Agrin is a major heparan sulfate proteoglycan in the human glomerular basement membrane
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 155381
Author(s) Groffen, A. J.; Ruegg, M. A.; Dijkman, H.; van de Velden, T. J.; Buskens, C. A.; van den Born, J.; Assmann, K. J.; Monnens, L. A.; Veerkamp, J. H.; van den Heuvel, L. P.
Author(s) at UniBasel Rüegg, Markus A.
Year 1998
Title Agrin is a major heparan sulfate proteoglycan in the human glomerular basement membrane
Journal Journal of Histochemistry and Cytochemistry
Volume 46
Number 1
Pages / Article-Number 19-27
Keywords agrin, perlecan, heparan sulfate proteoglycan, glomerular basement membrane
Mesh terms Adult; Agrin, immunology; Animals; Antibodies, Monoclonal; Basement Membrane, ultrastructure; Bungarotoxins, metabolism; Enzyme-Linked Immunosorbent Assay; Fluorescent Antibody Technique, Indirect; Heparan Sulfate Proteoglycans, metabolism; Heparitin Sulfate, metabolism; Humans; Immune Sera, metabolism; Kidney Cortex, metabolism; Kidney Glomerulus, ultrastructure; Microscopy, Fluorescence; Microscopy, Immunoelectron; Muscle, Skeletal, metabolism; Neuromuscular Junction, ultrastructure; Proteoglycans, metabolism; Rats
Abstract Agrin is a heparan sulfate proteoglycan (HSPG) that is highly concentrated in the synaptic basal lamina at the neuromuscular junction (NMJ). Agrin-like immunoreactivity is also detected outside the NMJ. Here we show that agrin is a major HSPG component of the human glomerular basement membrane (GBM). This is in addition to perlecan, a previously characterized HSPG of basement membranes. Antibodies against agrin and against an unidentified GBM HSPG produced a strong staining of the GBM and the NMJ, different from that observed with anti-perlecan antibodies. In addition, anti-agrin antisera recognized purified GBM HSPG and competed with an anti-GBM HSPG monoclonal antibody in ELISA. Furthermore, both antibodies recognized a molecule that migrated in SDS-PAGE as a smear and had a molecular mass of approximately 200-210 kD after deglycosylation. In immunoelectron microscopy, agrin showed a linear distribution along the GBM and was present throughout the width of the GBM. This was again different from perlecan, which was exclusively present on the endothelial side of the GBM and was distributed in a nonlinear manner. Quantitative ELISA showed that, compared with perlecan, the agrin-like GBM HSPG showed a sixfold higher molarity in crude glomerular extract. These results show that agrin is a major component of the GBM, indicating that it may play a role in renal ultrafiltration and cell matrix interaction.
Publisher Williams and Wilkins
ISSN/ISBN 0022-1554 ; 1551-5044
edoc-URL http://edoc.unibas.ch/dok/A5258415
Full Text on edoc Restricted
Digital Object Identifier DOI 10.1177/002215549804600104
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/9405491
ISI-Number WOS:000071080300004
Document type (ISI) Journal Article
 
   

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