Term
| what is the function of the von Willebrand factor? |
|
Definition
| mediates binding of platelets to collagen during initial phase |
|
|
Term
| what happens when fibrinogen is activated? |
|
Definition
|
|
Term
| what particularly is cleaved in fibrinogen that allows it to be active? |
|
Definition
|
|
Term
| tissue factor binds to what factor in the initial stage of clotting? |
|
Definition
|
|
Term
| What does factor 10 and 5 activate |
|
Definition
|
|
Term
| what does thrombin activates? |
|
Definition
|
|
Term
| what is the enzyme amplification cascade? |
|
Definition
| one enzyme at the start of the activation pathway can activate many molecules of a given substrate |
|
|
Term
| how many sites of binding are there in tissue factor? |
|
Definition
|
|
Term
| what is the structure of factor 7? |
|
Definition
| TF inhibitory peptide, Ca2+ binding site, and a substrate binding pocket labeled the catalytic triad |
|
|
Term
| what is the structure of the catalytic triad? |
|
Definition
| histidine, serine, aspartate |
|
|
Term
| What are the types of hemophilia? |
|
Definition
|
|
Term
| What is characterized by type A hemophilia? |
|
Definition
|
|
Term
| Type B hemophilia is characterized by? |
|
Definition
|
|
Term
| Which type of hemophilia can be treated? |
|
Definition
| type A (recombinant factor) |
|
|
Term
| activation of prothrombin requires how many proteolytic cleavages? |
|
Definition
|
|
Term
| what is the bond that keeps the prothrombin molecules together? |
|
Definition
|
|
Term
| What is the structure of the alpha thrombin |
|
Definition
| F 1-2, A and B (connected by disulfide bonds) |
|
|
Term
| the peptides that are cleaved by thrombin contain many of these AA's |
|
Definition
| Aspartate, Glutamate, and sulfated-tyrosine |
|
|
Term
| what's the overall charge of the peptide that is cleaved from fibrinogen? |
|
Definition
|
|
Term
| Thrombin activates this factor, which forms fibrin cross-links |
|
Definition
|
|
Term
| What is the specific bond catalyzed by activated Factor 13? |
|
Definition
|
|
Term
| What are the two amino acids that transglutaminase cleave? |
|
Definition
|
|
Term
| Name an example of an anti-protease? |
|
Definition
|
|
Term
| what is the mech of action of anti-thrombin 3? |
|
Definition
| binds and inactivates thrombin |
|
|
Term
| What is heparin used for? |
|
Definition
| promotes tighter binding of anti thrombin 3 to thrombin |
|
|
Term
| how does thrombin auto-regulate itself? |
|
Definition
| it binds to thrombomodulin |
|
|
Term
| what acts as cofactors of thrombin activation of Protein C |
|
Definition
| thrombomodulin and calcium |
|
|
Term
| this is Gla containing protease |
|
Definition
|
|
Term
| what happens when protein C is activated? |
|
Definition
| in conjunction w/protein S proteolyze and inactivate Factors 5a and 8a |
|
|
Term
|
Definition
| protease that converts plasminogen to plasmin |
|
|
Term
| plasmin provides what in the inactivation compounds? |
|
Definition
|
|
Term
| t-PA provides what in the inactive complexe? |
|
Definition
|
|
Term
| what is the function of carboxyglutamate? |
|
Definition
| brings enzymes onto the surface of the cell membrane |
|
|
Term
| what is the structure of the carboxyglutamate? |
|
Definition
| modified glutamate residue (extra COO-) |
|
|
Term
| Glutamate has a natural high affinity of? |
|
Definition
|
|
Term
| Which factors contain carboxyglutamate? |
|
Definition
| thrombin, factor 7,9, and 10 |
|
|
Term
| what is the function of vitamin K? |
|
Definition
| co factor that attaches a carboxy onto the glutamate |
|
|
Term
| What is function of dicoumarol and warfarin? |
|
Definition
| vit-K analog that inhibits the formation of carboxyglutamate, inhibiting coagulation |
|
|
Term
| the liver is signaled to do what in the presence of carboxypeptides? |
|
Definition
| synthesis of factors 2, 7, 9, 10 and protein C |
|
|
Term
| why should you monitor patients on vit K antagonist? |
|
Definition
| you wana make sure that carboxy protein production is still being formed. |
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