PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHOLIPASE-C IN BOVINE ROD OUTER SEGMENTS

被引:32
|
作者
GEHM, BD [1 ]
MCCONNELL, DG [1 ]
机构
[1] MICHIGAN STATE UNIV, DEPT BIOCHEM, E LANSING, MI 48824 USA
关键词
D O I
10.1021/bi00475a006
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
Preparations of rod outer segments from cattle retinas contained soluble and particulate phospholipase C activities which hydrolyzed phosphatidylinositol 4,5-bisphosphate (PIP2) and the other phosphoinositides. Ca2+ was required for PIP2 hydrolysis, but high (>300 µM) concentrations were inhibitory. Mg2+ and spermine at low concentrations stimulated the particulate activity but inhibited the soluble. Mn2+ inhibited both. High (> 100 µM) concentrations of the nonhydrolyzable GTP analogue guanylyl ß,γ- methylenediphosphonate inhibited PIP2 hydrolysis by both the soluble and particulate activities, but guanosine 5′-O-(3-thiotriphosphate) (GTP7S), fluoride, and cholera and pertussis toxins were without effect. Overall phospholipase C activity in ROS was unaffected by light. Evidence was found for multiple forms of the enzyme, requiring isolation and separate characterization before ruling out regulation by light or G-protein. © 1990, American Chemical Society.
引用
收藏
页码:5447 / 5452
页数:6
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