |
|
Definition
| acetoacetate, 3-hydroxybuterate, acetone |
|
|
Term
|
Definition
|
|
Term
| how are ketone bodies made |
|
Definition
| beta oxidation from acetyl CoA |
|
|
Term
| where do acetoacetate and 3-hydroxybuterate go once made |
|
Definition
| blood then peripherial cells and tissues |
|
|
Term
| where does acetone go when it is made |
|
Definition
|
|
Term
| what do peripherial cells do to ketone bodies |
|
Definition
| convert them back into acetyl CoA for the TCA cycle |
|
|
Term
| how to ketone bodies travel in the blood |
|
Definition
|
|
Term
| when are ketone bodies made in the liver |
|
Definition
| when acetyl CoA levels superscede oxidation capacity |
|
|
Term
|
Definition
| extra hepatic tissues: heart skeletal muscle, renal cortex, brain if other sources are gone |
|
|
Term
| how do FA oxidation disorders commonly present |
|
Definition
| hypoketosis and hypoglycemia |
|
|
Term
|
Definition
| decreased acetyl CoA avability |
|
|
Term
|
Definition
| increased reliance on glucose for energy |
|
|
Term
| how is hepatic acetyl CoA activated |
|
Definition
| hepatic acetyl CoA is increased and this activates pyruvate carboxylase and inhibits pyruvate dehydrogenase producing OAA, OAA is used for glyconeogenesis not TCA so acetyl CoA is channeled into ketone body synthesis |
|
|
Term
| how does FA oxidation have a role in gluconeogenesis |
|
Definition
| it increases NADH shifting OAA to malate |
|
|
Term
| how is acetoacetyl CoA made |
|
Definition
| fatty acyl Coa and 2 acetyl CoA with thiolase |
|
|
Term
| what does HMG CoA synthase do |
|
Definition
| combines a third molecule of acetyl Coa with acetoacyl Coa to make HMG CoA |
|
|
Term
| what is the rate limiting step of ketogenesis |
|
Definition
|
|
Term
|
Definition
| HMG CoA is cleaed to make acetoacetate and acetyl CoA |
|
|
Term
| how is 3-hydroxybuterate made |
|
Definition
| acetoacetate is reduced with NADH has the H donor |
|
|
Term
|
Definition
| acetoacetate is spontaneously decarboxylated in the blood |
|
|
Term
| explain the process of ketolysis |
|
Definition
1. 3-hydroxybuterate is oxidized to acetoacetate by 3-hydroxy buterate DH making NADH
2. acetoacetate is provided with CoA from succinyl CoA by succinyl CoA aceteacetate CoA transferase
3. acetoacetyl CoA is converted into 2 acetyl CoA |
|
|
Term
| what is another name for succinyl CoA aceteacetate CoA transferase |
|
Definition
|
|
Term
| ehere does ketolysis occur |
|
Definition
| extrahepatic cells with mitochondria, not in liver it cannot use ketone bodies |
|
|
Term
| why cant the liver use ketone bodies |
|
Definition
|
|
Term
|
Definition
| high ketones in the blood |
|
|
Term
|
Definition
| high ketones in the urine |
|
|
Term
| what disease has ketonemia and ketonuria |
|
Definition
| diametes type 1, mellitus |
|
|
Term
| what causes fruity smelling breath |
|
Definition
| diabetic detoacidisis, acetone |
|
|
Term
| what does increased ketone bodies and glucose cause |
|
Definition
| increased secretion of water and dehydration |
|
|
Term
| describe the structure of phospholipids |
|
Definition
| alcohol with a phosphodiester bond to diacylglycerol or sphingosine |
|
|
Term
| describe the polarity of phospholipids |
|
Definition
|
|
Term
| what is the prodominate lipid of cell membranes |
|
Definition
|
|
Term
| what are examples of the hydrophoic portions of phospholipids |
|
Definition
| glycolipids, proteins, cholesterol |
|
|
