Comparison of heparan sulfate proteoglycans from equine and human glomerular basement membranes
| Autor: | C. H. Schröder, J.H. Veerkamp, G.H.G.W. Janssen, L.P.W.J. van den Heuvel, T.J.A.M. van de Velden, J. van den Born, L.A.H. Monnens, Jhm Berden |
|---|---|
| Přispěvatelé: | Groningen Kidney Center (GKC), Groningen Institute for Organ Transplantation (GIOT), Guided Treatment in Optimal Selected Cancer Patients (GUTS) |
| Jazyk: | angličtina |
| Rok vydání: | 1990 |
| Předmět: |
Kidney Glomerulus
Fluorescent Antibody Technique Epitopes/immunology Amino Acids/analysis Biochemistry Basement Membrane Glycosaminoglycan chemistry.chemical_compound Epitopes Heparitin Sulfate/chemistry Amino Acids Polysaccharide-Lyases/metabolism Mesylates Chromatography Gel biology Chemistry Heparan sulfate Trypsin Chromatography Ion Exchange Ion Exchange Chromatography Gel medicine.drug Horses/metabolism Immune Sera/immunology Immunoblotting Carbohydrates Chondroitin Sulfate Proteoglycans/chemistry Kidney Glomerulus/chemistry Perlecan Peptide Mapping Carbohydrates/analysis medicine Animals Humans Horses Polysaccharide-Lyases Clostripain Molecular mass Immune Sera Molecular biology carbohydrates (lipids) Molecular Weight Proteoglycan Chondroitin Sulfate Proteoglycans Basement Membrane/chemistry Polyclonal antibodies biology.protein Heparitin Sulfate Heparan Sulfate Proteoglycans |
| Zdroj: | Essays in biochemistry, 22(8), 903-914 |
| ISSN: | 0020-711X |
| Popis: | 1. Proteoglycans extracted from human and equine glomerular basement membranes (GBM) were purified by ion-exchange chromatography and gel filtration. 2. The glycoconjugates had an apparent molecular mass of 200-400 kDa and consisted of 75% protein and 25% glycosaminoglycan. Glycosidase and HNO2 treatment and the amino sugar and sulfate composition of both proteoglycan preparations identified heparan sulfate (HS) as the predominant saccharide chain. 3. Hydrolysis with trifluoromethanesulfonic acid yielded comparable core proteins with molecular masses of ca 160 and 120 kDa. 4. The HS chains had an apparent molecular mass of 18 kDa. Results of heparitinase digestion and HNO2-treatment indicated a clustering of sulfate groups in the distal part of the HS side chains. 5. Peptide mapping after trypsin, clostripain or V8 protease digestion of radiolabeled human and equine heparan sulfate proteoglycans (HSPG) preparations with three different separation techniques showed large differences. 6. Polyclonal antisera raised against the HSPGs reacted against the core proteins. Both HSPG preparations and their antisera showed ca 40% cross-reactivity. About 50% of monoclonal antisera elicited against one HSPG preparation showed reaction with both HSPG preparations. 7. Polyclonal antisera stained all basement membranes in an intense linear fashion in indirect immunofluorescence studies of kidney sections from horse, man and various mammalian species. 8. Biochemical and immunological data indicate that HSPGs from equine and human GBM have a comparable structure, but the core proteins differ considerably. |
| Databáze: | OpenAIRE |
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