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Originally published as JHC exPRESS on June 13, 2005.
doi:10.1369/jhc.4A6596.2005
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Journal of Histochemistry and Cytochemistry
Volume 53 (11): 1345-1353, 2005
Copyright ©The Histochemical Society, Inc.

Localization of {alpha}-Dystroglycan on the Podocyte : from Top to Toe

Nils P.J. Vogtländer, Henry Dijkman, Marinka A.H. Bakker, Kevin P. Campbell, Johan van der Vlag and Jo H.M. Berden

Division of Nephrology (NPJV,MAHB,JvdV,JHMB) and Department of Pathology (HD), Radboud University Nijmegen Medical Centre, Nijmegen, The Netherlands, and Department of Physiology and Biophysics (KPC), Howard Hughes Medical Institute, University of Iowa, Iowa City, Iowa

Correspondence to: J.H.M. Berden MD, PhD, Division of Nephrology (545), Radboud University Nijmegen Medical Centre, PO Box 9101, 6500 HB Nijmegen, The Netherlands. E-mail: j.berden{at}nier.umcn.nl

{alpha}-DYSTROGLYCAN (DG) is a negatively charged membrane-associated glycoprotein that links the cytoskeleton to the extracellular matrix. Previously, we described that {alpha}-DG covers the whole podocyte cell membrane in the rat. However, our finding was challenged by the description of a strictly basolateral localization in human kidney biopsies, using a different antibody against {alpha}-DG. Therefore, we studied the exact localization of glomerular {alpha}-DG by using these two antibodies in both species. The studies were performed by using monoclonal antibodies (MoAbs) IIH6 and VIA4.1 in immunofluorescence, confocal microscopy, and immunoelectron microscopy on both rat and human kidney sections, as well as on cultured mouse podocytes. The apical localization of {alpha}-DG on podocytes was more dominant than the basolateral localization. The basolateral staining with MoAb VIA4.1 was more pronounced than that of MoAb IIH6. With both MoAbs, the staining in rat kidneys was more prominent, in comparison to human kidneys. We conclude that {alpha}-DG is expressed at both the basolateral and apical sides of the podocyte. This localization suggests that {alpha}-DG plays a dual role in the maintenance of the unique architecture of podocytes by its binding to the glomerular basement membrane, and in the maintenance of the integrity of the filtration slit, respectively. (J Histochem Cytochem 53:1345–1353, 2005)

Key Words: dystroglycan • podocyte • agrin • laminin • glomerulus • kidney • podocalyxin • renal


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