cathepsin

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cathepsin

[kə′thep·sən]
(biochemistry)
Any of several proteolytic enzymes occurring in animal tissue that hydrolyze high-molecular-weight proteins to proteoses and peptones.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
References in periodicals archive ?
Cathepsin L activity (n = 8/treatment) was measured to evaluate protease inhibition.
Figure 2 shows the levels of DNA fragmentation, cathepsin B C/L ratio, cathepsin L C/L ratio, and caspase-3 activity in the cardiac tissues of control and experimental rats.
Mann et al., "Effective activation of the proenzyme form of the urokinase-type plasminogen activator (pro-uPA) by the cysteine protease cathepsin L," FEBS Letters, vol.
Ultraviolet A enhances cathepsin L expression and enzymatic activity
The report provides comprehensive information on the Cathepsin L (EC 3.4.22.15), targeted therapeutics, complete with analysis by indications, stage of development, mechanism of action (MoA), route of administration (RoA) and molecule type.
Decreases in the expressions (mRNA) of cathepsin B and cathepsin L were also observed on the 10th day after DM induction, suggesting that the lower gene expression may be one of the mechanisms responsible for the lower enzyme activities.
For the inhibition studies, mouse cathepsin L (CtsL) and Bombyx cysteine protease (BCP), both of which belong to a papain family (C1A) in the MEROPS peptidase database, were employed.
Hydrolysis of the FRET substrate by active Cathepsin L results in increase of HiLyte Fluor[TM] 488 fluorescence.
americana has highest activities of dipeptidyl aminopeptidase I (52 nmol/h/mg protein), dipeptidyl aminoepeptidase II (20 nmol/h/mg protein), cathepsin B (622 nmol/h/mg protein), cathepsin L (2409 nmol/h/mg protein) and cathepsin H (49 nmol/h/mg protein) followed by abdomen in the case of first four types of proteases and by head in case of the last type of protease.
Rudensky, "A role for cathepsin L and cathepsin S in peptide generation for MHC class II presentation," Journal of Immunology, vol.
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).
Its identified peptidic fraction preserves fibers of the elastic and collagen networks in the skin by favoring the synthesis of molecules involved in the organization of the fibril network (collagens, fibrillin) and also by limiting their degradation by enzymes such as MMP-1, -2 and cathepsin L.