4.7 Review

Cathepsin H: Molecular characteristics and clues to function and mechanism

Journal

BIOCHEMICAL PHARMACOLOGY
Volume 212, Issue -, Pages -

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bcp.2023.115585

Keywords

Cathepsin H; Protease maturation; Protease substrate; Inhibitor; Pathophysiology

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CatH is a lysosomal cysteine protease with a unique aminopeptidase activity that is extensively expressed in various organs. Its specific enzymatic activity has critical effects on cancer cells and brain diseases. This review summarizes the expression, maturation, and enzymatic properties of CatH, and discusses the potential of CatH inhibitors in disease therapy.
Cathepsin H (CatH) is a lysosomal cysteine protease with a unique aminopeptidase activity that is extensively expressed in the lung, pancreas, thymus, kidney, liver, skin, and brain. Owing to its specific enzymatic activity, CatH has critical effects on the regulation of biological behaviours of cancer cells and pathological processes in brain diseases. Moreover, a neutral pH level is optimal for CatH activity, so it is expected to be active in the extra-lysosomal and extracellular space. In the present review, we describe the expression, maturation, and enzymatic properties of CatH, and summarize the available experimental evidence that mechanistically links CatH to various physiological and pathological processes. Finally, we discuss the challenges and potentials of CatH in-hibitors in CatH-induced disease therapy.

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