Term
| what is the function of membrane phospholipids |
|
Definition
| reservoir for intracellular messengers and anchors for proteins |
|
|
Term
| what is the function of non-membrane bound phospholipids |
|
Definition
| components of lung surfactant and essential components of bile acting as a detergent to solublilze cholestrol |
|
|
Term
| describe the structure of a glycosphingolipid |
|
Definition
| glycerol back bone, 2 fatty acyl groups on C1 and C2, phosphate on C3 |
|
|
Term
| what is the simplest glycerophospholipid |
|
Definition
|
|
Term
| what is another name for glycerophospholipid |
|
Definition
|
|
Term
| what are all phosphoglycerides a derivative of |
|
Definition
|
|
Term
| describe the structure of sphingophospholipids |
|
Definition
| sphingosine backbone, long chain FA at carboxyl (palmotyl CoA), long chain FA at amino that is desaturated, phosphate group |
|
|
Term
| what is a sphingosine composed of |
|
Definition
|
|
Term
| what are all phosphoglycerides formed from |
|
Definition
| phosphatidic acid with alcohol esterified to the carbon-3-phosphate |
|
|
Term
| what alcohols can be esterified to the carbon-3-phosphate of phosphoglycerides |
|
Definition
| serine, ethanolamine, choline, inositol, glycerol |
|
|
Term
| describe the structure of a plasmalogen |
|
Definition
| FA at C2 is repalced by an unsaturated alkyl group attached by an ether rather than an ester link |
|
|
Term
| describe the structure of platlet activating factor |
|
Definition
| unusual ether glycerophospholipid, saturated alkyl group eith ether link to C1, acetyl residue at C2 |
|
|
Term
| what is the function of platlet activating factor |
|
Definition
| binds to surface receptors, triggers potent thromboitic and acute inflammatory events, activates imglammatory cells and mediates hypersensitivity, acute inflammation, anaphylactic reactions |
|
|
Term
| what does platlet activating factor cause to happen (in other cells) |
|
Definition
| platlets to aggregate and degranulate, neutrophils and alveolar macrophages to generate superoxide radicals |
|
|
Term
| what is the function of superoxide radicals |
|
Definition
|
|
Term
| describe the structure of cardiolipin |
|
Definition
| two PA molecules esterified through phosphates to molecule of glycerol |
|
|
Term
| where is cardiolipin found |
|
Definition
|
|
Term
| where is cardiolipin in eukaryotes |
|
Definition
| inner mitochondrial membrane |
|
|
Term
| what is the function of cardiolipin |
|
Definition
| meintience of respiratory complexes of electron transport chain |
|
|
Term
| what is cardioipin recognized by, what does that make it |
|
Definition
| it is antigenic, recognized by antibodies raised against treponema pallidum |
|
|
Term
| what does treponemia pallidum cause |
|
Definition
|
|
Term
| describe the structure of sphingomyelin |
|
Definition
| sphingosine backbone, unsaturated 16 C FA at C3, long chain FA at amino through amide link, C1 of spingosine esterified to phosporylcholine |
|
|
Term
| what is the function of sphingomyelin |
|
Definition
|
|
Term
| what is sphingomyelin a precursor for |
|
Definition
|
|
Term
| what is the only significant sphingophosphilipid in humans |
|
Definition
|
|
Term
|
Definition
| nucleotide cytidine diphosphate |
|
|
Term
| what are the two ways you can activate an intermediate in phospholipid synthesis |
|
Definition
donation of phosphatidic acid from CDP diacylglycerol to alcohol.
