Possible role of endogenous histamine in mediation of LPS-induced secretion of corticosterone in mice.
Escherichia coli lipopolysaccharide (LPS) induced a strong secretion of corticosterone in C3H/HeN mice with a concomitant increase in the splenic histidine decarboxylase activity. Treatment of the mice with alpha-fluoromethyl histidine, a suicide substrate for the enzyme, markedly attenuated both the secretion and the increase. In C3H/HeJ mice, LPS provoked little corticosterone release and induction of the enzyme. However, these mice responded to tetradecanoyl phorbol acetate with a large increase in both this secretion and enzyme activity. Injection of LPS produced a comparable increase in the serum histamine and corticosterone level and activity of histidine decarboxylase in various tissues of genetically mast-cell-deficient W/WV mice and in closely related +/+ mice. These results suggest that secretion of corticosterone caused by LPS is mediated by histamine produced through induction of histidine decarboxylase in non-mast cells.
D000818:Animals; D003345:Corticosterone / Q000097:blood*; D006632:Histamine / Q000097:blood / Q000502:physiology*; D006640:Histidine Decarboxylase / Q000378:metabolism; D008070:Lipopolysaccharides / Q000494:pharmacology*; D008762:Methylhistidines / Q000494:pharmacology; D051379:Mice; D008809:Mice, Inbred C3H; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D008070:Lipopolysaccharides; D008762:Methylhistidines; C028309:alpha-fluoromethylhistidine; D006632:Histamine; D006640:Histidine Decarboxylase; D013755:Tetradecanoylphorbol Acetate; D003345:Corticosterone