Sandbox Reserved 596: Difference between revisions
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'''Function''' | '''Function''' | ||
The function of PZ was studied in 1991 by Hogg and Stenflo, who initially hypothesized PZ to amplify the coagulation cascade but found that bovine PZ has a higher affinity for thrombin than human PZ due to a 36 amino acid addition to the bovine PZ's C-terminus. Furthermore, they found that PZ virtually had no involvement in binding thrombin to phospholipids. It was not until 1998 that Han et al. described PZ present in the body as a complex with protein Z-dependent protease inhibitor (ZPI). The ZPI and PZ complex acts as an inhibitor of factor Xa attached to the | The function of PZ was studied in 1991 by Hogg and Stenflo, who initially hypothesized PZ to amplify the coagulation cascade but found that bovine PZ has a higher affinity for thrombin than human PZ due to a 36 amino acid addition to the bovine PZ's C-terminus. Furthermore, they found that PZ virtually had no involvement in binding thrombin to phospholipids. It was not until 1998 that Han et al. described PZ present in the body as a complex with protein Z-dependent protease inhibitor (ZPI). The ZPI and PZ complex acts as an inhibitor of factor Xa attached to the membrane surface (forming a calcium-dependent teritary complex). It is still unknown if the PZ and ZPI travel the body as a complex or if the complex forms at the phospholipid bilayer. While ZPI needs PZ, phospholipids, and calcium present to inhibit factor Xa, ZPI does not require other components to inhibit another coagulation factor XI. | ||
'''Clinical Relevance''' | '''Clinical Relevance''' | ||
'''References''' | '''References''' | ||
