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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.]
American Heritage® Dictionary of the English Language, Fifth Edition. Copyright © 2016 by Houghton Mifflin Harcourt Publishing Company. Published by Houghton Mifflin Harcourt Publishing Company. All rights reserved.


(Biochemistry) a proteolytic enzyme responsible for the autolysis of cells after death
[C20: from Greek kathepsein to boil down, soften]
Collins English Dictionary – Complete and Unabridged, 12th Edition 2014 © HarperCollins Publishers 1991, 1994, 1998, 2000, 2003, 2006, 2007, 2009, 2011, 2014


(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.
Random House Kernerman Webster's College Dictionary, © 2010 K Dictionaries Ltd. Copyright 2005, 1997, 1991 by Random House, Inc. All rights reserved.
References in periodicals archive ?
The activities of lysosomal enzymes ([beta]-glucuronidase, [beta]-N-acetylglucosaminidase, b-galactosidase, cathepsin B, and cathepsin D) were increased significantly in serum and the heart of iso-induced myocardial-infarcted rats (40, 41).
The hypothesis that increased levels of adhesion molecules and Cathepsin D affect cancerous cells moving away the primary tumor and contributes to migration of the cancerous cell and may cause remote organ metastases is defended.
In all groups, 20 paraffin blocks belonging to the primary tumor in the breast were stained by ICAM-1, VCAM-1, Cyclin D1 and Cathepsin D. Findings were examined by comparing with clinicopathological parameters.
Oakley et al., "Inhibition of lysosomal protease cathepsin D reduces renal fibrosis in murine chronic kidney disease," Scientific Reports, vol.
Recently, altered circulating cathepsin D levels have been described in two large community cohorts with prevalent insulin resistance by using proximity extension assay [7].
Despite the important roles of cathepsin D in many physiological and pathological conditions, whether its circulating levels associated with diabetes and clinical variable remain to be established.
This function is dependent on lysosomal proteases, most importantly, the cysteine cathepsins and the aspartic protease cathepsin D [3].
By late 1959, the fourth member of the family was identified as "Cathepsin D" (CatD) [5].
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%).
While OSM induced specific proteases in particular cell lines, cathepsin D was the one protease consistently induced in the majority of cell lines examined.
A report in Annals of Neurology (2000;47:399-403) points to the intracellular acid protease cathepsin D (catD) as an important risk factor for Alzheimer's disease.
Assay of cathepsin D activity was based on the spectrophotometric procedures of Pennington (1977) and Pluskal et al.