Selective activation of phospholipase D2 by unsaturated fatty acid

FEBS Letters

Arnold, Rebecca S.¹  Kim, Yong²  Kim, Jae Ho²  Lee, Sang Do²  Lopez, Isabel¹  Ryu, Sung Ho²  Lambeth, J.David¹  Suh, Pann-Ghill² 

[1] Department of Biochemistry, Emory University Medical School, Atlanta, GA 30322, USA;Department of Life Science and School of Environmental Engineering, Pohang University of Science and Technology, Pohang 790-784, South Korea

关键词: Phospholipase D2;    Oleic acid;    Phosphatidylinositol 4;    5-bisphosphate;    PLD;    phospholipase D;    PIP2;    phosphatidylinositol 4;    5-bisphosphate;    PC;    phosphatidylcholine;    PA;    phosphatidic acid;    ARF;    ADP-ribosylation factor;    PKC;    protein kinase C;    PE;    phosphatidylethanolamine;    PS;    phosphatidylserine;    PI;    phosphatidylinositol;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    GTPγS;    guanosine 5′-O-(3-thiotriphosphate);    ECL;    enhanced chemiluminescence;   

DOI  :  10.1016/S0014-5793(99)00745-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Although oleate has been implicated in the regulation of phospholipase D (PLD) activity, the molecular identity of the oleate-stimulated PLD is still poorly understood. We now report that oleate selectively stimulates the enzymatic activity of PLD2 but not of PLD1, with an optimal concentration of 20 μM in vitro. Intriguingly, phosphatidylinositol 4,5-bisphosphate (PIP₂) synergistically stimulates the oleate-dependent PLD2 activity with an optimal concentration of 2.5 μM. These results provide the first evidence that oleate is a PLD2-specific activating factor and PLD2 activity is synergistically stimulated by oleate and PIP₂.

【 授权许可】

Unknown