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Hypoxia-inducible factors (HIFs) are transcription factors that respond to decreases in available oxygen in the cellular environment, or hypoxia. [ 1 ] [ 2 ] They also respond to instances of pseudohypoxia , such as thiamine deficiency.
n/a n/a Ensembl n/a n/a UniProt n a n/a RefSeq (mRNA) n/a n/a RefSeq (protein) n/a n/a Location (UCSC) n/a n/a PubMed search n/a n/a Wikidata View/Edit Human Erythropoietin (/ ɪ ˌ r ɪ θ r oʊ ˈ p ɔɪ. ɪ t ɪ n, - r ə -, - p ɔɪ ˈ ɛ t ɪ n, - ˈ iː t ɪ n / ; EPO), also known as erythropoetin, haematopoietin, or haemopoietin, is a glycoprotein cytokine secreted mainly by the kidneys ...
Hypoxia-inducible factor 1-alpha, also known as HIF-1-alpha, is a subunit of a heterodimeric transcription factor hypoxia-inducible factor 1 that is encoded by the HIF1A gene. [ 5 ] [ 6 ] [ 7 ] The Nobel Prize in Physiology or Medicine 2019 was awarded for the discovery of HIF.
Endothelial PAS domain-containing protein 1 (EPAS1, also known as hypoxia-inducible factor-2alpha (HIF-2α)) is a protein that is encoded by the EPAS1 gene in mammals. It is a type of hypoxia-inducible factor, a group of transcription factors involved in the physiological response to oxygen concentration.
Hypoxia differs from hypoxemia and anoxemia, in that hypoxia refers to a state in which oxygen present in a tissue or the whole body is insufficient, whereas hypoxemia and anoxemia refer specifically to states that have low or no oxygen in the blood. [3] Hypoxia in which there is complete absence of oxygen supply is referred to as anoxia.
From 2000 to 2006, EPO tests at the Olympics were conducted on both blood and urine. [30] [31] However, several compounds have been identified that can be taken orally to stimulate endogenous EPO production. Most of the compounds stabilize the hypoxia-inducible transcription factors which activate the EPO gene. The compounds include oxo ...
Hypoxia-inducible factor (HIF) is an evolutionarily conserved transcription factor [7] that allows the cell to respond physiologically to low concentrations of oxygen. [8] A class of prolyl hydroxylases which act specifically on HIF has been identified; [ 9 ] hydroxylation of HIF allows the protein to be targeted for degradation. [ 9 ]
The alpha-3 subunit lacks the transactivation domain found in factors containing either the alpha-1 or alpha-2 subunits. It is thought that factors containing the alpha-3 subunit are negative regulators of hypoxia-inducible gene expression. At least three transcript variants encoding three different isoforms have been found for this gene. [7]