Involvement of vicinal dithiols in differential regulation of fMLP and phorbol ester-activated phospholipase D in stimulated human neutrophils.
In the human neutrophil, the fMLP-activated phospholipase D (PLD) was entirely calcium and tyrosine kinase dependent, but protein kinase C independent. An opposite regulation was observed with phorbol ester PMA, since the phospholipase D activity was mostly calcium insensitive, tyrosine kinase independent, but protein kinase C dependent. The arsenical compound, phenylarsine oxide (PAO), which reacts with vicinal sulhydryl groups, activated twofold at one minute the PMA stimulated-PLD activity, whereas it inhibited half of the fMLP-activated PLD after a time lag of 30 sec. Our data indicate that PAO acted on a mechanism regulating the balance between fMLP-activated and PMA-activated phospholipase D activity. Noteworthy, PAO similarly inhibited fMLP and PMA-induced O2(-)-production.
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INSERM Unité 326, Phospholipides Membranaires, Signalisation Cellulaire et Lipoprotéines, Hôpital Purpan, Toulouse, France.
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D001152:Arsenicals / Q000737:chemistry*; D002118:Calcium / Q000502:physiology; D002478:Cells, Cultured; D004789:Enzyme Activation / Q000187:drug effects; D006801:Humans; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000494:pharmacology*; D009504:Neutrophils / Q000201:enzymology*; D010739:Phospholipase D / Q000378:metabolism*; D011493:Protein Kinase C / Q000502:physiology; D011505:Protein-Tyrosine Kinases / Q000502:physiology; D016897:Respiratory Burst / Q000187:drug effects; D015398:Signal Transduction; D013481:Superoxides / Q000378:metabolism; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D001152:Arsenicals; C029341:oxophenylarsine; D013481:Superoxides; D009240:N-Formylmethionine Leucyl-Phenylalanine; D011505:Protein-Tyrosine Kinases; D011493:Protein Kinase C; D010739:Phospholipase D; D013755:Tetradecanoylphorbol Acetate; D002118:Calcium