An acetate switch regulates stress erythropoiesis

Nat Med. 2014 Sep;20(9):1018-26. doi: 10.1038/nm.3587. Epub 2014 Aug 10.

Abstract

The hormone erythropoietin (EPO), which is synthesized in the kidney or liver of adult mammals, controls erythrocyte production and is regulated by the stress-responsive transcription factor hypoxia-inducible factor-2 (HIF-2). We previously reported that the lysine acetyltransferase CREB-binding protein (CBP) is required for HIF-2α acetylation and efficient HIF-2-dependent EPO induction during hypoxia. We now show that these processes require acetate-dependent acetyl CoA synthetase 2 (ACSS2). In human Hep3B hepatoma cells and in EPO-generating organs of hypoxic or acutely anemic mice, acetate levels rise and ACSS2 is required for HIF-2α acetylation, CBP-HIF-2α complex formation, CBP-HIF-2α recruitment to the EPO enhancer and efficient induction of EPO gene expression. In acutely anemic mice, acetate supplementation augments stress erythropoiesis in an ACSS2-dependent manner. Moreover, in acquired and inherited chronic anemia mouse models, acetate supplementation increases EPO expression and the resting hematocrit. Thus, a mammalian stress-responsive acetate switch controls HIF-2 signaling and EPO induction during pathophysiological states marked by tissue hypoxia.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Acetates / metabolism*
  • Acetylation
  • Animals
  • Cell Hypoxia
  • Erythropoiesis*
  • Erythropoietin / genetics
  • Mice
  • Signal Transduction
  • Stress, Physiological*
  • Transcription Factors / metabolism

Substances

  • Acetates
  • HIF-2 protein, mouse
  • Transcription Factors
  • Erythropoietin