Age-related changes in the composition and structure of human articular-cartilage proteoglycans.
1. Analysis of the purified proteoglycans extracted from normal human articular cartilage with 4M-guanidinium chloride showed that there was an age-related increase in their content of protein and keratan sulphate. 2. The hydrodynamic size of the dissociated proteoglycans also decreased with advancing age, but there was little change in the proportion that could aggregate. 3. Results suggested that some extracts of aged-human cartilage had an increased content of hyaluronic acid compared with specimens from younger patients. 4. Dissociated proteoglycans, from cartilage of all age groups, bind to hyaluronic acid and form aggregates in direct proportion to the hyaluronic acid concentration. 5. Electrophoretic heterogeneity of the dissociated proteoglycans was demonstrated on polyacrylamide/agarose gels. The number of proteoglycan species observed was also dependent on the age of the patient.
D000293:Adolescent; D000328:Adult; D000368:Aged; D000375:Aging; D002358:Cartilage, Articular / Q000032:analysis*; D002499:Centrifugation, Density Gradient; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006820:Hyaluronic Acid / Q000378:metabolism; D046911:Macromolecular Substances; D008875:Middle Aged; D011506:Proteins / Q000032:analysis; D011509:Proteoglycans / Q000032:analysis* / Q000302:isolation & purification; D014574:Uronic Acids / Q000032:analysis
D046911:Macromolecular Substances; D011506:Proteins; D011509:Proteoglycans; D014574:Uronic Acids; D006820:Hyaluronic Acid