donation of phosphomonoester of alcohol from CDP alcohol to 1,2-DAG |
|
|
Term
| what is released as a side product of glycerophospholipid synthesis |
|
Definition
| cistidine monophosphate (CMP) |
|
|
Term
| where are most phospholipids made |
|
Definition
|
|
Term
| after made, where do phospholipids go |
|
Definition
| organells, plasma membrane, secreted to cell exterior by exocytosis |
|
|
Term
| what is the precursor for many phosphoglycerides |
|
Definition
|
|
Term
| what substrates do you need to make PA |
|
Definition
| glycerol phosphate and two fatty acyl CoA |
|
|
Term
| what is the only cell that cannot make phospholipids |
|
Definition
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
| what are the must abundent phospholipids in eukaryotic cells |
|
Definition
|
|
Term
| what are the steps in producing PE and PC from pre-existing pools |
|
Definition
1. kinase phosphorlyation of choline or ethanolamine
2. convert activated form CDP-choline. ethanolamine
3. choling-phosphate or ethanolamine-phosphate is transfered to a molecule is transfered to a molecule of diacylglycerol |
|
|
Term
| what phospholipids can the liver make |
|
Definition
|
|
Term
|
Definition
|
|
Term
| how do you form PC from PE or PS in the liver |
|
Definition
| PC from serum lipoproteins is secreted as bile, PS dis decarboxylated to PE by PS decarboxylase, PE is methlyated 3 times to make PC |
|
|
Term
| what does PS decarboxylase need to work |
|
Definition
| pyridoxal phosphate coenzyme |
|
|
Term
| why do we need to reutilize choline |
|
Definition
| de novo synthesis of choline in humans is not enough, choline is an essential nutrient, choline is used for synthesis of acetylcholin |
|
|
Term
|
Definition
|
|
Term
| what is dipalmitoylphosphatidylcholine, what is its function |
|
Definition
| surfactant that decreases surface tension in lungs, reduces pressure needed to imflate aveoli, prevents alveolar collapse |
|
|
Term
| what is another word for aveolar collapse |
|
Definition
|
|
Term
| describe the structure of DPPC |
|
Definition
| palmitate at positions 1 and 2 on glycerol |
|
|
Term
| what is the major lipid component of lung surfactant |
|
Definition
|
|
Term
|
Definition
|
|
Term
| what causes respiratory distress syndrome |
|
Definition
| insufficient lung surfactant |
|
|
Term
| how can lung formation in babies be accepelated |
|
Definition
| mother takes glucocorticoids shortly before delivery |
|
|
Term
| how can respiratory distress syndrome be treated |
|
Definition
| natural or synthetic surfactant |
|
|
Term
| how can fetal lung matirity be gauged |
|
Definition
| measuring DPPC, sphingomyelin ratio in amniotic fluid |
|
|
Term
| what does a ratio of 2 or higher mean in lung maturity |
|
Definition
| mature, sphingomyelin synthesis has shifted to DPPC in pneumocytes |
|
|
Term
| where does lung maturity usually occur |
|
Definition
|
|
Term
| why would an adult have RDS due to insufficient surfactant |
|
Definition
| surfactant making pneumocytes are damaged by infection or trauma |
|
|
Term
|
Definition
| base exchange reaction between ethanolamine of PE and free serine |
|
|
Term
|
Definition
|
|
Term
| is PS production reversible |
|
Definition
|
|
Term
|
Definition
|
|
Term
| describe the structure of PI |
|
Definition
| steric acid at C1 and archidonic acid on C2 |
|
|
Term
| what is the function of PI |
|
Definition
| resivour of arachidonic acid in membranes and substrate of prostaglandin synthesis |
|
|
Term
|
Definition
| free inositol and CDP-diacylglycerol |
|
|
Term
| describe the role of PI in signal transduction |
|
Definition
| phosphorlyation of membrane bound phosphatidylinositol makes polyphosphoinositides, degration of PIP2 by phospholipase C in response to a variety of neurotransmitters, hormones, and growth factors binding receptors, produces IP3 and DAG |
|
|
Term
|
Definition
| glycosylphosphatidylinositol |
|
|
Term
|
Definition
| covalent link between protein and Pi via a carbohydrate |
|
|
Term
| what is the function of GPI |
|
Definition
| bind cell surface proteins, anchor proteins allowing them to increase lateral mobility on surface of plasma membrane |
|
|
Term
| where are cell surface proteins bound by GPI found |
|
Definition
| in parasitic protozoans like trypanosomes and leishmania |
|
|
Term
| how can a protein be cleaved rom a GPI anchor |
|
Definition
| cleaved by phospholipase C releasing diacylglycerol |
|
|
Term
| what does a deficiency in GPI cause |
|
Definition
| hemolutic disease, paroxysmal nocturnal hemoglobinuria in hematopoietic cells |
|
|
Term
