Functional crosstalk between phospholipase D2 and signaling phospholipase A2/cyclooxygenase‐2‐mediated prostaglandin biosynthetic pathways

FEBS Letters

Ueno, Noriko¹  Murakami, Makoto¹  Kudo, Ichiro¹ 

[1] Department of Health Chemistry, School of Pharmaceutical Sciences, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan

关键词: Phospholipase A2;    Phospholipase D;    Arachidonic acid;    Prostaglandin;    Cyclooxygenase-2;    PLD;    phospholipase D;    PLA2;    phospholipase A2;    cPLA2;    cytosolic PLA2;    sPLA2;    secretory PLA2;    PLC;    phospholipase C;    AA;    arachidonic acid;    OA;    oleic acid;    COX;    cyclooxygenase;    PG;    prostaglandin;    MAPK;    mitogen-activated protein kinase;    PA;    phosphatidic acid;    DAG;    diacylglycerol;    PIP2;    phosphatidylinositol 4;    5-bisphosphate;    PEt;    phosphatidylethanol;    PMA;    phorbol myristate acetate;    FCS;    fetal calf serum;    IL-1;    interleukin-1;   

DOI  :  10.1016/S0014-5793(00)01691-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We performed reconstitution analyses of functional interaction between phospholipase A₂ (PLA₂) and phospholipase D (PLD) enzymes. Cotransfection of HEK293 cells with cytosolic (cPLA₂) or type IIA secretory (sPLA₂-IIA) PLA₂ and PLD₂, but not PLD₁, led to marked augmentation of stimulus-induced arachidonate release. Interleukin-1-stimulated arachidonate release was accompanied by prostaglandin E₂ production via cyclooxygenase-2, the expression of which was augmented by PLD₂. Conversely, activation of PLD₂, not PLD₁, was facilitated by cPLA₂ or sPLA₂-IIA. Thus, our results revealed functional crosstalk between signaling PLA₂s and PLD₂ in the regulation of various cellular responses in which these enzymes have been implicated.

【 授权许可】

Unknown