Title : Evidence that inhibition of phorbol ester-induced superoxide anion formation by cyclosporin A in phagocytes is not mediated by direct inhibition of protein kinase C.

Pub. Date : 1994 Aug 30

PMID : 8093097






3 Functional Relationships(s)
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1 Evidence that inhibition of phorbol ester-induced superoxide anion formation by cyclosporin A in phagocytes is not mediated by direct inhibition of protein kinase C. Cyclosporin A (CsA) has been reported to inhibit phorbol myristate acetate (PMA)-induced superoxide anion (O2-) formation in human neutrophils and murine macrophages. Tetradecanoylphorbol Acetate ERCC excision repair 8, CSA ubiquitin ligase complex subunit Homo sapiens
2 Evidence that inhibition of phorbol ester-induced superoxide anion formation by cyclosporin A in phagocytes is not mediated by direct inhibition of protein kinase C. Cyclosporin A (CsA) has been reported to inhibit phorbol myristate acetate (PMA)-induced superoxide anion (O2-) formation in human neutrophils and murine macrophages. Tetradecanoylphorbol Acetate ERCC excision repair 8, CSA ubiquitin ligase complex subunit Homo sapiens
3 We found that CsA inhibited O2- formation in HL-60 cells induced by PMA (30 nM) and phorbol dibutyrate (200 nM) with a half-maximal effect at 1 and 0.75 microM, respectively. Tetradecanoylphorbol Acetate ERCC excision repair 8, CSA ubiquitin ligase complex subunit Homo sapiens