使用一种新方法来寻找蛋白激酶Cδ的底物，从而鉴定出M2型丙酮酸激酶。
Use of a novel method to find substrates of protein kinase C delta identifies M2 pyruvate kinase.
作者信息
Siwko Stefan, Mochly-Rosen Daria
机构信息
Cancer Biology Program, CCSR Room 3145, 269 Campus Dr., Stanford University, Stanford, CA 94305, USA.
出版信息
Int J Biochem Cell Biol. 2007;39(5):978-87. doi: 10.1016/j.biocel.2007.01.018. Epub 2007 Jan 24.
Abstract
Protein kinase C (PKC) family members have been implicated in numerous cellular processes. However, identifying the substrates of each PKC isozyme remains a challenge. Here, we describe a method using two-dimensional (2D) isoelectric focusing gel electrophoresis to identify substrates of delta PKC (deltaPKC) in MCF-7 breast carcinoma cells. We show that M2 pyruvate kinase is a substrate of deltaPKC, and further characterize the interaction between M2 pyruvate kinase and deltaPKC in MCF-7 cells by immunoprecipitation. deltaPKC activation in vitro or in cells did not appear to alter the enzyme activity or polymerization of M2 pyruvate kinase.
摘要
蛋白激酶C（PKC）家族成员参与了众多细胞过程。然而，确定每种PKC同工酶的底物仍然是一项挑战。在此，我们描述了一种使用二维（2D）等电聚焦凝胶电泳来鉴定MCF-7乳腺癌细胞中δ蛋白激酶C（δPKC）底物的方法。我们表明，M2丙酮酸激酶是δPKC的一种底物，并通过免疫沉淀进一步表征了MCF-7细胞中M2丙酮酸激酶与δPKC之间的相互作用。体外或细胞内的δPKC激活似乎并未改变M2丙酮酸激酶的酶活性或聚合作用。
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