Mechanisms involved in α6β1-integrin-mediated Ca2+ signalling

被引：24
|
作者：
Schöttelndreier, H
Potter, BVL
Mayr, GW
Guse, AH
机构：
[1] Univ Hamburg, Hosp Eppendorf, Div Cellular Signal Transduct, Inst Med Biochem & Mol Biol, D-20246 Hamburg, Germany
[2] Univ Bath, Dept Pharm & Pharmacol, Wolfson Lab Med Chem, Bath BA2 7AY, Avon, England
来源：
CELLULAR SIGNALLING | 2001年 / 13卷 / 12期
基金：
英国惠康基金;
关键词：
integrin; extracellular matrix; Ca2+ signalling; inositol 1,4,5-trisphosphate; cyclic ADP-ribose; capacitative Ca2+ entry; SKF; 96365;
D O I：
10.1016/S0898-6568(01)00225-X
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
Contact of Jurkat T-lymphocytes with the extracellular matrix (ECM) protein laminin resulted in long-lasting alpha6 beta1-integrin-mediated Ca2+ signalling. Both Ca2+ release from thapsigargin-sensitive Ca2+ stores and capacitative Ca2+ entry via Ca2+ channels sensitive to SKF 96365 constitute important parts of this process. Inhibition of alpha6 beta1-integrin-mediated Ca2+ signalling by (1) the src kinase inhibitor PP2, (2) the PLC inhibitor U73122, and (3) the cyclic adenosine diphosphoribose (cADPR) antagonist 7-deaza-8-Br-cADPR indicate the involvement of src tyrosine kinases and the Ca2+-releasing second messengers D-myo-inositol 1.4,5-trisphosphate (InSP3) and cADPR. (C) 2001 Elsevier Science Inc. All rights reserved.
引用
收藏
页码：895 / 899
页数：5
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