Heparan sulfate proteoglycan from human and equine glomeruli and tubules.
- Comparative Study
- Journal Article
Summary
The research article explores the extraction and study of proteoglycans from human and horse glomeruli or tubules. The composition, characteristics and differences of these proteoglycans are examined in detail.
Methodology and Initial Findings
The researchers utilized a method known as guanidine extraction and anion exchange chromatography to isolate proteoglycans from both human and horse glomeruli or tubules. They found that:
- The proteoglycan preparations contained approximately equal amounts of heparan sulfate and chondroitin sulfates.
- During the preparation of glomerular or tubular basement membranes, more than 50% of the proteoglycans were extracted in the salt extract.
- Chondroitin sulfate proteoglycan was mainly found in water and salt extracts of glomeruli and tubules and heparan sulfate proteoglycan was found in the deoxycholate extracts and basement membranes.
Further Exploration on Glomerular Basement Membrane (GBM)
The researchers calculated the proportion of proteoglycans in glomerulus, noting that:
- The GBM contains about 12% (human) or 20% (equine) of the proteoglycans of the total glomerulus.
- The proteoglycans in GBM consist of more than 70% (equine) or 80% (human) of heparan sulfate.
Heparan Sulfate Proteoglycan Isolation
Further analysis and treatment of the proteoglycan preparations resulted in the following findings:
- Heparan sulfate proteoglycan was isolated from the proteoglycan preparations of human or equine glomeruli and tubules by additional treatment with nucleases and chondroitinase ABC.
- This was followed by CsCl gradient centrifugation.
- Protein was found to account for about 40% (dry weight) of the heparan sulfate proteoglycans.
- The amino acid composition of the proteoglycans is characterized by a high content of glycine, however, 3-hydroxyproline, 4-hydroxyproline, and hydroxylysine were found to be lacking.
Comparison of Proteoglycans
The final part of the analysis compared the biochemical characteristics of the proteoglycans from human, equine and rat glomeruli. The scientists found out that:
- The proteoglycans from human or equine glomeruli or tubules differed from those isolated from rat glomeruli.
- The distinction was noted in their higher protein content and their amino acid composition.
- The researchers discussed the potential significance of these differences.
Cite This Article
Publication
Researcher Affiliations
- Department of Biochemistry, University of Nijmegen, The Netherlands.
MeSH Terms
- Amino Acids / analysis
- Animals
- Borohydrides / pharmacology
- Chondroitin Sulfate Proteoglycans / analysis
- Chondroitin Sulfate Proteoglycans / isolation & purification
- Chromatography, DEAE-Cellulose
- Electrophoresis, Cellulose Acetate
- Glycosaminoglycans / isolation & purification
- Glycosaminoglycans / metabolism
- Heparan Sulfate Proteoglycans
- Heparitin Sulfate / analysis
- Heparitin Sulfate / isolation & purification
- Horses
- Humans
- Kidney Glomerulus / analysis
- Kidney Tubules / analysis
- Membranes
- Nitrous Acid / pharmacology
- Proteoglycans / isolation & purification
Citations
This article has been cited 1 times.- van den Heuvel LP, van den Born J, van de Velden TJ, Veerkamp JH, Monnens LA, Schroder CH, Berden JH. Isolation and partial characterization of heparan sulphate proteoglycan from the human glomerular basement membrane. Biochem J 1989 Dec 1;264(2):457-65.