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Diacylglycerols and mezerein activate neutrophils by a phorbol myristate acetate‐like mechanism
Author(s) -
O'Flaherty Joseph T.,
Redman Jimmy F.,
McCall Charles E.,
Wykle Robert L.,
Schmitt Jeffery D.
Publication year - 1985
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041250204
Subject(s) - phorbol , protein kinase c , cytochalasin b , chemistry , receptor , extracellular , biochemistry , diacylglycerol kinase , agonist , calcium , microbiology and biotechnology , biology , signal transduction , in vitro , organic chemistry
rac ‐1‐ O ‐Myristoyl‐2‐O‐acetylglycerol, rac ‐1‐ O ‐palmitoyl‐2‐O‐acetylglycerol, and rac ‐1‐ O ‐oleoyl‐2‐ O ‐acetylglycerol acted like phorbol myristate acetate and mezerein in stimulating human neutrophil aggregation. Responses to these agents were equally influenced by cytochalasin B, extracellular calcium and magnesium, arachidonate antimetabolites, and procedures that rendered the cells desensitized to other agonists. The compounds also inhibited the binding of [ 3 H]‐phorobol myristate acetate to its receptor on neutrophils. Thus, these agents are biologically homologous. They act by binding to a common receptor. This receptor may function physiologically as a transducer for endogenous glycerides that form in cells challenged by other stimuli.