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Cloning and characterization of the rat HIF-1 alpha prolyl-4-hydroxylase-1 gene.

Authors: Cobb, Ronald R  McClary, John  Manzana, Warren  Finster, Silke  Larsen, Brent  Blasko, Eric  Pearson, Jennifer  Biancalana, Sara  Kauser, Katalin  Bringmann, Peter  Light, David R  Schirm, Sabine 
Citation: Cobb RR, etal., Protein Expr Purif. 2005 Aug;42(2):295-304. doi: 10.1016/j.pep.2005.03.036.
Pubmed: (View Article at PubMed) PMID:15925519
DOI: Full-text: DOI:10.1016/j.pep.2005.03.036

Prolyl-4-hydroxylase domain-containing enzymes (PHDs) mediate the oxygen-dependent regulation of the heterodimeric transcription factor hypoxia-inducible factor-1 (HIF-1). Under normoxic conditions, one of the subunits of HIF-1, HIF-1alpha, is hydroxylated on specific proline residues to target HIF-1alpha for degradation by the ubiquitin-proteasome pathway. Under hypoxic conditions, the hydroxylation by the PHDs is attenuated by lack of the oxygen substrate, allowing HIF-1 to accumulate, translocate to the nucleus, and mediate HIF-mediated gene transcription. In several mammalian species including humans, three PHDs have been identified. We report here the cloning of a full-length rat cDNA that is highly homologous to the human and murine PHD-1 enzymes and encodes a protein that is 416 amino acids long. Both cDNA and protein are widely expressed in rat tissues and cell types. We demonstrate that purified and crude baculovirus-expressed rat PHD-1 exhibits HIF-1alpha specific prolyl hydroxylase activity with similar substrate affinities and is comparable to human PHD-1 protein.


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CRRD Object Information
CRRD ID: 13602003
Created: 2018-05-26
Species: All species
Last Modified: 2018-05-26
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.