Reductive glutamine metabolism by IDH1 mediates lipogenesis under hypoxia View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2012-01

AUTHORS

Christian M. Metallo, Paulo A. Gameiro, Eric L. Bell, Katherine R. Mattaini, Juanjuan Yang, Karsten Hiller, Christopher M. Jewell, Zachary R. Johnson, Darrell J. Irvine, Leonard Guarente, Joanne K. Kelleher, Matthew G. Vander Heiden, Othon Iliopoulos, Gregory Stephanopoulos

ABSTRACT

Acetyl coenzyme A (AcCoA) is the central biosynthetic precursor for fatty-acid synthesis and protein acetylation. In the conventional view of mammalian cell metabolism, AcCoA is primarily generated from glucose-derived pyruvate through the citrate shuttle and ATP citrate lyase in the cytosol. However, proliferating cells that exhibit aerobic glycolysis and those exposed to hypoxia convert glucose to lactate at near-stoichiometric levels, directing glucose carbon away from the tricarboxylic acid cycle and fatty-acid synthesis. Although glutamine is consumed at levels exceeding that required for nitrogen biosynthesis, the regulation and use of glutamine metabolism in hypoxic cells is not well understood. Here we show that human cells use reductive metabolism of α-ketoglutarate to synthesize AcCoA for lipid synthesis. This isocitrate dehydrogenase-1 (IDH1)-dependent pathway is active in most cell lines under normal culture conditions, but cells grown under hypoxia rely almost exclusively on the reductive carboxylation of glutamine-derived α-ketoglutarate for de novo lipogenesis. Furthermore, renal cell lines deficient in the von Hippel-Lindau tumour suppressor protein preferentially use reductive glutamine metabolism for lipid biosynthesis even at normal oxygen levels. These results identify a critical role for oxygen in regulating carbon use to produce AcCoA and support lipid synthesis in mammalian cells. More... »

PAGES

380

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature10602

DOI

http://dx.doi.org/10.1038/nature10602

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1053544093

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/22101433


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