Cathepsins


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Related to Cathepsins: Cathepsin L

Cathepsins

 

intracellular proteinases of the hydrolase class that catalyze the hydrolysis of the peptide bond in peptides and proteins.

Cathepsins are widely distributed in animal and plant tissues and in microorganisms. Cathepsins are divided according to the character and specificity of enzymic action into endopeptidases, which are capable of hydrolyzing internal peptide bonds in the molecules of proteins and peptides, and exopeptidases, which act solely on compounds with one or more free terminal carboxyl or amino groups. Cathepsins can also catalyze reactions that may result in lengthening the peptide chain. Almost all cathepsins are activated by compounds containing sulfhydryl groups (cysteine, glutathione).

References in periodicals archive ?
Speed of change Cathepsins B+L activity###2.74E-041.14E-05a###3.18E-048.69E-06b###2.37E-041.32E-05c
Beside the relative quantitative amount we checked the activity of some of these proteases by gelatine zymography for metalloproteases (Figure 4) which confirmed a clear increase of gelatinase activity in the normoalbuminuric group and by chromogenic substrates for DPP IV, Kallikreins, cathepsins, and PRTN3 (Figure 5).
In addition, LDL particles interact with proteoglycans (biglycan and decorin) and form aggregates, with a catalytic activity of sphingomyelinase, cathepsin D, cathepsin F and lysosomal acid lipase [15].
Another protein, cathepsin B is involved in all stages of neoplastic transformation, such as tumor growth, angiogenesis, invasion and metastasis.
[89.] Canuel M, Korkidakis A, Konnyu K, Morales CR (2008) Sortilin mediate the lysosomal targeting of cathepsins D and H.
Brown et al., "L-transepoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L," Biochemical Journal, vol.
were the first to show that mouse-activated T cells and mast cells expressed the mRNA encoding proteins, cytotoxic T-lymphocyte antigen-2s (CTLA-2[alpha] and CTLA-2[beta]), which were shown to be highly homologous to the proregions of mouse cathepsin L [1] (Figure 1).
Cystatins constitute a powerful regulatory system for endogenous cysteine proteinases (cathepsins) which are of ten secreted or leaking from the lysosomes of dying or diseased cells [13].
Results of the conducted research showed that during the process of autolysis, the release of cathepsins in the muscular tissues of red deer occurs as well as the manifestation of its activity (Fig.
Murohara, "Cysteine protease cathepsins in atherosclerosis-based vascular disease and its complications," Hypertension, vol.
The main proteolytic system which is attributed to the weakening of myofibrillar proteins in fish is lysosomal cathepsins. A considerable number of articles have demonstrated the contribution of endogenous muscle protease enzymes to textural degradation of fish during iced, refrigerated, or frozen storage and thermal processing [1-3].