cathepsin


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Related to cathepsin: Cathepsin C

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.]

cathepsin

(kəˈθɛpsɪn)
n
(Biochemistry) a proteolytic enzyme responsible for the autolysis of cells after death
[C20: from Greek kathepsein to boil down, soften]

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.
References in periodicals archive ?
During further maturing, the lysosome membrane permeability was increased and an active release of cathepsin D was observed as well as increase in the concentration of hydrogen ions in the sarcoplasm of the muscular fiber.
The activities of cathepsin K in BALF and serum were measured by ELISA kit according to the manufacturer's instruction.
Cathepsin L activity (n = 8/treatment) was measured to evaluate protease inhibition.
Seyrantepe, "Lysosomal cathepsin A plays a significant role in the processing of endogenous bioactive peptides," Frontiers in Molecular Biosciencies, vol.
Levy, "Conversion of angiotensin I to angiotensin II by cathepsin A isoenzymes of porcine kidney," Biochemical and Biophysical Research Communications, vol.
Recent data show that LF can serve as an allosteric enhancer of the proteolytic activity of cathepsin G [58].
Many members of the cysteine, cathepsin, and MMP subfamilies are potent elastases and/or collagenases that mediate the degradation of these ECM proteins, leading to AAA expansion and rupture [97, 98].
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.
The inheritance is autosomal recessive and the point of mutation is the gene for cathepsin C (CTCS), a lysosomal protease, which lies on chromosome (11q14-q21).16,17 In this case, genetic testing could not be performed to identify the gene mutation because of the low economic status of the guardians, but the dermatological, dental findings and paraclinical features strongly suggested the diagnosis of PLS.
The hypothesis that increased levels of adhesion molecules and Cathepsin D affect cancerous cells moving away the primary tumor and contributes to migration of the cancerous cell and may cause remote organ metastases is defended.
Cathepsin A (CathA) is a ubiquitously expressed component of a lysosomal multienzyme complex (LMC) with independent protective and catalytic functions [1, 2].