Role of secretory and cytosolic phospholipase A2 enzymes in lysophosphatidylcholine‐stimulated monocyte arachidonic acid release

FEBS Letters

Oestvang, Janne¹  Anthonsen, Marit W.¹  Johansen, Berit¹ 

[1] Department of Biology, Section on Molecular Biology and Biotechnology, Norwegian University of Science and Technology, N-7491 Trondheim, Norway

关键词: Phospholipase A2;    Lysophosphatidylcholine;    Atherosclerosis;    Arachidonic acid;    THP-1;    Mono Mac6;    lysoPC;    lysophosphatidylcholine;    PLA2;    phospholipase A2;    cPLA2;    cytosolic PLA2;    sPLA2;    secretory PLA2;    AA;    arachidonic acid;    LDL;    low density lipoprotein;    oxLDL;    oxidized LDL;    PAF;    platelet-activating factor;    iPLA2;    calcium-independent PLA2;    PMA;    4β-phorbol 12-myristate 13-acetate;    MTT;    3-(4;    5-dimethylthiazol-2-yl)-2;    5-difenyl tetrazolium bromide;    MAFP;    methyl arachidonyl fluorophosphate;    BEL;    bromoenol lactone;    OA;    oleic acid;    PTX;    pertussis toxin;    PAP;    phosphatidic acid phosphohydrolase;    BSA;    fatty acid-free bovine serum albumin;   

DOI  :  10.1016/S0014-5793(03)01242-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To determine if lysophosphatidylcholine (lysoPC) is able to induce proinflammatory changes in monocytes, its ability to stimulate arachidonic acid (AA) release, a product of phospholipase A2 (PLA₂) activity, has been analyzed. LysoPC increased AA release in THP-1 and Mono Mac6 cells in a time- and concentration-dependent manner. The monocytes expressed both secretory and cytosolic PLA₂ enzymes and AA release was strongly reduced by cellular pretreatment with different PLA₂ inhibitors and by pertussis toxin, an inhibitor of G_i-protein activation. This indicates that both cytosolic and secretory PLA₂ enzymes regulate specific lysoPC receptor-induced AA release, suggesting lysoPC participation in monocyte proinflammatory activation.

【 授权许可】

Unknown