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Matrix Metalloproteinase-2 in a Murine Model of Infantile-Type Polycystic Kidney Disease

CAROLYN A. RANKIN^*, YOSHIFUMI ITOH^*, CHUNQIAO TIAN, DONNA M. ZIEMER^*, JAMES P. CALVET^* and VINCENT H. GATTONE

^* Departments of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, Kansas.
Departments of Anatomy and Cell Biology, University of Kansas Medical Center, Kansas City, Kansas.

Correspondence to Dr. Vincent H. Gattone II, Department of Anatomy and Cell Biology, University of Kansas Medical Center, Kansas City, KS 66160-7400. Phone: 913-588-2731; Fax: 913-588-2710; E-mail: vgattone{at}kumc.edu

Abstract. It was previously found that elevated levels of matrix metalloproteinase (MMP)-2 (gelatinase A) and -9 (gelatinase B) were synthesized and secreted into the medium by cultured kidney tubules derived from cystic C57BL/6J-cpk mice. To determine whether increased synthesis and secretion occur in vivo in this mouse model of polycystic kidney disease, kidney protein extracts, mRNA, and tissue sections were compared for expression and activity of MMP-2 and -9. Although both MMP were detected in tissue extracts, the differences in expression levels and activity in normal and cystic kidneys were far greater for MMP-2. High levels of MMP-2 seemed to result from increased expression by the cystic kidneys predominantly in the second and third postnatal weeks (a time when the kidneys are undergoing rapid cystic enlargement). Much of the increased MMP was present in the inactive zymogen form, although active enzyme was readily detected by sodium dodecyl sulfate-polyacrylamide gel zymography and in situ zymography. MMP-2 was abnormally localized to the interstitium and to foci between cysts, suggesting that MMP-2 may regulate collagen accumulation at those sites, thus allowing cyst enlargement and limiting the severity of interstitial fibrosis.

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Copyright © 2008 by the American Society of Nephrology. Online ISSN: 1533-3450 Print ISSN: 1046-6673