Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension.
- 6 June 1995
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 92 (12), 5510-5514
- https://doi.org/10.1073/pnas.92.12.5510
Abstract
Hypoxia-inducible factor 1 (HIF-1) is found in mammalian cells cultured under reduced O2 tension and is necessary for transcriptional activation mediated by the erythropoietin gene enhancer in hypoxic cells. We show that both HIF-1 subunits are basic-helix-loop-helix proteins containing a PAS domain, defined by its presence in the Drosophila Per and Sim proteins and in the mammalian ARNT and AHR proteins. HIF-1 alpha is most closely related to Sim. HIF-1 beta is a series of ARNT gene products, which can thus heterodimerize with either HIF-1 alpha or AHR. HIF-1 alpha and HIF-1 beta (ARNT) RNA and protein levels were induced in cells exposed to 1% O2 and decayed rapidly upon return of the cells to 20% O2, consistent with the role of HIF-1 as a mediator of transcriptional responses to hypoxia.Keywords
This publication has 36 references indexed in Scilit:
- Purification and Characterization of Hypoxia-inducible Factor 1Journal of Biological Chemistry, 1995
- A molecular inventory of human pancreatic islets: sequence analysis of 1000 cDNA clonesHuman Molecular Genetics, 1993
- Vascular endothelial growth factor induced by hypoxia may mediate hypoxia-initiated angiogenesisNature, 1992
- Cloning of a Factor Required for Activity of the Ah (Dioxin) ReceptorScience, 1991
- Basic local alignment search toolJournal of Molecular Biology, 1990
- Regulation of the Erythropoietin Gene: Evidence That the Oxygen Sensor Is a Heme ProteinScience, 1988
- A family of unusually spliced biologically active transcripts encoded by a Drosophila clock geneNature, 1987
- A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradationCell, 1986
- Synthetic oligonucleotide probes deduced from amino acid sequence dataJournal of Molecular Biology, 1985
- Short‐term modulation of glycogen metabolism, glycolysis and gluconeogenesis by physiological oxygen concentrations in hepatocyte culturesEuropean Journal of Biochemistry, 1983