cathepsin

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cathepsin

 [kah-thep´sin]
an endopeptidase found in most cells, which takes part in cell autolysis and self-digestion of tissues.
Miller-Keane Encyclopedia and Dictionary of Medicine, Nursing, and Allied Health, Seventh Edition. © 2003 by Saunders, an imprint of Elsevier, Inc. All rights reserved.

ca·thep·sin

(kă-thep'sin),
One of a number of intracellular proteinases and peptidases (all endopeptidases) of animal tissues of varying specificities.
Farlex Partner Medical Dictionary © Farlex 2012

cathepsin

(kə-thĕp′sĭn)
n.
Any of various enzymes found in animal tissue that catalyze the hydrolysis of proteins into smaller proteins.
The American Heritage® Medical Dictionary Copyright © 2007, 2004 by Houghton Mifflin Company. Published by Houghton Mifflin Company. All rights reserved.

cathepsin

Any ENZYME that acts to split the interior PEPTIDE bonds of a protein, causing its decomposition.
Collins Dictionary of Medicine © Robert M. Youngson 2004, 2005

cathepsin

or

kathepsin

the intracellular, proteolytic enzymes that bring about AUTOLYSIS.
Collins Dictionary of Biology, 3rd ed. © W. G. Hale, V. A. Saunders, J. P. Margham 2005
References in periodicals archive ?
Two-Way ANOVA with main effects as treatment and test method pH (pH 5.5 or ultimate pH) were used to analyze cathepsin L. The least significant difference (LSD) was used to determine if significant differences occurred between treatments.
Cathepsin L activity was measured at both the optimum pH for enzyme activity (pH 5.5) and ultimate pH (Figure 2).
the current study measured the levels of DNA fragmentation, cathepsin B C/L ratio, cathepsin L C/L ratio and activity of caspase in the heart tissue ofall groups.
Inhibition of JNK pathway impairs ultraviolet A-induced cathepsin L expression and enzymatic activity
Jun and Fos knockdown reduces ultraviolet A-induced cathepsin L expression and activity
* The report provides a snapshot of the global therapeutic landscape for Cathepsin L (EC 3.4.22.15)
* The report reviews Cathepsin L (EC 3.4.22.15) targeted therapeutics under development by companies and universities/research institutes based on information derived from company and industry-specific sources
Expression (mRNA) of cathepsin B, cathepsin L, and [beta]-D-glucuronidase in diabetic (DM) and normal (NL) rat livers.
For inhibition studies of CTLA-2[alpha], purification of recombinant mouse cathepsin L (CtsL) was performed according to the method described by Kramer et al.
Cathepsin L, a lysosomal endopeptidase, is a member of the papain-like family of cysteine proteinases (1).
Thus dipeptidyl aminopeptidase I was increased by 429%, dipeptidyl aminopeptidase II by 355%, cathepsin L by 246%, cathepsin H by 37% and cathepsin D by 123%.
Hence capthesin B and soluble proteins manifested elevated activities by 14% and 32%, respectively while dipeptidyl aminopeptidase I, dipeptidyl aminopeptidase II, cathepsin L, cathepsin H and cathepsin D were depleted by 27%, 21%, 66%, 44% and 39%, respectively.