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Involvement of STIM1 in the proteinase-activated receptor 1-mediated Ca2+ influx in vascular endothelial cells

✍ Scribed by Katsuya Hirano; Mayumi Hirano; Akiko Hanada

Publisher
John Wiley and Sons
Year
2009
Tongue
English
Weight
384 KB
Volume
108
Category
Article
ISSN
0730-2312

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✦ Synopsis

Abstract

Thrombin increases the cytosolic Ca^2+^ concentrations and induces NO production by activating proteinase‐activated receptor 1 (PAR~1~) in vascular endothelial cells. The store‐operated Ca^2+^ influx is a major Ca^2+^ influx pathway in non‐excitable cells including endothelial cells and it has been reported to play a role in the thrombin‐induced Ca^2+^ signaling in endothelial cells. Recent studies have identified stromal interaction molecule 1 (STIM1) to function as a sensor of the store site Ca^2+^ content, thereby regulating the store‐operated Ca^2+^ influx. However, the functional role of STIM1 in the thrombin‐induced Ca^2+^ influx and NO production in endothelial cells still remains to be elucidated. Fura‐2 and diaminorhodamine‐4M fluorometry was utilized to evaluate the thrombin‐induced changes in cytosolic Ca^2+^ concentrations and NO production, respectively, in porcine aortic endothelial cells transfected with small interfering RNA (siRNA) targeted to STIM1. STIM1‐targeted siRNA suppressed the STIM1 expression and the thapsigargin‐induced Ca^2+^ influx. The degree of suppression of the STIM1 expression correlated well to the degree of suppression of the Ca^2+^ influx. The knockdown of STIM1 was associated with a substantial inhibition of the Ca^2+^ influx and a partial reduction of the NO production induced by thrombin. The thrombin‐induced Ca^2+^ influx exhibited the similar sensitivity toward the Ca^2+^ influx inhibitors to that seen with the thapsigargin‐induced Ca^2+^ influx. The present study provides the first evidence that STIM1 plays a critical role in the PAR~1~‐mediated Ca^2+^ influx and Ca^2+^‐dependent component of the NO production in endothelial cells. J. Cell. Biochem. 108: 499–507, 2009. © 2009 Wiley‐Liss, Inc.

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