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*
Institute for Clinical Pathology, University of Vienna, Allgemeines
Krankenhaus, Austria.
Institute of Anatomy, Neuromuscular Research Department, University of
Vienna, Vienna, Austria.
Correspondence to Dr. Dontscho Kerjaschki, Institute for Clinical Pathology, University of Vienna, Allgemeines Krankenhaus, Währinger Gürtel 18-20, A-1090 Vienna, Austria. Phone: +43 1 40400 5176; Fax: +43 1 40400 5193; E-mail: dontscho.kerjaschki{at}akh-wien.ac.at
Abstract. Extensive flattening of podocyte foot processes and
increased permeability of the glomerular capillary filter are the major
pathologic features of minimal change nephrosis (MCN) and focal segmental
glomerulosclerosis (FSGS). Adhesion proteins anchor and stabilize podocytes on
the glomerular basement membrane (GBM), and presumably are involved in the
pathogenesis of foot process flattening. Thus far, 
3
ß1-integrin was localized to basal cell membrane domains. In
this report, - and ß-dystroglycan (DG) were detected at precisely
the same location by immunoelectron microscopy, and the presence of -
and ß-DG chains was confirmed by immunoblotting on isolated human
glomeruli. Because the major DG binding partners in the GBM (laminin, agrin,
perlecan), and the intracellular dystrophin analogue utrophin are also present
in glomeruli, it appears that podocytes adhere to the GBM via DG complexes,
similar to muscle fibers in which actin is linked via dystrophin and DG to the
extracellular matrix. As with muscle cells, it is therefore plausible that
podocytes use precisely actin-guided DG complexes at their "soles"
to actively govern the topography of GBM matrix proteins. Expression of the
/ß-DG complex was reported to be reduced in muscular dystrophies,
and therefore a search for similar pathologic alterations in archival kidney
biopsies from patients with MCN (n = 16) and FSGS (n = 8)
was conducted by quantitative immunoelectron microscopy. The density of
-DG on the podocyte's soles was significantly reduced to 25% in MCN,
whereas it was not different in normal kidneys and FSGS. The expression of
ß-DG was reduced to >50% in MCN, and was slightly increased in FSGS.
Levels of DG expression returned to normal in MCN after steroid treatment
(n = 4). Expression of ß1-integrin remained at normal
levels in all conditions. These findings point to different potentially
pathogenic mechanisms of foot process flattening in MCN and FSGS.
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