Oligodendrocyte adhesion activates protein kinase C-mediated phosphorylation of myelin basic protein.
Oligodendrocyte adhesion activates protein kinase C-mediated phosphorylation of myelin basic protein.
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少突胶质细胞粘附激活蛋白激酶 C 介导的髓磷脂碱性蛋白磷酸化。
DOI：
10.1126/science.2431483
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
Campagnoni,AT
中科院分区：
文献类型：
--
作者：
Vartanian,T;Szuchet,S;Dawson,G;Campagnoni,AT
当分离的成年少突胶质细胞附着在基质上时，就会发生髓鞘形成。对其发生机制的研究表明，少突胶质细胞-基质相互作用(i)激活了蛋白激酶c依赖的髓鞘碱性蛋白磷酸化，（ii）促进了髓鞘碱性蛋白的合成。此外，当激活蛋白激酶C（第二信使二酰基甘油或促进肿瘤的磷脂酯）的药物被添加到非附着的少突胶质细胞中时，它们通过诱导髓鞘碱性蛋白的磷酸化来模拟基质的影响；增加细胞腺苷3′，5′-单磷酸腺苷（环AMP）的试剂抑制髓鞘碱性蛋白的磷酸化。因此，至少在体外，少突胶质细胞和基质之间的相互作用可能介导髓鞘形成事件，髓鞘碱性蛋白的磷酸化可能是最终导致髓鞘形成的一系列步骤的早期要求。
When isolated adult oligodendrocytes adhere to a substratum myelinogenesis occurs. Investigation of the mechanism by which this happens indicated that the oligodendrocyte-substratum interaction (i) activated protein kinase C-dependent phosphorylation of myelin basic protein and (ii) promoted the synthesis of myelin basic protein. In addition, when agents that activate protein kinase C (second messenger diacylglycerol or a tumor-promoting phorbol ester) were added to nonattached oligodendrocytes, they mimicked the influence of the substratum by inducing phosphorylation of myelin basic protein; and reagents that increase cellular adenosine 3′, 5′-monophosphate (cyclic AMP) inhibited phosphorylation of myelin basic protein. Thus, at least in vitro, the interaction between oligodendrocytes and the substratum may mediate myelinogenic events, and phosphorylation of myelin basic protein may be an early requirement in the sequence of steps that ultimately results in myelin formation.