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Triphenyltin chloride inhibits superoxide production by human neutrophils stimulated with a surface active agent
Author(s) -
Matsui Hisao,
Wada Osamu,
Ushijima Yoshio,
Akuzawa Takafumi
Publication year - 1983
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 - 10.1016/0014-5793(83)80296-8
Subject(s) - superoxide , xanthine oxidase , chemistry , biochemistry , nadph oxidase , xanthine , oxidase test , chloride , superoxide dismutase , phorbol , respiratory burst , enzyme , microbiology and biotechnology , protein kinase c , biology , organic chemistry
Treatment of human neutrophils with triphenyltin chloride (TPTCl)‐inhibited superoxide (O − 2 ) production stimulated with phorbol myristate acetate (PMA). TPTCl was more potent as inhibitor of O − 2 production than other phenyltin compounds. The O − 2 production by the xanthine oxidase—acetaldehyde system was not inhibited by TPTCl. This finding indicates that TPTCl does not itself react with O − 2 . Furthermore, TPTCl did not influence the isolated NADPH oxidase at all, though O − 2 production of neutrophils stimulated with PMA in the presence of TPTCl was inhibited. These results indicate that TPTCl inhibits the activation process of the O − 2 generating system.