cathepsin

(redirected from Cathepsin d)
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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 ?
4C3), Cyclin D1/Bcl-1 (SP4), Cathepsin D Ab-1 antibodies.
For positive controls, tonsil tissue for ICAM-1, placenta for VCAM-1, an intestinal tissue diagnosed with mantle zone lymphoma for cyclin D1, a hepatic tissue for cathepsin D, breast tissue for ER/PR and positive stained breast carcinoma for cerbB2 were used.
A statistically significant difference was found between the groups for cathepsin D (Table 3).
Cathepsin D is a proteolytic enzyme which was first identified in 1980 and released by cancerous and stromal cells.
RSV restored the function of lysosomes through an increase of the protein expression and activity of mature cathepsin D, which contributes to the completed autophagic flux.
The protective effects of RSV, which included upregulating the expression of mature cathepsin D and increasing cathepsin D activity, were also blocked and accompanied by accumulation of Ox-LDL in HUVECs after knockdown of SIRT1.
Western blotting analysis of the protein level of LAMP1 (c) and cathepsin D (d) after HUVEC pretreatment with 50 [micro]M resveratrol for 1 h, and subsequently incubation with Ox-LDL (60 [micro]g/mL) for 12 h.
Western blot analysis of SIRT1, LC3-II, p62, and cathepsin D (b-f).
Cavailles V, Augereau P, Rochefort H (1993) Cathepsin D gene is controlled by a mixed promoter, and estrogens stimulate only TATA-dependent transcription in breast cancer cells.
Touitou I, Cavailles V, Garcia M, Defrenne A, Rochefort H (1989) Differential regulation of cathepsin D by sex steroids in mammary cancer and uterine cells.
Wang F1, Duan R, Chirgwin J, Safe SH (2000) Transcriptional activation of cathepsin D gene expression by growth factors.
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.