Serine/threonine protein kinases synergistically regulate phospholipase D1 and 2 and secretion in RBL-2H3 mast cells

被引：19

作者：

Chahdi, A ^{[1
]}

Choi, WS ^{[1
]}

Kim, YM ^{[1
]}

Fraundorfer, PF ^{[1
]}

Beaven, MA ^{[1
]}

机构：

[1] NHLBI, Lab Mol Immunol, NIH, Bethesda, MD 20892 USA

来源：

MOLECULAR IMMUNOLOGY | 2002年 / 38卷 / 16-18期

关键词：

phospholipase D1 and 2; protein kinases; mast cells; secretion;

D O I：

10.1016/S0161-5890(02)00074-3

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：

The role of phospholipase (PL) D in secretion was examined in RBL-2H3 mast cells which contain both PLD1 and 2. The effects of pharmacologic stimulants and inhibitors of Ca2+/calmodulin-dependent kinase II, protein kinase C, and protein kinase A suggested that all three kinases synergistically stimulate PLD and, when associated with a calcium signal, secretion as well to indicate a possible linkage between these two events. Overexpression of either PLD1 or 2 markedly enhanced the activation of PLD by pharmacologic stimulants as well as antigen and both isoforms thus appear co-ordinately regulated. As the expressed PLD1 was associated with secretory granules and PLD2 with the plasma membrane, the two isoforms may serve distinct but complementary functions in secretion. Published by Elsevier Science Ltd.

引用

页码：1269 / 1276

页数：8

共 26 条

[1] ANTIGEN AND THAPSIGARGIN PROMOTE INFLUX OF CA2+ IN RAT BASOPHILIC RBL-2H3 CELLS BY OSTENSIBLY SIMILAR MECHANISMS THAT ALLOW FILLING OF INOSITOL 1,4,5-TRISPHOSPHATE-SENSITIVE AND MITOCHONDRIAL CA2+ STORES [J].