Succinate is an inflammatory signal that induces IL-1 beta through HIF-1 alpha
Details
Publication Year 2013-04-11,Volume 496,Issue #7444,Page 238-242
Journal Title
NATURE
Publication Type
Journal Article
Abstract
Macrophages activated by the Gram-negative bacterial product lipopolysaccharide switch their core metabolism from oxidative phosphorylation to glycolysis(1). Here we show that inhibition of glycolysis with 2-deoxyglucose suppresses lipopolysaccharide-induced interleukin-1 beta but not tumour-necrosis factor-a in mouse macrophages. A comprehensive metabolic map of lipopolysaccharide-activated macrophages shows upregulation of glycolytic and down-regulation of mitochondrial genes, which correlates directly with the expression profiles of altered metabolites. Lipopolysaccharide strongly increases the levels of the tricarboxylic-acid cycle intermediate succinate. Glutamine-dependent anerplerosis is the principal source of succinate, although the 'GABA (gamma-aminobutyric acid) shunt' pathway also has a role. Lipopolysaccharide-induced succinate stabilizes hypoxia-inducible factor-1 alpha, an effect that is inhibited by 2-deoxyglucose, with interleukin-1 beta as an important target. Lipopolysaccharide also increases succinylation of several proteins. We therefore identify succinate as a metabolite in innate immune signalling, which enhances interleukin-1 beta production during inflammation.
Publisher
NATURE PUBLISHING GROUP
Keywords
RECEPTOR GPR91; HYPOXIA; ACTIVATION; PROTEIN; CELLS; GAMMA; LINKS; METABOLISM; INHIBITION; MECHANISM
Research Division(s)
Inflammation
Terms of Use/Rights Notice
© 2013 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.


Creation Date: 2013-04-11 12:00:00
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