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溴氰菊酯对鼠脑蛋白质磷酸化作用的影响
引用本文:姜建成,冷欣夫.溴氰菊酯对鼠脑蛋白质磷酸化作用的影响[J].中国生物化学与分子生物学报,1989,5(5):401-405.
作者姓名:姜建成  冷欣夫
作者单位:中国科学院动物研究所 北京 (姜建成),中国科学院动物研究所 北京(冷欣夫)
摘    要:以小鼠大脑碎片与γ-~(32)P]ATP一起保温,观察到溴氰菊酯对蛋白1—3磷酸化的刺激作用和对4、5磷酸化的抑制作用,表明溴氰菊酯对大脑蛋白质磷酸化产生了影响。从鼠脑分离了C、D、S三个组分,分别进行的蛋白质磷酸化试验结果表明,C、D组分可能是重要的磷酸化部位。 蛋白1、2、3的磷酸化明显地受到溴氰菊酯的刺激,这三个蛋白质可能是“蛋白Ⅲb”的几种形式。溴氰菊酯对“蛋白Ⅲb”磷酸化的刺激,可能会影响神经末梢的神经激素释放,从而影响到与其相关的某些神经功能。

关 键 词:蛋白质磷酸化作用  溴氰菊酯  依赖环腺苷酸的蛋白激酶  “蛋白Ⅲb”  
收稿时间:1989-10-20

Effects of Deltamethrin on Phosphorylation of Mouse Brain Protein
Jiang,Jian-cheng Leng,Xin-fu.Effects of Deltamethrin on Phosphorylation of Mouse Brain Protein[J].Chinese Journal of Biochemistry and Molecular Biology,1989,5(5):401-405.
Authors:Jiang  Jian-cheng Leng  Xin-fu
Institution:(Institute of zoology, Academia Sinica, Beijing
Abstract:This paper reports the effects of deltamethrin on phosphorylation of mouse brain protein by in vitro incubation with (γ-32p) ATP. The phosphoproteins were separated by two-dimensional polyacrylamide-gel electrophoresis and autoradiographed to obtain the phosphorylation pattern. The results showed that protein 1 to 6 were phosphorylated by cyclic AMP-dependent protein kinase, since cyclic AMP stimulated the labelling of these proteins.Addition of deltamethrin into the reaction mixture for phosphorylation of proteins in mouse brain fragments resulted in increased labelling of three proteins (1,2 and 3) and decreased labelling of the other three proteins (4,5 and 6) .The proteins 1 to 3 with molecular weight around 55 kD and isoelectric point at pH7.0-7.5 seem to belong to "protein Ⅲb" which had been identified and proved to be heterogenous on isoeloctric focusing .Stimulating the phosphorylation of "protein Ⅲb" by deltamethrin may affct the release of neurohormones from nerve endings, thereby interfering normal nerve function.Fractions C, D and S were prepared from mouse brain by the method of sucrose density ingradent centrifugation. In experiments with these three fractions, stimulating effects of deltamethrin on the phosphorylation of proteins 1,2 and 3 were de tected in the phosphorylation pattern which were similar to that of the brain fragments, but the amount and labelling intensity of phosphorylated proteins appeared in C and D were larger than that in S respectively, suggesting that C and D were more likely to be the vital sites for protein phosphorylation, and therefore the possible targets for deltamethrin action.
Keywords:Protein phosphorylation Deltamethrin Cyclic AMP dependent protein kinase "Protein Ⅲb"
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