Document Detail


HIF-1alpha-prolyl hydroxylase: molecular target of nitric oxide in the hypoxic signal transduction pathway.
MedLine Citation:
PMID:  12099689     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We have investigated inhibitory mechanisms of hypoxic activation of HIF-1alpha by nitric oxide (NO). Using a Hep3B cell-derived cell line, HRE7 cells, we found that the inhibition of HIF-1alpha activity by NO requires a substantial amount of oxygen, albeit at a lower level. We further investigated the effect of NO on the binding activity of the von Hippel-Lindau tumor suppressor protein (pVHL) to the N-terminal activation domain (NAD) overlapping the oxygen-dependent degradation domain (ODD) of HIF-1alpha, because this reaction involves prolyl hydroxylation in NAD that requires oxygen. Although we could not detect any binding activity when NAD was incubated with whole cell extracts from cells treated with CoCl(2) or desferrioxamine, the binding capacity was manifested when Hep3B cells were treated together with NO. This activation was also observed when whole cell extracts from CoCl(2)-treated cells were incubated with NO. The prolyl hydroxylase from Hep3B cells treated with CoCl(2) was partially purified about 80-fold, and several enzymatic properties were examined. The enzyme required ferrous ion and 2-oxoglutaric acid. Strong activation of the prolyl hydroxylase by NO was observed without further addition of ferrous ion.
Authors:
Feng Wang; Hiroki Sekine; Yasuo Kikuchi; Chikahisa Takasaki; Chisa Miura; Okuda Heiwa; Taro Shuin; Yoshiaki Fujii-Kuriyama; Kazuhiro Sogawa
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  295     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2002 Jul 
Date Detail:
Created Date:  2002-07-08     Completed Date:  2002-08-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  657-62     Citation Subset:  IM    
Copyright Information:
(c) 2002 Elsevier Science (USA).
Affiliation:
Department of Biomolecular Science, Graduate School of Life Sciences, Tohoku University, Aoba-ku Sendai 980-8578, Japan.
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MeSH Terms
Descriptor/Qualifier:
Anoxia*
Blotting, Western
Cell Line
Cobalt / metabolism
DNA Fragmentation
DNA, Complementary / metabolism
Dose-Response Relationship, Drug
Electrophoresis, Polyacrylamide Gel
Humans
Hypoxia-Inducible Factor 1, alpha Subunit
Ketoglutaric Acids / metabolism
Luciferases / metabolism
Nitric Oxide / metabolism*,  pharmacology
Oxygen / metabolism
Procollagen-Proline Dioxygenase / metabolism*
Protein Binding
Protein Structure, Tertiary
Sepharose / chemistry
Signal Transduction*
Sodium Chloride / pharmacology
Time Factors
Transcription Factors / metabolism*
Transcription, Genetic
Transfection
Chemical
Reg. No./Substance:
0/DNA, Complementary; 0/HIF1A protein, human; 0/Hypoxia-Inducible Factor 1, alpha Subunit; 0/Ketoglutaric Acids; 0/Transcription Factors; 10102-43-9/Nitric Oxide; 328-50-7/alpha-ketoglutaric acid; 7440-48-4/Cobalt; 7646-79-9/cobaltous chloride; 7647-14-5/Sodium Chloride; 7782-44-7/Oxygen; 9012-36-6/Sepharose; EC 1.13.12.-/Luciferases; EC 1.14.11.2/Procollagen-Proline Dioxygenase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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