The effects of trypsin treatment on proteoglycan biosynthesis by bovine articular cartilage.
The effects of mild or severe trypsin treatment of bovine articular-cartilage slices in tissue culture were studied by monitoring the incorporation of [35S]sulphate into proteoglycans. Moderate trypsin treatment caused a subsequent marked inhibition of proteoglycan biosynthesis, which was reversible with time. Analysis on Sepharose CL-2B of the proteoglycan species synthesized showed that, directly after trypsin treatment, there was a 30% increase in the synthesis of the low-Mr proteoglycan (Kav. 0.71), and the total decrease in proteoglycan biosynthesis was reflected in a decrease in the synthesis of the high-Mr proteoglycan species (Kav. 0.31). The small proteoglycan was partially characterized and shown to be a true biosynthetic product and not a breakdown product. Trypsin treatment (20 micrograms/ml per 100 mg of tissue) of cartilage slices also resulted in an increase in the glycosaminoglycan chain size of the large proteoglycan, but not of the small proteoglycan.
D000818:Animals; D002358:Cartilage, Articular / Q000187:drug effects / Q000378:metabolism*; D002417:Cattle; D002499:Centrifugation, Density Gradient; D002850:Chromatography, Gel; D046508:Culture Techniques; D006025:Glycosaminoglycans / Q000378:metabolism; D007930:Leucine / Q000378:metabolism; D011509:Proteoglycans / Q000096:biosynthesis*; D013431:Sulfates / Q000378:metabolism; D014357:Trypsin / Q000494:pharmacology*
D006025:Glycosaminoglycans; D011509:Proteoglycans; D013431:Sulfates; D014357:Trypsin; D007930:Leucine