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• W94723644 endingPage "352" @default.
• W94723644 startingPage "325" @default.
• W94723644 abstract "The name cathepsin is derived from a Greek word meaning to digest and was used originally for acidic proteases, with the letters designating individual enzymes [1,2]. Examples of cathepsins are found in three classes of proteases, for example, cathepsin D is an aspartic protease, cathepsin B a cysteine protease, and cathepsin G is a serine protease. Although several cathepsins have collagenolytic activity, there are no cathepsins among the metalloproteases. Most cathepsins are lysosomal proteases with acidic pH optima ranging from the extremely acidic pH optimum of cathepsin D (i.e., pH 2.8) to the slightly acidic pH optimum of cathepsin B (i.e., pH 6.5). On the other hand, cathepsin E has an acidic pH optimum (i.e., pH 3.0) yet is not lysosomal [3], and cathepsin S has a neutral pH optimum yet is lysosomal [4]. The lysosomal cathepsins are synthesized as pre-proenzymes and acquire N-linked oligosaccharides cotranslationally. Their maturation involves proteolytic processing and modification of the oligosaccharides, processes that occur during their trafficking to the lysosome and that affect their ability to bind to receptors that target them to the lysosomes [5–7]. As indicated earlier, the cathepsins are primarily endopeptidases, hydrolyzing internal peptide bonds. However, cathepsin H is an exopeptidase of the aminopeptidase class [8], and cathepsin B has both endopeptidase and exopeptidase activities, the latter as a carboxydipeptidase [9]." @default.
• W94723644 created "2016-06-24" @default.
• W94723644 creator A5059642830 @default.
• W94723644 creator A5088763474 @default.
• W94723644 date "1996-01-01" @default.
• W94723644 modified "2023-09-24" @default.
• W94723644 title "Cathepsins D and B in breast cancer" @default.
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