Neuron-specific protein F1/GAP-43 shows substrate specificity for the beta subtype of protein kinase C.
Neuron-specific protein F1/GAP-43 shows substrate specificity for the beta subtype of protein kinase C.
复制标题
神经元特异性蛋白 F1/GAP-43 对蛋白激酶 C 的 β 亚型具有底物特异性。
DOI：
10.1016/0006-291x(90)90818-8
复制
发表时间：
1990
影响因子：
3.1
通讯作者：
Routtenberg,A
中科院分区：
文献类型：
--
作者：
Sheu,FS;Marais,RM;Parker,PJ;Bazan,NG;Routtenberg,A
我们确定了与长时程增强(LTP)有关的β或伽马蛋白激酶C(PKC)亚型是否选择性地调节蛋白F1的磷酸化。测定了纯化的牛PKC亚型和经磷脂酰丝氨酸(PS)和钙激活的重组PKC亚型对纯化的大鼠蛋白F1的相对磷酸化能力。GAP-43)。在与组蛋白的酶活性持平后，重组的BetaII PKC对蛋白质F1的磷酸化程度是重组Gamma PKC的6倍。牛β-PKC磷酸化蛋白F1的程度是牛-γ-PKC的3倍。即使当PS被脂氧素B4取代时，βPKC在磷酸化蛋白F1中的作用仍优于伽马PKC。结合以往的脑细胞研究显示，β-PKC和蛋白F1的mRNA表达水平平行，本研究结果表明，在突触可塑性的发育过程中，β-PKC调节蛋白F1的磷酸化。
We determined whether the beta or gamma protein kinase C (PKC) subtypes implicated in long-term potentiation (LTP) selectively regulates protein F1 phosphorylation. Purified bovine PKC subtypes and recombinant PKC subtypes activated by phosphatidylserine (PS) and calcium were tested for their relative ability to phosphorylate purified rat protein F1 (a.k.a. GAP-43). After equalizing enzyme activity against histone, the recombinant betaII PKC phosphorylated protein F1 to a 6 fold greater extent than the recombinant gamma PKC. Bovine betaI PKC phosphorylated protein F1 to a 3 fold greater extent than bovine gamma PKC. Even when PS was replaced by lipoxin B4, which can selectively increase gamma PKC activity, betaI PKC was still superior to gamma PKC in phosphorylating protein F1. Taken together with previous cellular studies of brain showing parallel levels of expression of beta PKC mRNA and protein F1 mRNA, the present results make it attractive to propose that beta PKC regulates protein F1 phosphorylation during the development of synaptic plasticity.