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. 1978 Apr 1;171(1):149–154. doi: 10.1042/bj1710149

Studies on cathepsin B in human articular cartilage.

M T Bayliss, S Y Ali
PMCID: PMC1184144  PMID: 417724

Abstract

The thiol proteinase cathepsin B (EC 3.4.22.1), previously called cathepsin B1, was assayed in human articular cartilage by its hydrolysis of the synthetic substrate alpha-N-benzoyl-DL-arginine 2-naphthylamide. The enzyme was activated by cysteine and EDTA and completely inhibited by iodoacetamide and HgCl2. It was also partially inhibited by whole human serum. Human osteoarthrotic cartilage had increased activity when compared with normal cartilage. Cathepsin B activity of normal cartilage was age-related, being high in juveniles and declining to low values in adult and elderly individuals. Cathepsin D and cathepsin B both exhibited a zonal variation through the cartilage depth; the surface cells appeared to contain more activity than those close to the subchondral bone.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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