Lipid structure and Ca2+-ATPase function

被引:28
作者
Lee, AG [1 ]
Dalton, KA [1 ]
Duggleby, RC [1 ]
East, JM [1 ]
Starling, AP [1 ]
机构
[1] UNIV SOUTHAMPTON, INST BIOMOLEC SCI, SOUTHAMPTON SO9 3TU, HANTS, ENGLAND
基金
英国惠康基金;
关键词
ATPase; calcium; phospholipid;
D O I
10.1007/BF01788361
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
Effects of lipid structure on the function of the Ca2+-ATPase of skeletal muscle of sarcoplasmic reticulum are reviewed. Binding of phospholipids to the ATPase shows little specificity. Phosphatidylcholines with short (C14) or long (C24) fatty acyl chains have marked effects on the activity of the ATPase, including a change in the stoichiometry of Ca binding. Low ATPase activity in gel phase lipid follows from low rate of phosphorylation. Phosphatidylinositol 4-phosphate increases ATPase activity by increasing the rate of dephosphorylation of the phosphorylated ATPase. Stimulation is not seen with other anionic phospholipids; phosphatidic acid decreases ATPase activity in a Mg2+-dependent manner.
引用
收藏
页码:289 / 298
页数:10
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