cathepsin

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ca·thep·sin

 (kə-thĕp′sĭn)
n.
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.

cathepsin

(kəˈθɛpsɪn)
n
(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

ca•thep•sin

(kəˈθɛp sɪn)

n.
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 ?
Speed of pH decline and decline rate of the cathepsins activity and myofibrillar toughness in Longissimus (L), Semimembranosus (SM) and Semitendinosus (ST) of goatlingmuscles.
The proteolytic activities of specific group of proteases in normo-, micro- and macroalbuminuric HFDa fractions were assayed using 0.1 mM glycyl-prolyl-p-nitroanilide (GP-pNA) and 0.25 mM N-benzoyl-proline-phenylalanine-arginine-p-nitroanilide (Be-PFR-pNA), N-methoxysuccinyl-alanine-alanine-proline-valine-p-nitroanilide (Me-AAPV-pNA), and succinyl-alanine-alanine-proline-phenylalanine p-nitroanilide (Suc-AAPFpNA) chromogenic substrate of chromogenic substrates to establish activity of DPP IV, Kallikreins, proteinase 3, and cathepsins, respectively [23, 33-35].
We hypothesize that cadmium induces lysosomes to permeabilize, release cathepsins, leading to apoptosis in osteoblast-like cells Saos-2 and MG-63.
Apart from MMP, matrix and fibrous cap degradation is also activated by cathepsins and other elastolytic enzymes (Table 1) [6].
Cystatin C, is a small ubiquitously expressed protein found in nearly all body fluids, and is the most potent endogenous extracellular inhibitor of cysteine cathepsins [91].
Cystatins the crucial inhibitors for proper brain functioning have been reported from several mammalian sources and an imbalance of proteinases (cathepsins) with their endogenous inhibitor cystatins is closely associated with senile plaque, cerebrovascular amyloid deposits, and neurofibrillary tangles in Alzheimer's disease.
Similar findings have been reported for the propeptides of cathepsins [31, 33, 34].
Physarolisins as well as arabidopsins are the only major intracellular enzymes, in addition to cathepsins D and E, among the three types of peptidases studied, and elucidation of their physiological roles is awaited.
Recent researches have shown that cathepsins are involved the processing of certain neuropeptides in the central nervous system (CNS) [12]where cystatin Cisalso present in high concentration and their concentration is suggested to play an important role in brain diseases.
The research into the activity of tissue enzymes were also assessed - with regards to cathepsins and calpains - in the muscular fiber of red deer meat.