ZINC INHIBITION OF CALMODULIN - PROPOSED MOLECULAR MECHANISM OF ZINC ACTION ON CELLULAR FUNCTIONS

被引:92
作者
BREWER, GJ
ASTER, JC
KNUTSEN, CA
KRUCKEBERG, WC
机构
[1] Department of Human Genetics, University of Michigan Medical School, Ann Arbor
[2] The University of Mississippi Medical School, Jackson
关键词
calcium adenosine triphosphatase (Ca‐ATPase); calmodulin; erythrocyte membrane; zinc;
D O I
10.1002/ajh.2830070107
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
Calcium stimulates, and zinc inhibits, a wide variety of cell types. In the erythrocyte, we have found calcium and zinc to have antagonistic actions in a variety of systems. An important mechanism for calcium effects on cells is activation of calmodulin. Calmodulin is a small ubiquitous protein which, when activated by calcium, has a large array of cellular regulatory functions. We now report that calmodulin function is inhibited by low concentrations of zinc. Zinc inhibition of calmodulin provides a rational molecular mechanism for the diverse cellular inhibitory effects of zinc, as well as for zinc's antagonism of calcium effects. Copyright © 1979 Wiley‐Liss, Inc., A Wiley Company
引用
收藏
页码:53 / 60
页数:8
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