Phospholipase D hydrolyzes ether- and ester-linked glycerophospholipids by different pathways in MDCK cells.
Phospholipase D hydrolyzes ether- and ester-linked glycerophospholipids by different pathways in MDCK cells.
复制标题
磷脂酶 D 在 MDCK 细胞中通过不同途径水解醚连接和酯连接的甘油磷脂。
DOI：
10.1006/bbrc.1995.2221
复制
发表时间：
1995
影响因子：
3.1
通讯作者：
Daniel,LW
中科院分区：
文献类型：
--
作者：
Huang,C;Wykle,RL;Daniel,LW
MDCK cells were prelabeled with 1-O -[3H]hexadecyl-2-lyso-GPC and [14C]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.
