STRETCH ACTIVATES MYOSIN LIGHT CHAIN KINASE IN ARTERIAL SMOOTH-MUSCLE

被引:24
作者
BARANY, K [1 ]
ROKOLYA, A [1 ]
BARANY, M [1 ]
机构
[1] UNIV ILLINOIS,COLL MED,DEPT BIOCHEM,CHICAGO,IL 60612
关键词
D O I
10.1016/S0006-291X(05)81036-8
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
Stretching of porcine carotid arterial muscle increased the phosphorylation of the 20 kDa myosin light chain from 0.23 to 0.68 mol [32P]phrophate/mol light chain, wheareas stretching of phorbol dibutyrate treated muscle increased the phosphorylation from 0.30 to 0.91 mol/mol. Two-dimensional gel electrophoresis followed by two-dimensional tryptic phosphopeptide mapping was used to identify the enzyme involved in the stretch-induced phosphorylation. Quantitation of the [32P]phosphate content of the peptides revaled considerable light chain phosphorylation by protein kinase C only in the phorbol dibutyrate treated arterial muscle, whereas most of the light chain phosphorylation was attributable to myosin light chain kinase. Upon stretch of either the untreated or treated muscle, the total increment in [32P]phosphate incorporation into the light chain could be accounted for by peptides characteristic for myosin light chain kinase catalyzed phosphorylation, demonstrating that the stretch-induced phosphorylation is caused by this enzyme exclusively. © 1990 Academic Press, Inc.
引用
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页码:164 / 171
页数:8
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