Topic
Protein Z
About: Protein Z is a research topic. Over the lifetime, 225 publications have been published within this topic receiving 5976 citations. The topic is also known as: vitamin K-dependent protein Z precursor variant 1 & PROZ.
Papers published on a yearly basis
Papers
More filters
TL;DR: The major effect of PZ and ZPI is to dampen the coagulation response prior to the formation of the prothrombinase complex, which dramatically delays the initiation and reduces the ultimate rate of thrombin generation in mixtures containing prothromabin, factor V, phospholipids, and Ca(++).
166 citations
TL;DR: Concomitant PZ deficiency dramatically increases the severity of the prothrombotic phenotype of factor VLeiden mice, and the potential roles of PZ and ZPI deficiency in human thrombosis are in progress.
Abstract: Protein Z (PZ) is a 62 kDa vitamin K-dependent plasma protein that serves as a cofactor for the inhibition of factor Xa by protein Z-dependent protease inhibitor (ZPI). ZPI is a recently identified 72 kDa member of the serpin superfamily of proteinase inhibitors that contains a tyrosine at its reactive center. PZ circulates in plasma in a complex with ZPI. Inhibition of factor Xa by ZPI in the presence of phospholipids and Ca++ is enhanced 1000-fold by PZ, but ZPI also inhibits factor XIa in a process that does not require PZ, phospholipids or Ca++. ZPI activity is consumed during coagulation through proteolysis mediated by factor Xa with PZ and factor Xla. Concomitant PZ deficiency dramatically increases the severity of the prothrombotic phenotype of factor VLeiden mice. Studies to determine the potential roles of PZ and ZPI deficiency in human thrombosis are in progress.
160 citations
TL;DR: The presence of PZ dampens the coagulation response in human plasma and that concomitant PZ deficiency dramatically increases the severity of the prothrombotic phenotype of factor V(Leiden) mice, indicating that PZ plays a physiologically important role in the regulation of coagulations.
Abstract: Protein Z (PZ) is a vitamin K-dependent plasma protein whose function has been uncertain. The structure of PZ is very similar to that of the coagulation-related factors VII, IX, and X and PC, but PZ differs from these other proteins in that it is not the zymogen of a serine protease. We have shown recently that PZ forms a calcium ion-dependent complex with activated factor X at phospholipid surfaces and that this interaction leads to the inhibition of activated factor X activity through, in part, the action of a previously unidentified plasma protein named PZ-dependent protease inhibitor. Herein, we report that the presence of PZ dampens the coagulation response in human plasma and that concomitant PZ deficiency dramatically increases the severity of the prothrombotic phenotype of factor VLeiden mice. The results indicate that PZ plays a physiologically important role in the regulation of coagulation.
159 citations
TL;DR: In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and aXyl-GlC-Ser structure in the first epidermal growth factor-like domains of human factors VIII and IX and protein Z in addition to that of bovines protein Z.
156 citations
TL;DR: Among vitamin K-dependent proteins, factor IX, factor X, protein C, and protein Z each contain about one residue of beta-hydroxyaspartic acid whereas protein S contains two or three residues.
150 citations