PROTEOLYTIC MODIFICATION OF MEMBRANE-ASSOCIATED PHOSPHOLIPASE C-BETA BY MU-CALPAIN ENHANCES ITS ACTIVATION BY G-PROTEIN BETA-GAMMA-SUBUNITS IN HUMAN PLATELETS

被引：23
作者：
BANNO, Y
ASANO, T
NOZAWA, Y
机构：
[1] GIFU UNIV,SCH MED,DEPT BIOCHEM,GIFU 500,JAPAN
[2] AICHI PREFECTURAL COLONY,INST DEV RES,DEPT BIOCHEM,KASUGAI,AICHI 48003,JAPAN
来源：
FEBS LETTERS | 1994年 / 340卷 / 03期
关键词：
PHOSPHOLIPASE C ACTIVATION; G-PROTEIN BETA-GAMMA SUBUNIT; PROTEOLYSIS BY CALPAIN; HUMAN PLATELET;
D O I：
10.1016/0014-5793(94)80134-7
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：
Membrane-associated phosphoinositide-phospholipase C (PI-PLC)-beta (150 kDa) and its truncated forms (100 kDa and 45 kDa) were purified from human platelets. The 100 kDa PI-PLC-beta was found to be activated to a greater extent by brain G-protein beta gamma subunits compared to the intact 150 kDa enzyme. Furthermore, treatment with mu-calpain of the intact PI-PLC-beta (150 kDa) caused a marked augmentation of its activation by pr subunits. This enhanced PLC activation by beta gamma subunits was due to truncation beta gamma mu-calpain, producing a 100 kDa PI-PLC, but not by another protease, thrombin.
引用
收藏
页码：185 / 188
页数：4
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