Tyrosine phosphatase PTP1B modulates store-operated calcium influx

被引：16

作者：

Hsu, S

Schmid, A

Sternfeld, L

Anderie, I

Solis, G

Hofer, HW

Schulz, I

机构：

[1] Univ Saarland, Dept Physiol, D-66421 Homburg, Germany

[2] Univ Konstanz, Fac Biol, D-78457 Constance, Germany

来源：

CELLULAR SIGNALLING | 2003年 / 15卷 / 12期

关键词：

store-operated calcium influx; protein tyrosine phosphorylation; PTP1B;

D O I：

10.1016/S0898-6568(03)00088-3

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

We have studied modulation of "store-operated calcium influx" by tyrosine phosphatases in the pancreatic acinar cell line AR42J and in HEK 293 cells. We show that inhibition of tyrosine phosphatases by bis-(N,N-dimethyl-hydroxamido) hydrooxovanadate (DMHV) leads to an increase in Ca2+ release-activated Ca2+ (CRAC) entry. This effect can be blocked in the presence of 2-aminoethyldiphenyl borate (2-APB). Furthermore, transfection of HEK 293 cells with the human wild-type tyrosine phosphatase PTP1B leads to inhibition of CRAC influx, whereas transfection with the substrate-trapping mutant of PTP1B (D181A) slightly increases Ca2+ influx. It also decreases enzymatic activity of PTP1B as compared to non-transfected cells. Our data suggest that CRAC influx is modulated by tyrosine phosphorylation and dephosphorylation which involves the tyrosine phosphatase PTP1B. (C) 2003 Elsevier Inc. All rights reserved.

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页码：1149 / 1156

页数：8

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