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J. Biol. Chem., Vol. 279, Issue 33, 34827-34832, August 13, 2004
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3 Integrin*
From the aDepartments of Medicine, kAnatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, New York 10461, the Departments of eMedicine and iBiochemistry, Juntendo University, Tokyo 113-8421, Japan, the fDepartment of Neurology, University of Heidelberg, 69120 Heidelberg, Germany, the gDepartment of Surgery, University of Muenster, 48149 Muenster, Germany, the hDepartment of Immunology, University of Washington, Seattle, Washington 98195, and the jDepartment of Medicine, Children's Hospital, Boston, Massachusetts 02115
Podocyte foot process effacement and disruption of the slit diaphragm are typically associated with glomerular proteinuria and can be induced in rats by the injection of puromycin aminonucleoside. Here, we show that the induction of puromycin aminonucleoside nephrosis involves podocyte migration conducted by a coordinated interplay between the cysteine protease cathepsin L and 
3 integrin. Puromycin aminonucleoside treatment up-regulates cathepsin L expression in podocytes in vivo as well as expression and enzymatic activity of cathepsin L in podocytes in vitro. Isolated podocytes from mice lacking cathepsin L are protected from cell puromycin aminonucleoside-induced cell detachment. The functional significance of cathepsin L expression was underscored by the observation that puromycin aminonucleoside-induced cell migration was slowed down in cathepsin L-deficient podocytes and by the preservation of cell-cell contacts and expression of vital slit diaphragm protein CD2AP. Cathepsin L expression and activity were induced in podocytes lacking 3 integrin. Similarly, acute functional inhibition of 3 integrin in wild type podocytes with a blocking antibody increased the expression of cathepsin L activity. Down-regulation of 3 integrin protected against puromycin aminonucleoside-induced podocyte detachment. In summary, these data establish that podocyte foot process effacement is a migratory event involving a novel interplay between cathepsin L and 3 integrin.
Received for publication, February 23, 2004 , and in revised form, June 1, 2004.
* This work was supported by National Institutes of Health NIDDK Grants DK057683 and DK064236 (to P. M.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
b Present address: Renal Unit, Massachusetts General Hospital, and Harvard Medical School, Charlestown, MA 02129.
c Both supported by fellowships from the Kidney and Urology Foundation of America.
d Supported by the Deutsche Forschungsgemeinschaft.
l To whom correspondence should be addressed: Division of Nephrology, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461. Tel.: 718-430-3158; Fax: 718-430-8963; E-mail: mundel{at}aecom.yu.edu.
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