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cathepsin

Cathepsin is a cysteine proteinase that degrades elastin and fibrillar collagen. In addition, cathepsin is an endopeptidase associated with lysosomes in the cell, often with low pH optimum.

Cathepsins are involved in intralysosomal protein degradation and in a wide range of other physiological and pathological processes. Because of their broad specificity, the cathepsins can obviously compensate for one another.

Cathepsins fulfill a unique role among lysosomal proteases. Cathepsins are classified based on their structure and catalytic type into serine (cathepsins A and G), aspartic (cathepsins D and E, present in endosomes), and the most prominent cathepsin family of cysteine cathepsins (cathepsins B, C, F, H, K, L, O, S, V, W, and X), with cathepsins B, C, D, and L being ubiquitously expressed, while the rest exhibit a tissue- or cell-type-specific expression.

Cathepsins are also synthesized as inactive pre-proenzymes and undergo posttranslational glycosylation. The activity of cathepsins is regulated at different levels. First, the transcription of cathepsin genes is controlled by cell-type-specific mechanisms and exogenous factors. Thus, different cell types do express different cathepsins.

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