| how is phospharitylglycerol and cardiolipin made |
|
Definition
| CDP diacylglycerol and glycerol 3 phosphate |
|
|
Term
| what is cardiolipin made from |
|
Definition
| 2 phosphatidic acid connected by glycerol |
|
|
Term
| what is the precursor for cardiolipin |
|
Definition
|
|
Term
| where is phosphatidylglycerol found in large amounts |
|
Definition
|
|
Term
| describe the process of making cardiolipin |
|
Definition
| transfer of diacylglycerophosphate from CDP diacylglycerol to a pre-existing molecule of phosphatidylglycerol |
|
|
Term
| how is sphingomyelin made |
|
Definition
| palmitoyl CoA condenses with serine, CoA and CO2 released |
|
|
Term
| what does reduction in sphingomyelin production, what is the product at this point |
|
Definition
|
|
Term
| what coenzyme do you need to make sphingomyelin, where does it come from |
|
Definition
| pyrdoxal phosphate, vitamin B6 derivative |
|
|
Term
| describe the process of sphingomyelin production |
|
Definition
1. sphingosine acylated at amino with a long chain FA desaturated to make cremide
2.phosphorylcholine from phosphatidylcholine is transfered to ceramide making sphingomyelin and DAG |
|
|
Term
| what is a major component of skin and regulates skin water permability |
|
Definition
|
|
Term
| what type of FA does sphingomyelin of myelin sheath have |
|
Definition
| long chain like lingoceric acid, nervonic acid |
|
|
Term
| what FA does gray made sphingomyelin have |
|
Definition
|
|
Term
| what degrades phosphoglcerides, where |
|
Definition
| phospholipases in all tissues and pancreatic juice |
|
|
Term
| what things outside the body act as phospholipases |
|
Definition
| toxins and venoms, pathogenic bacteria use it to dissolve membranes and spread infection |
|
|
Term
| what is sphingomyelin degraded by, what is it classified as |
|
Definition
| lysosomalphospholipase sphingomyelinase |
|
|
Term
| what do phospholipases do to the molecule |
|
Definition
| hydrolyze phosphodiester bonds |
|
|
Term
| what makes phospholipases specific |
|
Definition
| each cleaves the phospholipid at a specific spot |
|
|
Term
| what are the major enzymes that degrade phospholipids |
|
Definition
| phospholipase A1, A2, C, D |
|
|
Term
| what does lysophospholipase need as a substrate |
|
Definition
|
|
Term
| how is lysphosphoglyceride made |
|
Definition
| removal of FA at C1 oe C2 |
|
|
Term
| what is the secondary functions of phospholipases |
|
Definition
| remodel phospholipids, release molecular messengers like DAG, iP3 or substrates for synthesis of messengers |
|
|
Term
| what is an example of a substrate for synthesis of messengers |
|
Definition
|
|
Term
| what do phospholipase A1 and A2 do |
|
Definition
| remove specific FA from membrane bound phospholipids |
|
|
Term
| what replaces after A1 and A2 do its job, what enzyme facilitates this |
|
Definition
| alternative FA using acyl CoA transferse |
|
|
Term
| how can unique lung surfactant be made |
|
Definition
| replacing with alternativie FA after using A1 and A2 phospholipases |
|
|
Term
| what degrades sphingomyelin |
|
Definition
|
|
Term
| where does sphingomyelinase come from |
|
Definition
|
|
Term
| how does sphingomyelinase do its job, what happens to the product to complee degredation |
|
Definition
| hydrolytically removes phosphorylcholine leaving ceramide which is cleaved by cermidase into sphingosine and FA |
|
|
Term
| what can released sphingosine and FA function in, how |
|
Definition
| regulate signal transduction pathways by influencing activity of protein kinase C by phosphorlyating its substrates, promote apoptosis |
|
|
Term
| what type of inheritance is niemann-pick disease |
|
Definition
|
|
Term
| what causes niemann-pick disease |
|
Definition
| inability to degrade sphingomyelin |
|
|
Term
| what is deficnent in niemann-pick disease |
|
Definition
| sphingomyelinase a type of phosphilipase C |
|
|
Term
| what are the symptoms of type A neimann-pick disease |
|
Definition
| lipid deposits in liver and spleen, liver and spleen enlarged, sphingomyelin cannot be degraded, severe infantile |
|
|
Term
| what happens to infants with severe lysosomal storage disease, why |
|
Definition
| rapid neurodegeneration due to sphingomyelin in CNS deposition causing early death |
|
|
Term
| what are the symptoms of type C niemann-pick disease |
|
Definition
| little to no damage to neural tissue, lungs spleen liver and bone marrow affected making it chronic, life expectancy to adulthood |
|
|
Term
| what population is more likley to have type A neimann pick disease |
|
Definition
| ashkenazi jewish population |
|
|
