کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10843499 | 1069262 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Cloning and characterization of the rat HIF-1α prolyl-4-hydroxylase-1 gene
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Cloning and characterization of the rat HIF-1α prolyl-4-hydroxylase-1 gene Cloning and characterization of the rat HIF-1α prolyl-4-hydroxylase-1 gene](/preview/png/10843499.png)
چکیده انگلیسی
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-1α, is hydroxylated on specific proline residues to target HIF-1α 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-1α specific prolyl hydroxylase activity with similar substrate affinities and is comparable to human PHD-1 protein.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 42, Issue 2, August 2005, Pages 295-304
Journal: Protein Expression and Purification - Volume 42, Issue 2, August 2005, Pages 295-304
نویسندگان
Ronald R. Cobb, John McClary, Warren Manzana, Silke Finster, Brent Larsen, Eric Blasko, Jennifer Pearson, Sara Biancalana, Katalin Kauser, Peter Bringmann, David R. Light, Sabine Schirm,