PHOSPHORYLATION OF COAGULATION FACTOR-II BY PHOSPHOLIPID CA2+- DEPENDENT PROTEIN-KINASE (PROTEIN-KINASE-C)

被引：7

作者：

ABE, K ^{[1
]}

SAKURADA, K ^{[1
]}

TANAKA, M ^{[1
]}

UEHARA, Y ^{[1
]}

MATSUNO, K ^{[1
]}

MIYAZAKI, T ^{[1
]}

KATOH, N ^{[1
]}

机构：

[1] NATL INST ANIM HLTH,HOKKAIDO BRANCH LAB,SAPPORO 004,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 176卷 / 03期

关键词：

D O I：

10.1016/0006-291X(91)90401-R

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Prothrombin is a major constituent of the blood coagulation cascade and requires phospholipid and Ca2+ for its activation. We have found that phospholipid Ca2+-dependent protein kinase (Protein kinase C) phosphorylates prothrombin and the associated apparent Km value for prothrombin (0.86 μM) is comparable to the Km value reported for most known substrates of protein kinase C. A 2-dimension separation analysis revealed that serine residue was apparently phosphorylated by PKC. The phosphorylation was inhibited by such phosphatidylserine- and/or Ca2+ competitive protein kinase C inhibitors as trifluoperazine, palmitoylcarnitine and gossypol. These results suggest that protein kinase C phosphorylation was involved in the regulation of blood coagulation. © 1991.

引用

页码：1123 / 1129

页数：7

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