Miyawaki A, Furuichi T, Maeda N, Mikoshiba K
Division of Behavior and Neurobiology, National Institute for Basic Biology, Okazaki, Japan.
Neuron. 1990 Jul;5(1):11-8. doi: 10.1016/0896-6273(90)90029-f.
P400, inositol 1,4,5-trisphosphate receptor (InsP3-R), is a key protein to understanding the mechanisms of inositol 1,4,5-trisphosphate (InsP3)-mediated Ca2+ mobilization. We obtained the cerebellar-type P400/InsP3-R cDNA and generated an L cell transfectant (L15) that produces cDNA-derived P400/InsP3-R. In membranes, this protein displays high affinity, specificity, and capacity for InsP3, as does the cerebellar P400/InsP3-R. InsP3 can also induce greater 45Ca2+ release from the membrane vesicles of L15 cells than from those of control L cells. These results provide direct evidence that the cDNA-derived P400/InsP3-R protein is actually involved in physiological Ca2+ mobilization, through binding to InsP3 molecules in the same manner as the cerebellar P400/InsP3-R.
P400,即肌醇1,4,5 - 三磷酸受体(InsP3 - R),是理解肌醇1,4,5 - 三磷酸(InsP3)介导的Ca2+动员机制的关键蛋白。我们获得了小脑型P400/InsP3 - R cDNA,并构建了产生cDNA衍生的P400/InsP3 - R的L细胞转染体(L15)。在细胞膜中,该蛋白对InsP3表现出高亲和力、特异性和结合能力,与小脑P400/InsP3 - R相同。InsP3还能比对照L细胞的膜囊泡诱导L15细胞的膜囊泡释放更多的45Ca2+。这些结果提供了直接证据,表明cDNA衍生的P400/InsP3 - R蛋白实际上通过与小脑P400/InsP3 - R相同的方式结合InsP3分子参与了生理性Ca2+动员。