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从胎鼠脑部分离出的神经生长锥。III. 钙依赖性蛋白磷酸化。

Nerve growth cones isolated from fetal rat brain. III. Calcium-dependent protein phosphorylation.

作者信息

Katz F, Ellis L, Pfenninger K H

出版信息

J Neurosci. 1985 Jun;5(6):1402-11. doi: 10.1523/JNEUROSCI.05-06-01402.1985.

Abstract

Calcium-dependent protein kinase activities have been studied in nerve growth cone particles (GCPs) and compared with those of synaptosomes. GCPs contain a set of phosphoproteins qualitatively similar to that of synaptic nerve terminals. However, major quantitative differences appear to exist: whereas synapsin I phosphorylation is relatively weak, the major kinase substrates of GCPs are a 46,000-dalton membrane protein (calcium/calmodulin dependent) and two acidic proteins of 80,000 and 40,000 daltons, phosphorylated by a calcium/phospholipid-dependent protein kinase. The presence of synaptic kinase activities in GCPs is consistent with their neuronal origin. The role of these kinases in GCPs is not understood at present. They may be involved in growth-related functions and/or may prepare the sprouting neuron for synaptic function.

摘要

已对神经生长锥颗粒(GCPs)中的钙依赖性蛋白激酶活性进行了研究,并与突触体的钙依赖性蛋白激酶活性进行了比较。GCPs含有一组磷蛋白,其性质与突触神经末梢的磷蛋白相似。然而,似乎存在主要的数量差异:突触素I的磷酸化相对较弱,而GCPs的主要激酶底物是一种46,000道尔顿的膜蛋白(钙/钙调蛋白依赖性)和两种80,000和40,000道尔顿的酸性蛋白,它们由钙/磷脂依赖性蛋白激酶磷酸化。GCPs中存在突触激酶活性与其神经元起源一致。目前尚不清楚这些激酶在GCPs中的作用。它们可能参与与生长相关的功能和/或可能使发芽的神经元为突触功能做好准备。

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