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Vol. 9, No. 3, 2001
Issue release date: May–June 2001
Section title: Original Paper
Exp Nephrol 2001;9:214–222
(DOI:10.1159/000052614)

Decreased Glomerular Expression of Agrin in Diabetic Nephropathy and Podocytes, Cultured in High Glucose Medium

Yard B.A. · Kahlert S. · Engelleiter R. · Resch S. · Waldherr R. · Groffen A.J. · van den Heuvel L.P.W.J. · van der Born J. · Berden J.H.M. · Kröger S. · Hafner M. · van der Woude F.J.
aV. Medizinische Universitätsklinik, Klinikum Mannheim, University of Heidelberg; bFachhochschule Mannheim; cGemeinschaftspraxis für Pathologie, Heidelberg, Germany; Departments of dPediatrics and eNephrology, University Hospital, Nijmegen, The Netherlands and fMax Planck Institut für Hirnforschung, Frankfurt, Germany

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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Published online: 4/23/2001

Number of Print Pages: 9
Number of Figures: 5
Number of Tables: 1

ISSN: (Print)
eISSN: 1660-2129 (Online)

For additional information: http://www.karger.com/NEE

Abstract

Aim: A decrease in glomerular heparan sulfate (HS) proteoglycan (PG), without apparent decrease in HSPG core protein expression, has been reported to occur in diabetic nephropathy (DN). In most studies however, agrin, the major HSPG core protein in the glomerular basement membrane, has not been studied. This prompted us to study the glomerular expression of agrin in parallel to the expression of HS-glycosaminoglycans (GAG) in biopsies of patients with DN. Furthermore, the influence of glucose on agrin production in cultured podocytes and the expression of agrin in fetal kidneys was investigated. Methods: Cryostat sections of renal biopsies from patients with DN (n = 8) and healthy controls (HC, n = 8), were stained for agrin and HS-GAG. Sections of fetal kidneys were double stained for agrin and CD35 or CD31. Stainings were performed by indirect immunofluorescence (IIF). The production of agrin by cultured human podocytes was tested by ELISA and IIF. Results: The expression of agrin, detected by AS46, was significantly reduced in biopsies from patients with DN compared to HC (p < 0.01). Similar findings were observed when monoclonal antibody JM72 was used (p < 0.05). In addition, a significant reduction in the glomerular expression of HS-GAG was detected with JM403 in these patients (p < 0.01). Agrin is expressed in cultured podocytes, the expression hereof was reduced when the cells were cultured in the presence of 25 mM D-glucose (p < 0.01). In biopsies of human fetal kidneys, glomerular expression of agrin coincided with the expression of CD31. In early stages of glomerular differentiation there was a strong staining for agrin and CD31 while CD35 was only slightly positive. Conclusions: Our data argue against a selective dysregulation in HSPG sulfation in DN, but suggest a pivotal role for hyperglycemia in the downregulation of agrin core protein production.


  

Author Contacts

Dr. B.A. Yard
V. Medizinische Universitätsklinik, Klinikum Mannheim
University of Heidelberg, Theodor-Kutzer-Ufer 1–3
D–68135 Mannheim (Germany)
Tel. +49 621 3832340, Fax +49 621 3833804

  

Article Information

Received: Received: September 20, 1999
Accepted: May 19, 2000
Number of Print Pages : 9
Number of Figures : 5, Number of Tables : 1, Number of References : 44

  

Publication Details

Experimental Nephrology (Journal of Renal Cell Biology)

Vol. 9, No. 3, Year 2001 (Cover Date: May-June 2001)

Journal Editor: L.G. Fine, London
ISSN: 1018–7782 (print), 1421–9956 (Online)

For additional information: http://www.karger.com/journals/exn


Article / Publication Details

First-Page Preview
Abstract of Original Paper

Published online: 4/23/2001

Number of Print Pages: 9
Number of Figures: 5
Number of Tables: 1

ISSN: (Print)
eISSN: 1660-2129 (Online)

For additional information: http://www.karger.com/NEE


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