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*
Department of Anatomy and Cell Biology, University of Heidelberg,
Germany
Department of Medicine,
Ludwig-Maximilians-Universität, Munich,
Germany
Departments of Medicine and Anatomy and Structural Biology, Albert
Einstein College of Medicine, Bronx, New York.
Correspondence to Dr. Peter Mundel, Division of Nephrology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461. Phone: 718-430-3158; Fax: 718-430-8963; E-mail: mundel{at}aecom.yu.edu
Abstract. The glomerular slit diaphragm between podocyte foot
processes shares typical morphologic features with an adherens junction.
Differentiated cultured podocytes form cellular structures comparable to
filtration slits in vivo. At those sites, zonula occludens-1 (ZO-1)
was coexpressed with P-cadherin as well as with
-, ß-, and
-catenin. In situ, P-cadherin was detected at the slit
diaphragm in association with ZO-1 as shown by confocal microscopy and
immunogold double labeling electron microscopy. P-cadherin expression in
vivo and in vitro was confirmed by reverse transcription-PCR.
These findings led to the concept that the slit diaphragm represents an
adherens junction composed of P-cadherin,
-, ß-, and
-catenin, and ZO-1. In contrast to an adherens junction of a similar
composition recently described in cultured fibroblasts, the slit diaphragm
complex does not contain vinculin, which was found in nearby focal contacts. A
P-cadherinbased adherens junction is well-suited to explain the zipper-like
structure of the slit diaphragm. The present study should allow new avenues
leading to the identification of additional slit diaphragm-associated proteins
conferring specificity to this unique cell junction.
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N.-Y. Shih, J. Li, R. Cotran, P. Mundel, J. H. Miner, and A. S. Shaw CD2AP Localizes to the Slit Diaphragm and Binds to Nephrin via a Novel C-Terminal Domain Am. J. Pathol., December 1, 2001; 159(6): 2303 - 2308. [Abstract] [Full Text] [PDF] |
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