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M413248200v1
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Papers In Press, published online ahead of print December 15, 2004
J. Biol. Chem, 10.1074/jbc.M413248200
Submitted on November 23, 2004
Revised on December 14, 2004
Accepted on December 15, 2004

Hypoxia-enhanced expression of the proprotein convertase furin is mediated by HIF-1: Impact on the bioactivation of proproteins

Stephanie McMahon, FrancineGrondin Grondin, Patrick P. McDonald, Richard E. Darren, and Claire M. Dubois

Department of Pediatrics, University of Sherbrooke, Sherbrooke, Quebec J1H 5N4

Corresponding Author: claire.m.dubois{at}usherbrooke.ca

Hypoxia is a common tumorigenesis enhancer, mostly owing to its impact on gene expression of many angiogenic and invasion-related mediators, some of which are natural substrates for the proprotein convertase furin. Analysis of furin promoters revealed the presence of putative binding sites for HIF-1, a transcription complex that plays a pivotal role in cellular adaptation to hypoxia. In fact, we demonstrate herein that the levels of fur mRNA, encoding furin, are remarkably increased upon hypoxic challenge. Co-transfection of a HIF-1a DN in WT cells or transfection of a furin promoter-reporter gene in HIF-1-deficient cells indicated the requirement of HIF-1 for furin promoter activation by hypoxia. Direct HIF-1 action on the furin promoter was identified as a canonical HRE site with enhancer capability. The hypoxic/HIF-1 regulation of furin correlated with an increased proteolytic activation of the substrates MT1-MMP and TGFb1. Our findings unveil a new facet of the physiological consequences of hypoxia/HIF-1, through enhanced furin-induced proteolytic processing/activation of proproteins known to be involved in tumorigenesis.


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