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J Am Soc Nephrol 10:2480-2487, 1999
© 1999 American Society of Nephrology

YB-1 Regulation of the Human and Rat Gelatinase A Genes via Similar Enhancer Elements

PETER R. MERTENS*, MARIA ALEXANDRA ALFONSO-JAUME{dagger}, KARIN STEINMANN{dagger} and DAVID H. LOVETT{dagger}

* Medical Clinic II, RWTH Aachen, Germany;
{dagger} The Department of Medicine, San Francisco VAMC/University of California, San Francisco, California.

Correspondence to Dr. Peter R. Mertens, Medizinische Klinik II, RWTH Aachen, Pauwelsstraße 30, 52057 Aachen, Germany. Phone: +49 241 808 9532; Fax: +49 241 888 8446; E-mail: pmertens{at}post.klinikum.rwth-aachen.de

Abstract. Experimental and clinical studies strongly suggest that gelatinase A plays a central role in the evolution of glomerular injury and sclerosis. The sequences of the 5' flanking regions of the human and rat gelatinase A genes do not share similarities with other members of the matrix metallo-proteinase gene family and are regulated in a distinctive manner. The human and rat gelatinase A genes include regions of significant homology (r2 human; RE-1 rat), which have been shown to act as potent cis-activators of transcription. The rat RE-1 sequence interacts specifically with the developmentally regulated transcription factors AP2 and YB-1, resulting in a synergistic activation of gelatinase A transcription. Although the human r2 sequence specifically interacts with AP2 (Mol Cell Biol 10: 6524-6532, 1990), there is no clear evidence for the presence of a canonical YB-1 binding site (Y-box) within this sequence. This study demonstrates, despite the absence of a canonical Y-box sequence in the r2 element, that YB-1 and AP2 specifically interact with r2, yielding synergistic transactivation of the human gelatinase A gene. It is concluded that the r2 element is the conserved functional analog of the RE-1 element, and that interactions of AP2 and YB-1 govern human gelatinase A gene expression.




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