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钙/磷脂调节脑突触体中一种分子量为“87k”的底物蛋白的磷酸化。

Calcium/phospholipid regulates phosphorylation of a Mr "87k" substrate protein in brain synaptosomes.

作者信息

Wu W C, Walaas S I, Nairn A C, Greengard P

出版信息

Proc Natl Acad Sci U S A. 1982 Sep;79(17):5249-53. doi: 10.1073/pnas.79.17.5249.

DOI:10.1073/pnas.79.17.5249
PMID:6957862
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC346873/
Abstract

Depolarization-induced calcium influx into rat cerebral cortex synaptosomes increased the phosphorylation of several synaptosomal proteins as examined by 32Pi incorporation. A phosphopeptide mapping technique involving NaDodSO4/polyacrylamide gels has been used to show that phosphorylation of a Mr 87,000 substrate protein is stimulated by depolarization-induced calcium influx. Phosphorylation of this Mr 87,000 substrate occurred in synaptosomal cytosol and was markedly stimulated by calcium/phosphatidylserine. Calmodulin inhibited this phosphorylation reaction. This substrate for calcium/phospholipid-dependent protein kinase is enriched in and appears to be specific to neurons.

摘要

去极化诱导的钙离子流入大鼠大脑皮质突触体，通过³²Pi掺入法检测发现，这增加了几种突触体蛋白的磷酸化。一种涉及十二烷基硫酸钠/聚丙烯酰胺凝胶的磷酸肽图谱技术已被用于表明，去极化诱导的钙离子流入刺激了分子量为87,000的底物蛋白的磷酸化。这种分子量为87,000的底物蛋白的磷酸化发生在突触体胞质溶胶中，并被钙/磷脂酰丝氨酸显著刺激。钙调蛋白抑制这种磷酸化反应。这种钙/磷脂依赖性蛋白激酶的底物在神经元中富集且似乎对神经元具有特异性。

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Calcium/phospholipid regulates phosphorylation of a Mr "87k" substrate protein in brain synaptosomes.钙/磷脂调节脑突触体中一种分子量为“87k”的底物蛋白的磷酸化。
Proc Natl Acad Sci U S A. 1982 Sep;79(17):5249-53. doi: 10.1073/pnas.79.17.5249.
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2
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J Biol Chem. 1980 Mar 25;255(6):2273-6.
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