SPERMINE STIMULATION OF PHOSPHOPROTEIN DEPHOSPHORYLATION IN THE BRAIN OF MANDUCA-SEXTA

被引：5

作者：

BLOOM, TJ ^{[1
]}

COMBEST, WL ^{[1
]}

GILBERT, LI ^{[1
]}

机构：

[1] UNIV N CAROLINA,DEPT BIOL,CB 3280 COKER HALL,CHAPEL HILL,NC 27599

来源：

INSECT BIOCHEMISTRY | 1990年 / 20卷 / 01期

基金：

美国国家科学基金会;

关键词：

brain; cAMP-dependent protein kinase; dephosphorylation; Manduca sexta; phosphatase; polyamines;

D O I：

10.1016/0020-1790(90)90018-P

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An in vitro analysis of endogenous dephosphorylation of a particulate-associated cAMP-dependent 34 kDa phosphoprotein from the brains of Manduca sexta larvae revealed the presence of phosphatase activity in the same fraction. The rate of dephosphorylation is stimulated by the polyamine spermine, is markedly inhibited by vanadate and Zn2+, and proceeds in the absence of divalent cations. The purified protein inhibitor of phosphatase 1, inhibitor-2, inhibits dephosphorylation in a dose dependent manner. The calmodulin antagonists trifluoperazine and calmidazolium also block dephosphorylation, suggesting the presence of phosphatase 2-B. This study suggests the possible co-localization of a particulate associated cAMP-dependent protein kinase and associated phosphatases with their phosphorylated protein substrates in the insect brain. © 1990.

引用

页码：29 / &

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