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Human Cathepsin O2, a Matrix Protein-degrading Cysteine Protease Expressed in Osteoclasts
Its capacity to efficiently degrade Type I collagen and its high expression in osteoclasts suggest that cathepsin O2 may play a major role in human osteoclastic bone resorption.
Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization.
The high sequence identity and the overlapping chromosomal gene loci suggest that both proteases evolved from an ancestral cathepsin L-like precursor by gene duplication.
Cathepsin V, a Novel and Potent Elastolytic Activity Expressed in Activated Macrophages*
It is demonstrated that macrophages express a third elastolytic cysteine protease, cathepsin V, which exhibits the most potent elastase activity yet described among human proteases and that cathePSin V is present in atherosclerotic plaque specimens.
Vinyl sulfones as mechanism-based cysteine protease inhibitors.
Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins.
The purification method for cathepsin S from bovine spleen involved (NH4)2SO4 fractionation, chromatography on CM-Sephadex C-50, gel filtration on Sephacryl S-200 and chromatofocusing.
Role of Cysteine Cathepsins in Extracellular Proteolysis
The development of cathepsin inhibitors as anti matrix-degrading drugs appears to be a successful strategy.
Substrate Profiling of Cysteine Proteases Using a Combinatorial Peptide Library Identifies Functionally Unique Specificities*
The substrate specificities of papain-like cysteine proteases and human cathepsins L, V, K, S, F, B, and five proteases of parasitic origin were studied using a completely diversified positional scanning synthetic combinatorial library.
Regulation of Collagenase Activities of Human Cathepsins by Glycosaminoglycans*
It is demonstrated that complex formation with glycosaminoglycans (GAGs) is unique for cathepsin K among human papain-like cysteine proteases and that different GAGs compete for the binding to cathePSin K, suggesting a novel mechanism for the regulation of matrix protein degradation by G AGs.