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Suppression of Phorbol Myristate Acetate‐Triggering of Macrophage H 2 O 2 Release by Sarcoma 180 Originating Factor
Author(s) -
Tomioka Haruaki,
Saito Hajime
Publication year - 1985
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1985.tb00900.x
Subject(s) - phorbol , macrophage , biology , microbiology and biotechnology , tetradecanoylphorbol acetate , phagocytosis , biochemistry , protein kinase c , immunology , phosphorylation , in vitro
A high molecular weight proteinaceous factor in the cell extract of sarcoma 180 (S‐180) was found to inhibit phorbol myristate acetate (PMA)‐triggering of macrophage H 2 O 2 release. This factor (S‐180 factor) was stable at 56 C for 1 hr and resistant to ultraviolet‐irradiation. The S‐180 factor inhibited the specific binding of PMA to macrophages and this was accompanied by a parallel reduction of PMA‐triggered H 2 O 2 release. S‐180 factor preferentially depressed macrophage H 2 O 2 release in response to phorbol diesters including PMA, 4β‐phorbol 12β,13α‐diacetate, 4β‐phorbol 12β,13α‐didecanoate, 4β‐phorbol 12β,13α‐dibenzoate, and 4‐ o ‐methyl‐PMA rather than the H 2 O 2 release triggered by wheat germ aggulutinin or by phagocytosis of latex particles. The S‐180 factor failed to affect the PMA‐elicited macrophage cell spreading and macrophage phagocytic activity against latex beads with or without PMA‐mediated stimulation. A similar inhibitory factor was found in the extracts of some other murine tumor cells (Ehrlich carcinoma and thymic leukemia) and normal cells (liver, spleen, and peritoneal exudate cells).