首页> 外文OA文献 >Bradykinin B2 receptor-induced and inositol tetrakisphosphate-evoked Ca2+ entry is sensitive to a protein tyrosine phosphorylation inhibitor in ras-transformed NIH/3T3 fibroblasts.
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Bradykinin B2 receptor-induced and inositol tetrakisphosphate-evoked Ca2+ entry is sensitive to a protein tyrosine phosphorylation inhibitor in ras-transformed NIH/3T3 fibroblasts.

机译:缓激肽B2受体诱导和肌醇四磷酸酯诱发的Ca2 +进入对ras转化NIH / 3T3成纤维细胞中的蛋白酪氨酸磷酸化抑制剂敏感。

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摘要

Signal transduction from mouse bradykinin B2 receptors to calcium influx was studied in ras-transformed NIH/3T3 (DT) fibroblasts. DT cells were preloaded with fura-2 and whole-cell voltage-clamped. Activation of B2 receptors resulted in a decrease of cellular fluorescence at the excitation wavelength of 340, or 360 nm after MnCl2 application, in both the presence and absence of external Ca2+ in DT cells, at a holding potential of -40 mV. This Mn2+ entry through the Ca2+ influx pathway increased with membrane hyperpolarization. Internal application of inositol 1,3,4,5-tetrakisphosphate (InsP4), but not of inositol 1,4,5-trisphosphate, mimicked membrane potential-dependent Mn2+ entry. Bradykinin- and InsP4-induced Ca2+ influx was blocked by 10-100 microM genistein, a tyrosine kinase inhibitor. B2 receptor activation induced time-dependent tyrosine phosphorylation of mitogen-activated protein kinase and 120 kDa protein, which was dose-dependently inhibited by genistein. Bradykinin was unable to induce Ca2+ oscillations in genistein-treated DT cells. Our results show that bradykinin-induced Ca2+ influx and oscillations depend upon protein tyrosine phosphorylation. The results suggest that two bradykinin B2 receptor-activated signal pathways, protein tyrosine phosphorylation and formation of InsP4, merge at the Ca2+ influx process in ras-transformed NIH/3T3 fibroblasts.
机译:在ras转化的NIH / 3T3(DT)成纤维细胞中研究了从小鼠缓激肽B2受体到钙流入的信号转导。 DT细胞预装了fura-2,并进行了全细胞电压钳制。 B2受体的激活导致DT细胞中存在或不存在外部Ca2 +的情况下,在-40 mV的保持电势下,在MnCl2施加后340或360 nm的激发波长处,细胞荧光减弱。 Mn2 +通过Ca2 +流入途径的进入随膜超极化而增加。内部应用肌醇1,3,4,5-四磷酸(InsP4),而不是肌醇1,4,5-三磷酸,模仿膜电位依赖性Mn2 +进入。缓激肽和InsP4诱导的Ca2 +内流被酪氨酸激酶抑制剂10-100 microM染料木黄酮阻断。 B2受体激活诱导丝分裂原激活的蛋白激酶和120 kDa蛋白的时间依赖性酪氨酸磷酸化,其被染料木黄酮剂量依赖性抑制。缓激肽不能在染料木素处理过的DT细胞中诱导Ca2 +振荡。我们的结果表明,缓激肽诱导的Ca2 +内流和振荡取决于蛋白酪氨酸的磷酸化。结果表明,在ras转化的NIH / 3T3成纤维细胞中,两个缓激肽B2受体激活的信号途径(蛋白质酪氨酸磷酸化和InsP4的形成)在Ca2 +流入过程中合并。

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