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An acetate switch regulates stress erythropoiesis
Journal article   Peer reviewed

An acetate switch regulates stress erythropoiesis

Min Xu, Jason S Nagati, Jian Xie, Jiwen Li, Holly Walters, Young-Ah Moon, Robert D Gerard, Chou-Long Huang, Sarah A Comerford, Robert E Hammer, …
Nature medicine, Vol.20(9), pp.1018-1026
09/2014
DOI: 10.1038/nm.3587
PMCID: PMC4159437
PMID: 25108527
url
https://www.ncbi.nlm.nih.gov/pmc/articles/4159437View
Open Access

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.
Signal Transduction Cell Hypoxia Erythropoiesis Transcription Factors - metabolism Erythropoietin - genetics Animals Acetates - metabolism Stress, Physiological Mice Acetylation

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