Endothelin-1 activates phospholipase C and mobilizes Ca2+ from extra- and intracellular pools in osteoblastic cells.
Endothelin-1 activates phospholipase C and mobilizes Ca2+ from extra- and intracellular pools in osteoblastic cells.
复制标题
Endothelin-1 激活磷脂酶 C 并从成骨细胞的细胞外和细胞内池中动员 Ca2。
DOI:
--
复制
发表时间:
1989
影响因子:
--
通讯作者:
Kamejiro Yamashita
中科院分区:
文献类型:
--
作者:
Y. Takuwa;Y. Ohue;N. Takuwa;Kamejiro Yamashita
The effect of endothelin-1 (ET), a novel vasoactive peptide derived from endothelial cells, on osteoblastic MC3T3-E1 cells was studied. ET specifically binds to a single class of high-affinity receptors in MC3T3-E1 cells and induces phospholipase C activation with the production of two second messengers, inositol trisphosphate and 1,2-diacylglycerol, and a biphasic increase in intracellular free Ca2+ concentration ([Ca2+]i), which consists of an initial transient increase and an ensuing sustained plateau, as measured with a fluorescent indicator, fura-2. The second plateau phase but not the initial transient increase in [Ca2+]i induced by ET is abolished by removal of extracellular Ca2+ but not by either nicardipine, verapamil, or diltiazem. The ET-stimulated production of inositol trisphosphate is not abolished by removal of extracellular Ca2+, indicating that ET-stimulated phospholipase C activation is not a consequence of an increase in Ca2+ influx across the plasma membrane. ET causes stimulation of DNA synthesis and reduction of alkaline phosphatase activity in MC3T3-E1 cells. A protein kinase C activator phorbol 12,13-dibutyrate mimics these effects of ET. The results demonstrate that ET activates the inositol lipid signaling pathway and induces mobilization of Ca2+ from both extra- and intracellular pools and activation of protein kinase C in osteoblastic MC3T3-E1 cells.
DOI:
10.1016/s0006-291x(89)80193-7
发表时间:
1989
影响因子:
3.1
作者:
Sugiura,M;Inagami,T;Hare,GM;Johns,JA
通讯作者:
Johns,JA
影响因子:
3.1
作者:
Enright, E;Bland, AP;Kelly, AL
通讯作者:
Kelly, AL