Calmodulin inhibits inositol trisphosphate-induced Ca2+ mobilization from the endoplasmic reticulum of islets.
Calmodulin inhibits inositol trisphosphate-induced Ca2+ mobilization from the endoplasmic reticulum of islets.
复制标题
钙调蛋白抑制肌醇三磷酸诱导的胰岛内质网 Ca2+ 动员。
DOI：
10.1016/s0006-291x(86)80189-9
复制
发表时间：
1986
影响因子：
3.1
通讯作者：
McDaniel,ML
中科院分区：
文献类型：
--
作者：
Wolf,BA;Colca,JR;McDaniel,ML
IP 3诱导的Ca 2+从胰岛内质网（ER）释放被认为是葡萄糖诱导的胰岛素分泌中的关键细胞内事件。钙调素可增加ATP依赖的Ca ~（2+）稳态，并抑制57.2%的IP 3诱导的Ca ~（2+）从ER的动员。相反，钙调素拮抗剂，N-（6-氨基己基）-5-氯-1-萘磺酰胺（W-7），诱导Ca 2+从ER释放。W-7（100 μM）和IP 3（10 μM）的组合导致比单独的W-7或IP 3更大的Ca 2+从ER的释放。W-7显示不影响ER的结构完整性。我们的研究结果表明，IP 3诱导的Ca 2+释放从ER是由钙调素依赖性的过程。
IP3-induced Ca2+release from the endoplasmic reticulum (ER) of islets is believed to be a key intracellular event in glucose-induced insulin secretion. Calmodulin was shown to increase ATP-dependent Ca2+steady-state and inhibit by 57.2% IP3-induced Ca2+mobilization from the ER. Conversely, the calmodulin antagonist, N-(6-aminohexyl)-5-chloro-l-naphtalene sulfonamide (W-7), induced Ca2+release from the ER. The combination of W-7 (100 μM) and IP3(10 μM), resulted in a greater release of Ca2+from the ER than either W-7 or IP3alone. W-7 was shown not to affect the structural integrity of the ER. Our results suggest that IP3-induced Ca2+release from the ER is regulated by a calmodulin-dependent process.