The following article is from The Great Soviet Encyclopedia (1979). It might be outdated or ideologically biased.

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).

Mentioned in

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

EFFECT OF THE MUSCLE BIOCHEMICAL CHARACTERISTICS ON THE TENDERNESS OF AGED MEAT IN YOUNG GOATLING (CAPRA NUBIANA) ANIMALS

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).

Proteases and protease inhibitors of urinary extracellular vesicles in diabetic nephropathy

Another protein, cathepsin B is involved in all stages of neoplastic transformation, such as tumor growth, angiogenesis, invasion and metastasis.

Comparison of expression of selected proteins in the cells of intestinal and diffuse type gastric cancer--immunohistochemical analysis

[89.] Canuel M, Korkidakis A, Konnyu K, Morales CR (2008) Sortilin mediate the lysosomal targeting of cathepsins D and H.

Two faces of Cathepsin D: physiological guardian angel and pathological demon

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.

Antidepressant fluoxetine modulates the in vitro inhibitory activity of buffalo brain cystatin: a thermodynamic study using UV and fluorescence techniques

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).

Studies of inhibitory mechanisms of propeptide-like cysteine protease inhibitors

Purification and characterization of cathepsins D from Japanese monkey lung.

Structure and function studies on enzymes with a catalytic carboxyl group(s): from ribonuclease [T.sub.1] to carboxyl peptidases

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].

Studies on interaction of buffalo brain cystatin with donepezil: an Alzheimer's drug

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.

Investigation on Autolytic Processes and Microstructural Changes in Red Deer Meat

Murohara, "Cysteine protease cathepsins in atherosclerosis-based vascular disease and its complications," Hypertension, vol.

Dilating Vascular Diseases: Pathophysiology and Clinical Aspects

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].

Preventing Soft Texture Fish Fillets through Brine Injection Technology