Bradykinin B2 receptor-activated Ca influx; interaction of IP4, ras-GAP IP4-binding protein, and protein tyrosine phosphorylation

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• 作者：Higashida ; Haruhiro ; Hashii ; Minako ; Taketo ; Megumi ; Yokoyama ; Shigeru
• 刊名：Neuroscience Research
• 出版年：1997
• 期刊代码：53_01680102
• 类别：neu
• 出版时间：1997
• 卷：21
• 期：Supplement 1
• 页码：S6
• 文件大小：89.8 K

摘要

We have reported that application of bradykinin (BK), a neuropeptide, increases in [Ca²⁺]ⁱ, which is extracellular Ca²⁺-dependent in Ki-ras-transformed NIH/3T3 (DT) fibroblasts. Activation of BK B2 receptors resulted in a decrease of cellular fluorescence at the excitation wavelength of 360 nm after MnC¹² application in DT cells. This Mn²⁺ entry increased with membrane hyperpolarization. Internal application of Ins(1,3,4,5)P4 mimicked the membrane potential-dependent Mn²⁺ entry. BK- and InsP4-induced Ca²⁺ influx was blocked by a tyrosine kinase inhibitor, genistein. Bradykinin receptor activation induced tyrosine phosphorylation of MAP kinase, which was inhibited by genistein. These results suggest that two B2 receptor-activated signal pathways, protein tyrosine phosphorylation and InsP4, merge at the hyperpolarization-activated Ca²⁺ influx process in ras-transformed NIH/3T3 fibroblasts.