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Am J Physiol Renal Physiol (March 11, 2003). doi:10.1152/ajprenal.00157.2002
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Submitted on April 23, 2002
Accepted on March 4, 2003

Relaxin Increases Ubiquitin-Dependent Degradation of Fibronectin In Vitro and Ameliorates Renal Fibrosis In Vivo

Glenn A. McDonald1*, Pradip Sarkar2, Helmut Rennke3, Elaine Unemori4, Raghu Kalluri2, and Vikas P. Sukhatme2

1 Department of Medicine, The University of Texas Medical School at Houston, Houston, TX, USA
2 Department of Medicine, Beth Israel Deaconess Medical Center, Boston, MA, USA
3 Department of Pathology, Brigham and Women's Hospital, Boston, MA, USA
4 Connetics Corp., Palo Alto, CA, USA

* To whom correspondence should be addressed. E-mail: glenn.a.mcdonald{at}uth.tmc.edu.

Fibronectin, a large adhesive glycoprotein, is a prominent constituent of the extracellular matrix (ECM). Abnormalities in fibronectin homeostasis occur in numerous disease states, ranging from primary fibrosing conditions to neoplastic transformation. We demonstrate that fibronectin is a target protein substrate for ubiquitin-dependent degradation. Co-immunoprecipitation experiments and confocal microscopy demonstrated a ubiquitin-fibronectin interaction. In an in vitro model of renal fibrosis, relaxin, an insulin-like growth factor, increased ubiquitin-dependent fibronectin degradation. Relaxin also was evaluated in an anti-glomerular basement membrane (anti-GBM) model of renal fibrosis. Animals treated with relaxin experienced renoprotection, manifested by decreased serum creatinine and proteinuria. Histologic evaluation of kidney sections from animals treated with relaxin showed decreased glomerulosclerosis and interstitial fibrosis. We conclude that relaxin might be developed as a useful agent for the treatment of renal fibrosis.




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