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 ?
Keywords: Breast carcinoma, Cathepsin D, immunohistochemistry, metastasis
Cathepsin D is a lysosomal aspartyl protease which acts as a mature active enzyme in the lysosomes in an acidic pH and synthesized by stromal reactive cells and macrophages.
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. Slides were examined by comparing the aforesaid clinicopathological parameters.
Newly diagnosed type 2 diabetic patients had significantly higher levels of cathepsin D in BMI, systolic blood pressure (BP), diastolic BP, total cholesterol, LDL cholesterol, and triglyceride than those in control subjects.
Of note, compared with the control group, circulating cathepsin D concentrations in newly diagnosed type 2 diabetic patient group were significantly increased (median level: 227 ng/ml versus 174 ng/ml, P < 0.01) (Table 1).
Similarly, the protective effects of RSV on the expression and activity of mature cathepsin D were also abolished by SIRT1 siRNA (Figures 5(b), 5(f), and 5(g)).
The most important proteinase for LDL degradation is cathepsin D [32].
[11.] Reid WA, Valler MJ, Kay J (1986) Immunolocalization of cathepsin D in normal and neoplastic human tissues.
[13.] Moallem SA, Hales BF (1995) Induction of apoptosis and cathepsin D in limbs exposed in vitro to an activated analog of cyclophosphamide.
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%.
Thus the head contained highest concentrations of arginyl aminopeptidase, leucyl aminopeptidase, tripeptidyl aminopeptidase, proline endopeptidase, and cathepsin D, while the gut contained highest levels of all lysosomal proteases tested in this study (except cathepsin D, which was highest in the thorax part) as well as alanyl aminopeptidase and dipeptidyl aminopeptidase IV out of cytoplasmic proteases.
On the other hand cathepsin D was depleted in living flies but exhibited drastically raised levels in dead flies while the remaining lysosomal proteases were left undisturbed except cathepsin B which was decreased further in dead than living flies.