Partial reversal by beta-d-xyloside of salicylate-induced inhibition of glycosaminoglycan synthesis in articular cartilage

✍ Scribed by Marshall J. Palmoski; Kenneth D. Brandt

• Book ID: 102752317
• Publisher: John Wiley and Sons
• Year: 1982
• Tongue: English
• Weight: 882 KB
• Volume: 25
• Category: Article
• ISSN: 0004-3591
• DOI: 10.1002/art.1780250909

✦ Synopsis

Abstract

While net ^35^S‐glycosaminoglycan synthesis in normal canine articular cartilage was suppressed by 10^−3^M sodium salicylate to about 70% of the control value, addition of xyloside (10^−6^M–10^−3^M) to the salicy‐late‐treated cultures led to a concentration‐dependent increase in glycosaminoglycan synthesis, which rose to 120–237% of controls. Similar results were obtained when ^3^H‐glucosamine was used to measure glycosaminoglycan synthesis, confirming that salicylate suppresses and xyloside stimulates net glycosaminoglycan synthesis, and not merely sulfation. Salicylate (10^−3^M) did not affect the activity of xylosyl or galactosyl transferase prepared from canine knee cartilage, and net protein synthesis was unaltered by either salicylate or xyloside. The proportion of newly synthesized proteoglycans existing as aggregates when cartilage was cultured with xyloside was similar to that in controls, although the average hydrodynamic size of disaggregated proteoglycans and of sulfated glycosaminoglycans was diminished.