Reactive oxygen species are involved in the activation of cellular phospholipase A2

Vanadate (V) potentiated (4‐ to 10‐fold) the activation of cellular phospholipase A2 (PLA2) induced by H2O2 (H), a phorbol ester (T), a Ca2+‐ionophore (A) and opsonized zymosan in macrophages. V+H induced in intact cells the activation and translocation of PLA2 and protein kinase C(PKC) to the plasm...

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Veröffentlicht in:FEBS letters 1992-09, Vol.309 (2), p.190-192
Hauptverfasser: Goldman, R., Ferber, E., Zort, U.
Format: Artikel
Sprache:eng
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Zusammenfassung:Vanadate (V) potentiated (4‐ to 10‐fold) the activation of cellular phospholipase A2 (PLA2) induced by H2O2 (H), a phorbol ester (T), a Ca2+‐ionophore (A) and opsonized zymosan in macrophages. V+H induced in intact cells the activation and translocation of PLA2 and protein kinase C(PKC) to the plasma membrane. V+H and V+T+A induced strong chemiluminescence (CL) which was abrogated by a specific NADPH oxidase inhibitor diphenylene iodonium (DPI). DPI markedly suppressed the stimulation of PLA2 by V+T+A and V+OZ. The results suggest that the formation of endogenous reactive oxygen species (ROS) is important for PLA2 activation.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(92)81092-Z