Agrin is a major heparan sulfate proteoglycan in the human glomerular basement membrane
| Autor: | Lambert P. van den Heuvel, Karel J.M. Assmann, H. Dijkman, Thea J. van de Velden, Jacques H. Veerkamp, C.A.F. Buskens, Leo A. H. Monnens, Markus A. Rüegg, Alexander J. Groffen, Jacob van den Born |
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| Přispěvatelé: | Groningen Kidney Center (GKC), Groningen Institute for Organ Transplantation (GIOT), Functional Genomics, Constitutional and Administrative Law, Human genetics, Amsterdam Neuroscience - Cellular & Molecular Mechanisms |
| Jazyk: | angličtina |
| Rok vydání: | 1998 |
| Předmět: |
0301 basic medicine
Immunologische ontstekingsprocessen in de nier Kidney Glomerulus Pathofysiologie immunologie en behandeling van nieraandoeningen Fluorescent Antibody Technique Immune Sera/metabolism Heparitin Sulfate/metabolism urologic and male genital diseases Basement Membrane Extracellular matrix Inflammatory reactions in the kidneys Monoclonal Fluorescent Antibody Technique Indirect Microscopy Immunoelectron Neuromuscular Junction/metabolism Heparan Sulfate Proteoglycans/metabolism Microscopy Agrin biology Chemistry Glomerular basement membrane Structuur en functie van heparansulfaat proteoglycanen in de humane basaal membraan van de nier Antibodies Monoclonal Pathophysiology immunology and treatment of renal disease Cell biology medicine.anatomical_structure Biochemistry Kidney Glomerulus/cytology Proteoglycans of renal basement membranes Muscle Proteoglycans Basal lamina Anatomy Adult Indirect Kidney Cortex Histology animal structures medicine.drug_class Immunoelectron microscopy Neuromuscular Junction Heparan sulfate proteoglycan Enzyme-Linked Immunosorbent Assay Kidney Cortex/cytology Perlecan Skeletal/metabolism Monoclonal antibody Neuromuscular junction Antibodies Fluorescence 03 medical and health sciences Proteoglycanen van basaalmembranen van de nier Agrin/biosynthesis medicine Animals Humans Muscle Skeletal Immunoelectron Muscle Skeletal/metabolism 030102 biochemistry & molecular biology Basement Membrane/metabolism Bungarotoxins/metabolism urogenital system Immune Sera Bungarotoxins Proteoglycans/metabolism Rats carbohydrates (lipids) 030104 developmental biology nervous system Microscopy Fluorescence biology.protein Heparitin Sulfate Structure and function of heparan sulphate proteoglycans in human renal basement membranes Heparan Sulfate Proteoglycans |
| Zdroj: | Journal of Histochemistry & Cytochemistry, 46(1), 19-27 The Journal of Histochemistry and Cytochemistry, 46(1), 19-27. Histochemical Society Inc. 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 1998, ' Agrin is a major heparan sulfate proteoglycan in the human glomerular basement membrane ', Journal of Histochemistry and Cytochemistry, vol. 46, no. 1, pp. 19-27 . https://doi.org/10.1177/002215549804600104 Journal of Histochemistry and Cytochemistry, 46, pp. 19-27 Journal of the American Society of Nephrology, 8, A2396-A2396. Williams & wilkins 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 1998, ' Agrin is a major heparan sulfate proteoglycan in the human glomerular basement membrane ', The Journal of Histochemistry and Cytochemistry, vol. 46, no. 1, pp. 19-27 . https://doi.org/10.1177/002215549804600104 Journal of Histochemistry and Cytochemistry, 46, 19-27 Journal of Histochemistry and Cytochemistry, 46(1), 19-27. Histochemical Society Inc. Journal of the American Society of Nephrology, 8, pp. A2396-A2396 |
| ISSN: | 0022-1554 1046-6673 |
| Popis: | 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. (J Histochem Cytochem 46:19-27, 1998) |
| Databáze: | OpenAIRE |
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