Phospholipase D hydrolyzes ether- and ester-linked glycerophospholipids by different pathways in MDCK cells.
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.
Huang
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Department of Biochemistry, Bowman Gray School of Medicine, Wake Forest University, Winston-Salem, NC 27157-1016, USA.
Wykle
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Daniel
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D000818:Animals; D002460:Cell Line; D004285:Dogs; D004789:Enzyme Activation; D004952:Esters / Q000737:chemistry; D004987:Ethers / Q000737:chemistry; D019204:GTP-Binding Proteins / Q000378:metabolism; D006868:Hydrolysis; D007668:Kidney / Q000166:cytology / Q000378:metabolism; D010712:Phosphatidic Acids / Q000737:chemistry / Q000378:metabolism*; D010739:Phospholipase D / Q000378:metabolism*; D011493:Protein Kinase C / Q000378:metabolism; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D004952:Esters; D004987:Ethers; D010712:Phosphatidic Acids; D011493:Protein Kinase C; D010739:Phospholipase D; D019204:GTP-Binding Proteins; D013755:Tetradecanoylphorbol Acetate