Hypoxia up-regulates triosephosphate isomerase expression via a HIF-dependent pathway

The glycolytic enzyme triosephosphate isomerase (TPI) catalyses the reversible conversion of dihydroxyacetone phosphate into glyceraldehyde-3-phosphate. We report here that the expression of TPI at both the mRNA and protein levels is increased by hypoxia in vivo and in vitro. The temporal pattern of...

Full description

Saved in:
Bibliographic Details
Published in:Pflügers Archiv 2004-05, Vol.448 (2), p.175-180
Main Authors: Gess, Bernhard, Hofbauer, Karl-Heinz, Deutzmann, R, Kurtz, Armin
Format: Article
Language:English
Subjects:
Actins - biosynthesis
Animals
Carbon Monoxide - pharmacology
Cells, Cultured
Cloning, Molecular
DNA, Complementary - biosynthesis
DNA, Complementary - genetics
DNA-Binding Proteins - physiology
Electrophoresis, Polyacrylamide Gel
Gene Expression Regulation, Enzymologic - physiology
Hypoxia
Hypoxia - metabolism
Hypoxia-Inducible Factor 1
Hypoxia-Inducible Factor 1, alpha Subunit
Male
Muscle, Smooth, Vascular - cytology
Muscle, Smooth, Vascular - enzymology
Nuclear Proteins - physiology
Nuclease Protection Assays
Rats
Rats, Sprague-Dawley
RNA, Messenger - biosynthesis
RNA, Messenger - isolation & purification
Signal Transduction - physiology
Transcription Factors - physiology
Triose-Phosphate Isomerase - biosynthesis
Triose-Phosphate Isomerase - genetics
Up-Regulation
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The glycolytic enzyme triosephosphate isomerase (TPI) catalyses the reversible conversion of dihydroxyacetone phosphate into glyceraldehyde-3-phosphate. We report here that the expression of TPI at both the mRNA and protein levels is increased by hypoxia in vivo and in vitro. The temporal pattern of hypoxic TPI induction is very similar to that of genes triggered by the hypoxia-inducible transcription factor (HIF) and is mimicked characteristically by cobalt and by deferoxamine, but is absent in cells with a defective aryl hydrocarbon receptor nuclear translocator (ARNT, here HIF-1beta) and in cells lacking HIF-1alpha protein. We conclude from these findings that the expression of TPI is regulated via the HIF pathway and thus belongs to the family of classic oxygen-regulated genes. The physiological meaning of an increased expression of TPI in hypoxygenated tissues is probably to increase the flow of triosephosphates through the glycolytic cascade thus leading to an increase of anaerobic energy generation.
ISSN:0031-6768
1432-2013
DOI:10.1007/s00424-004-1241-1