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The endothelium is actively involved in many functions of the cardiovascular system, such as the modulation of arterial pressure and the maintenance of blood flow. These functions require a great versatility of the intracellular Ca 2+  signaling that resides in the fact that different signals can be encoded by varying the frequency and the amplitude of the Ca 2+  response. Cells use both extracellular and intracellular Ca 2+  pools to modulate the intracellular Ca 2+  concentration. In non-excitable cells, the inositol 1,4,5-trisphosphate receptor (IP 3 R), located on the endoplasmic reticulum (ER), is responsible for the release of Ca 2+  from the intracellular store. The proteins STIM1 and STIM2 are also located on the ER and they are involved in the activation of a store-operated Ca 2+  entry (SOCE). Due to their Ca 2+  sensor property and their close proximity with IP 3 Rs on the ER, STIMs could modulate the activity of IP 3 R. In this study, we showed that STIM1 and STIM2 are expressed in bovine aortic endothelial cells and they both interact with IP 3 R. While STIM2 appears to play a minor role, STIM1 plays an important role in the regulation of agonist-induced Ca 2+  mobilization in BAECs by a positive effect on both the SOCE and the IP 3 R-dependent Ca 2+  release.

STIM1 Positively Regulates the Ca2+ Release Activity of the Inositol 1,4,5-Trisphosphate Receptor in Bovine Aortic Endothelial Cells