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Articles in PresS, published online ahead of print December 3, 2002
Am J Physiol Renal Physiol, 10.1152/ajprenal.00266.2002
Submitted on July 24, 2002
Accepted on December 1, 2002
1 Institute of Biology, National for Scientific Research "Demokritos", Athens, Attiki, Greece
2 Laboratory of Pathology, National Institutes of Health, Bethesda, Maryland, USA
3 Department of Pediatrics, University of Minnesota, Minneapolis, Minnesota, USA
* To whom correspondence should be addressed. E-mail: pkit{at}mail.demokritos.gr.
In cultured human glomerular epithelial cells (HGEC), the presence of 25 mM glucose resulted in decreased expression of 
3, 2 and 
1 integrin subunits, and increased expression of 5 and v3 integrins. This change was accompanied by decreased binding of HGEC to type IV collagen (tIV). In the presence of normal glucose concentrations (5 mM), cell binding to tIV was primarily mediated by 21 and 51 integrins, as indicated by experiments in which cell adhesion to tIV was competed by specific anti-integrin monoclonal antibodies. In the presence of high glucose (25 mM), the up-regulated 5 and v3 integrins were mainly involved in cell binding to tIV. Furthermore, high glucose decreased the expression of MMP-2, a collagenase regulated in part by 31 integrin, as suggested by the use of ligand-mimicking antibodies against these integrins, which resulted in the release of increased amounts of MMP-2 in the culture medium. Finally, TIMP-2, the specific inhibitor of MMP-2, was up-regulated in high glucose, and could contribute to matrix accumulation. These changes could help explain basement membrane thickening in diabetes.
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