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Title[redir]:
Cyclosporin A prevents the hypoxic ... | Article | H1 Connect
Description:
The mechanism by which hypoxia induces gene transcription involves the inhibition of hypoxia-inducible factor (HIF)-1alpha prolyl hydroxylase activity, whi

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finding, latest, recommendation, hydroxylation, hif, hypoxiainducible, apr, hifalpha, expression, prolyl, faculty, hypoxic, mar, factor, proline, complex, control, gene, phd, nov, cyclosporin, factoralpha, ronald, conaway, authors, findings, oxygen, sensing, biology, feb, ueli, schibler, hydroxylases, oct, sep, patrick, ofarrell, protein, interacts, vhl, oxygendependent, degradation, alpha, aug, hippellindau, opinions, collections, reviews, connecting, world,

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hypoxia-inducible transcription factor hypoxia-inducible factor-1alpha hypoxia-inducible factor 1alpha ph-dependent nucleolar sequestration oxygen-dependent degradation domains promote oxygen-dependent degradation o2-regulated prolyl hydroxylation hif-1alpha -pvhl complex hypoxia-inducible genes intracellular oxygen concentration proline hydroxylation motif promoting proline hydroxylation finding sequence determinants finding hifalpha targeted finding coordinate regulation previous studies suggested oxygen sensing mechanism rna polymerase ii finding hif activation finding os-9 interacts prolyl hydroxylases phd1 hif transactivation domain hif-1 transcriptional activity authors' findings suggest vhl-mediated destruction proline hydroxylation faculty opinions hif-1alpha o2 sensing h1 company finding fih-1 finding targeting finding structure prolyl hydroxylases hif-alpha authors' findings protein prolyl hydroxylase expression regulates hif doctors search hypoxic adaptation d'angelo biological chemistry m211293200 pmid paper reports block induction hypoxic cells depend simply previously appreciated

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ScholarlyArticle:
      context:https://schema.org
      headline:Cyclosporin A prevents the hypoxic adaptation by activating hypoxia-inducible factor-1alpha Pro-564 hydroxylation.
      abstract:The mechanism by which hypoxia induces gene transcription involves the inhibition of hypoxia-inducible factor (HIF)-1alpha prolyl hydroxylase activity, which prevents von Hippel-Lindau (vHL)-dependent targeting of HIF-1alpha to the ubiquitin-proteasome pathway. HIF-1alpha is stabilized, translocates to the nucleus, interacts with hypoxia-responsive elements, and promotes the activation of target genes. This report shows that cyclosporin A (CsA) interferes with the hypoxic signaling cascade in C6 glioma cells. CsA inhibits hypoxia-dependent gene transcription in a reporter gene assay and prevents the hypoxic accumulation of HIF-1alpha. Addition of the 530-603 C-terminal oxygen-dependent degradation (ODD) domain of HIF-1alpha to the green fluorescent protein (GFP) destabilized the protein in an oxygen-dependent manner. CsA prevented the hypoxic stabilization of an ODD.GFP fusion protein. An assay for 2-oxoglutarate-dependent dioxygenases was developed using a light mitochondrial kidney fraction as a source of enzyme. It uses the capacity of specific peptides to stimulate the degradation of [(14)C]2-oxoglutarate. CsA stimulated the enzymatic activity in the presence of a peptide that mimicked the 557-576 sequence of HIF-1alpha. The enzyme promoted [(35)S]vHL binding to glutathione S-transferase (GST).ODD fusion protein. This association increased in the presence of CsA. CsA effects were not observed when the proline residue corresponding to Pro-564 in the HIF-1alpha sequence was replaced by a hydroxyproline or an alanine residue. Finally, CsA increased vHL-ODD interaction during hypoxia. We conclude that CsA destabilizes HIF-1alpha by promoting hydroxylation of Pro-564 in the ODD domain. Such a mechanism may prevent hypoxic adaptation during CsA-induced nephrotoxicity and contribute to the adverse effects of this drug.
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WebPage:
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