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Vol. 14, Issue 8, 3470-3481, August 2003
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by Inhibition of Prolyl Hydroxylases
¶
* Institute of Physiology, University of Luebeck, Germany;
Institute of Physiology, University of Duisburg-Essen, Germany; and
Department of Cell Biology, University of Kaiserslautern, Germany
Submitted December 5, 2002;
Revised April 7, 2003;
Accepted April 7, 2003
Monitoring Editor: Suzanne Pfeffer
Hypoxia inducible factor-1 (HIF-1) is the master regulator of metabolic
adaptation to hypoxia. It is appreciated that HIF-1
accumulation is
achieved under normoxic conditions by e.g., nitric oxide. We determined
molecular mechanisms of HIF-1 accumulation under the impact of
S-nitrosoglutathione (GSNO). In human embryonic kidney cells GSNO
provoked nuclear accumulation of HIF-1. This appeared unrelated to gene
transcription and protein translation, thus pointing to inhibition of
HIF-1 degradation. Indeed, GSNO as well as the hypoxia mimic
CoCl2 decreased ubiquitination of HIF-1 and GSNO-induced
HIF-1 failed to coimmunoprecipitate with pVHL (von Hippel Lindau
protein). Considering that HIF-1-pVHL interactions require prolyl
hydroxylation of HIF-1, we went on to demonstrate inhibition of
HIF-1 prolyl hydroxylases (PHDs) by GSNO. In vitro HIF-1-pVHL
interactions revealed that GSNO dose-dependently inhibits PHD activity but not
the interaction of a synthetic peptide resembling the hydroxylated
oxygen-dependent degradation domain of HIF-1 with pVHL. We conclude
that GSNO-attenuated prolyl hydroxylase activity accounts for HIF-1
accumulation under conditions of NO formation during normoxia and that PHD
activity is subject to regulation by NO.
Both authors contributed equally to this work.
¶ Corresponding author. E-mail address: bruene{at}rhrk.uni-kl.de.
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