Open AccessProteoglycan Structure and Metabolism in Normal and Osteoarthritic Cartilage of Guinea Pigs
Author(s) -
Schwartz Edith R.,
Leveille Cynthia R.,
Stevens Jeff W.,
Oh Won H.
Publication year - 1981
Publication title -
arthritis & rheumatism
Language(s) - English
Resource type - Journals
eISSN - 1529-0131
pISSN - 0004-3591
DOI - 10.1002/art.1780241212
Subject(s) - proteoglycan , glucosamine , cartilage , chemistry , osteoarthritis , biochemistry , sulfation , vitamin , agarose , ascorbic acid , uronic acid , metabolism , in vivo , hydroxyproline , agarose gel electrophoresis , polysaccharide , anatomy , biology , extracellular matrix , pathology , medicine , food science , dna , alternative medicine , microbiology and biotechnology
Sulfated proteoglycan structure and metabolism in osteoarthritic articular cartilage from the hind‐limb joints of guinea pigs in which the disease had been surgically induced were evaluated and compared with those from nonoperated or sham‐operated controls. In these studies, conducted on animals receiving high and low dietary levels of ascorbic acid, the effect of vitamin C on these variables was also examined. Sulfated proteoglycan biosynthesis per unit of DNA as reflected by in vivo uptake of 35 S‐sulfate was stimulated both by arthritic development and high dietary vitamin C. Under these conditions, the specific activities, 35 S‐cpm/μg uronic acid, of the proteoglycans were elevated. Neither arthritic development nor variation in dietary levels of vitamin C altered the structure of the proteoglycans. Two species of proteoglycans that exhibited the same electrophoretic mobilities in agarose/acrylamide gels, the same elution profiles on high performance liquid chromatography, and the same galactosamine/glucosamine ratios were found in all normal and osteoarthritic cartilage specimens tested. The specific activities of these two species were dissimilar. In all samples, the larger of the two species had a higher specific activity.