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Role of secretory and cytosolic phospholipase A 2 enzymes in lysophosphatidylcholine‐stimulated monocyte arachidonic acid release
Author(s) -
Oestvang Janne,
Anthonsen Marit W.,
Johansen Berit
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01242-0
Subject(s) - lysophosphatidylcholine , phospholipase a2 , cytosol , arachidonic acid , proinflammatory cytokine , pertussis toxin , phospholipase a , enzyme , monocyte , chemistry , biochemistry , phospholipase , lipid signaling , lysophosphatidic acid , receptor , biology , inflammation , phosphatidylcholine , g protein , phospholipid , immunology , membrane
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 (PLA 2 ) 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 PLA 2 enzymes and AA release was strongly reduced by cellular pretreatment with different PLA 2 inhibitors and by pertussis toxin, an inhibitor of G i ‐protein activation. This indicates that both cytosolic and secretory PLA 2 enzymes regulate specific lysoPC receptor‐induced AA release, suggesting lysoPC participation in monocyte proinflammatory activation.