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Cathepsin H (CatH) is a lysosomal cysteine protease distinguished by its unique dual aminopeptidase and endopeptidase activities. Unlike other cathepsins, it includes a disulfide-linked mini-chain that anchors substrate N-termini via electrostatic interactions, enabling sequential cleavage of N-terminal basic residues (Arg/Lys). This exopeptidase function, optimal at neutral pH, facilitates its role in extracellular spaces, while its endopeptidase activity at acidic pH (4.5–5.5) supports lysosomal protein degradation.
Therapeutically, CatH’s role in neuropeptide processing (e.g., enkephalin and galanin biosynthesis) highlights its potential in pain management and neurodegenerative therapies. Inhibitors targeting its active site (e.g., E-64) reduce tumor invasion in preclinical models, while pH-selective compounds (Z-Arg-NHMec) spare lysosomal functions. Diagnostic applications leverage its elevated expression in gliomas and breast cancers for early detection and stratification. These multifunctional roles position CatH as a critical node in both lysosomal proteostasis and disease pathogenesis.
Common uses include proteolytic enzyme studies, neurological research, cancer research.
Not a hazardous substance or mixture.
12 - Non Combustible Liquids
