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Cathepsin H is a lysosomal cysteine protease in the papain family, encoded by the CTSH gene in humans. It is unique among cathepsins for its predominant aminopeptidase activity, although it can also function as an endopeptidase. Synthesized as a proenzyme, cathepsin H is proteolytically processed into a heavy and light chain and retains a mini-chain essential for its aminopeptidase activity. It plays a major role in lysosomal protein degradation and is involved in diverse physiological processes such as intracellular turnover, extracellular matrix remodeling, and activation of cytotoxic granule components in immune cells. Cathepsin H shows increased expression in various pathologies, including cancers (notably prostate), inflammation, and infection, and is explored as a potential therapeutic target and disease biomarker. Endogenous cystatin family inhibitors tightly regulate its activity, while pharmacological inhibition remains an area of therapeutic research.
Proteolytic inhibition (blocking cysteine protease activity), Modulation of aminopeptidase activity
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