PHOSPHATIDATE-DEPENDENT PROTEIN-PHOSPHORYLATION

被引：174
作者：
BOCCKINO, SB
WILSON, PB
EXTON, JH
机构：
[1] VANDERBILT UNIV,MED CTR,SCH MED,HOWARD HUGHES MED INST LAB,NASHVILLE,TN 37232
[2] VANDERBILT UNIV,MED CTR,SCH MED,DEPT MOLEC PHYSIOL & BIOPHYS,NASHVILLE,TN 37232
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1991年 / 88卷 / 14期
关键词：
D O I：
10.1073/pnas.88.14.6210
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Phosphatidate-dependent protein phosphorylation was observed in soluble extracts from rat liver, brain, lung, and testis. The phosphorylation was stimulated by free Ca2+ in the range of 360-800 nM. Incubation mixtures containing phosphatidate provided markedly different profiles of protein phosphorylation from those with phosphatidylserine plus 1,2-diolein. Phosphatidate-dependent phosphorylation of a 30-kDa protein in the soluble fraction from heart was also observed. This phosphorylation did not require Ca2+. Soluble fractions from liver, testis, brain, and lung phosphorylated the 30-kDa heart protein in a phosphatidate-dependent Ca2+-independent manner. We propose that part of the action of phosphatidate in cells may be mediated by a protein kinase(s).
引用
收藏
页码：6210 / 6213
页数：4
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