PHOSPHOLIPASE-D HYDROLYZES ETHER-LINKED AND ESTER-LINKED GLYCEROPHOSPHOLIPIDS BY DIFFERENT PATHWAYS IN MDCK CELLS

被引：7

作者：

HUANG, CF ^{[1
]}

WYKLE, RL ^{[1
]}

DANIEL, LW ^{[1
]}

机构：

[1] WAKE FOREST UNIV,BOWMAN GRAY SCH MED,DEPT BIOCHEM,WINSTON SALEM,NC 27157

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 213卷 / 03期

关键词：

D O I：

10.1006/bbrc.1995.2221

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：

MDCK cells were prelabeled with 1-($) under bar O-[H-3]hexadecyl-2-lyso-GPC and [C-14]myristic acid, which selectively labeled the glycerophospholipid subclasses with 93% of tritium in the alkyl-linked subclass and 85% of carbon-14 in the diacyl-linked subclass. By this approach, we have demonstrated that PLD upon activation via PKC pathway selectively catalyzes the degradation of ether-linked glycerophospholipid subclass. In contrast, G-protein regulatory PLD activity seems to preferentially hydrolyze ester-linked subclass. These results suggest that the selective hydrolysis of PLD action may play an important role in cellular signal transduction under physiological and pathological conditions. (C) 1995 Academic Press. Inc.

引用

页码：950 / 957

页数：8

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