PHOSPHORYLATION OF SMG P21B IN RAT PERITONEAL MAST-CELLS IN ASSOCIATION WITH HISTAMINE-RELEASE INHIBITION BY DIBUTYRYL-CAMP

被引：6

作者：

IZUSHI, K ^{[1
]}

SHIRASAKA, T ^{[1
]}

CHOKKI, M ^{[1
]}

TASAKA, K ^{[1
]}

机构：

[1] OKAYAMA UNIV,FAC PHARMACEUT SCI,DEPT PHARMACOL,OKAYAMA 700,JAPAN

来源：

FEBS LETTERS | 1992年 / 314卷 / 03期

关键词：

SMG-P21B; PROTEIN PHOSPHORYLATION; PROTEIN KINASE-A; HISTAMINE RELEASE; RAT MAST CELL;

D O I：

10.1016/0014-5793(92)81480-A

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：

IP3 formation and histamine release from rat peritoneal mast cells stimulated by compound 48/80 were dose-dependently inhibited by Bt2cAMP. These inhibitions were restored to the control level in the presence of H-8, a protein kinase A inhibitor. The 22 kDa protein in mast cells was revealed as a markedly phosphorylated protein by incubating with Bt2cAMP, and this phosphorylation was also diminished by H-8. The 22 kDa phosphoprotein of rat mast cells comigrated with phosphorylated smg p21B, purified from human platelets and phosphorylated by protein kinase A in cell-free system, in both one- and two-dimensional PAGE analysis. Moreover, 22 kDa protein in mast cells was identified as smg p21B by immunoblot analysis using an antibody against smg p21B. From the present study, it became clear that smg p21B is phosphorylated by means of protein kinase A system in rat peritoneal mast cells, and it was assumed that phosphorylated smg p21B plays some important role in the suppression of IP3 formation and histamine release from rat peritoneal mast cells.

引用

页码：241 / 245

页数：5

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