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Any of various enzymes found in animal tissue that catalyze the hydrolysis of proteins into smaller proteins.

[German Kathepsin, from Greek kathepsein, to digest : kat-, kata-, cata- + hepsein, to boil.]


(Biochemistry) a proteolytic enzyme responsible for the autolysis of cells after death
[C20: from Greek kathepsein to boil down, soften]


(kəˈθɛp sɪn)

any of a class of intracellular enzymes that break down protein in certain abnormal conditions and after death.
[1925–30; < Greek kathéps(ein) to digest]
ca•thep′tic (-tɪk) adj.
References in periodicals archive ?
Background: Cathepsin L (CatL) is a cysteine protease with strong matrix degradation activity that contributes to photoaging.
Laminar Shear Stress Inhibits Cathepsin L Activity in Endothelial Cells.
15) - Pipeline Review, H1 2016', provides in depth analysis on Cathepsin L (EC 3.
Relationship between tenderising the levels of cathepsin B, cathepsin L, calpain I, calpain II, and AY-glucoronidaes.
com)-- AnaSpec is pleased to announce the release of two new SensoLyte[R] assay kits for the measurement of Cathepsin L activity - the SensoLyte[R] 520 and Rh110 Cathepsin L Assay Kits.
DAP I by 429%, DAP II by 355% and DAP IV by 178%, followed by cathepsin L (246%), cathepsin D (123%), tripeptidyl aminopeptidase (109%), arginyl aminopeptidase (78%), alanyl aminopeptidase (72%), leucyl aminopeptidase (49%), cathepsin H (37%) and proline endopeptidase (19%).
Thus elevated activities were found in cathepsin L (by 128%), cathepsin H (by 54%), cathepsin D (by 771%) and soluble protein (by 16%) whereas depleted activities were detected in dipeptidyl aminopeptidase I (by 17%), dipeptidyl aminopeptidase II (by 10%) and catheprill B (by 43%) (Table I and II).