The effects of trypsin treatment on proteoglycan biosynthesis by bovine articular cartilage

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Abstract
The effects of mild or severe trypsin treatment of bovine articular-cartilage slices in tissue culture were studied by monitoring the incorporation of [35S]sulfate 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-MW proteoglycan (Kav. 0.71) and the total decrease in proteoglycan biosynthesis was reflected in a decrease in the synthesis of the high-MW proteoglycan species (Kav. 0.31). The small proteoglycan was partially characterized and shown to be a true biosynthesis product and not a breakdown product. Trypsin treatment (20 .mu.g/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 same proteoglycan.

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