cathepsin

(redirected from Cathepsin L)
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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.

ca·thep·sin

(kă-thep'sin),
One of a number of intracellular proteinases and peptidases (all endopeptidases) of animal tissues of varying specificities.

cathepsin

/ca·thep·sin/ (kah-thep´sin) one of a number of enzymes each of which catalyzes the hydrolytic cleavage of specific peptide bonds.

cathepsin

(kə-thĕp′sĭn)
n.
Any of various enzymes found in animal tissue that catalyze the hydrolysis of proteins into smaller proteins.

cathepsin

Any ENZYME that acts to split the interior PEPTIDE bonds of a protein, causing its decomposition.

cathepsin

or

kathepsin

the intracellular, proteolytic enzymes that bring about AUTOLYSIS.

cathepsin

a proteinase found in most cells, which takes part in cell autolysis and self-digestion of tissues.

cathepsin D
an acid hydrolase isolated from cartilage which plays a part in the endogenous degradation of proteoglycans in degenerative diseases of joints.
References in periodicals archive ?
Jun and Fos knockdown reduces ultraviolet A-induced cathepsin L expression and activity
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases.
Expression of the human cathepsin L inhibitor hurpin in mice: Skin alterations and increased carcinogenesis.
The report reviews key players involved in Cathepsin L (EC 3.
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%.
Of lysosomal proteases, cathepsin L, cathepsin H and soluble proteins also exhibited further increased activities in daed than living M.