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• W2134260140 abstract "The acceleration effect of chondroitin-4-sulfate(CS-) proteoglycan on the processing of procathepsin L in vitro was investigated using enzyme purified from the culture medium of MLC cells. Procathepsin L was slightly processed even when it was incubated without CS-proteoglycan for 60 min in 50 mm acetate buffer, pH 5.5, and trace amounts of the 31 kDa mature form and 35-38 kDa intermediates of cathepsin L were formed. On the other hand, in the presence of CS-proteoglycan, procathepsin L was completely converted to the mature form within the same 60 minute time period. Moreover, Z-Phe-Arg-MCA hydrolyzing activity was increased significantly by the incubation with CS-proteoglycan, while no considerable increase in the activity was observed during the incubation without CS-proteoglycan. Since the specific cathepsin L inhibitor, CLIK-195, inhibited the processing of procathepsin L accelerated by CS-proteoglycan, the trace amount of cathepsin L activity may participate in the processing. These results suggest that CS-proteoglycan may play a role in accelerating the processing of procathepsin L as an endogenous enhancer in the extracellular environment in vivo." @default.
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• W2134260140 date "2002-01-09" @default.
• W2134260140 modified "2023-10-13" @default.
• W2134260140 title "Chondroitin Sulfate Proteoglycan Is a Potent Enhancer in the Processing of Procathepsin L" @default.
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• W2134260140 doi "https://doi.org/10.1515/bc.2002.216" @default.
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