calpains


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Related to calpains: Cathepsins

cal·pains

(kal'pānz),
Calcium-dependent thiol proteinases that are cytoplasmic mammalian enzymes. Calpains of different types react in varying degrees to concentrations of calcium ions.
[calcium + suffix -pain, protease, fr. papain]

calpains

A family of proteolytic enzymes with cysteine in the catalytic site (cysteine proteases). Calpains modulate cell function, some in specific tissues, some ubiquitously. They have been implicated in a range of diseases including cancer, multiple sclerosis, diabetes, Alzheimer's disease and cataracts.
References in periodicals archive ?
The non-significant improvement in texture in the BF muscle may be related to the low calpain values (Koohmaraie, Seideman, Schollmeyer, Dutson & Babiker, 1988), as well as the high collagen level (Hildrum et al.
Relationship between tenderising the levels of cathepsin B, cathepsin L, calpain I, calpain II, and AY-glucoronidaes.
Calpain zymography with casein or fluorescein isothiocyanate casein.
Calpain cleavage and inactivation of the sodium calcium exchanger-3 occur downstream of A13 in Alzheimer's disease.
1) and degradation (Table 1) of A[beta] are performed by proteases and because proteases such as calpain (127) and caspase (128,129) may be involved in the downstream pathological cascade.
RIP kinases, PARP1, NADPH oxidases and calpains have been identified as potential signaling components o in programmed necrosis.
Now, a team from the Perelman School of Medicine, University of Pennsylvania, in collaboration with the University of California at San Francisco and the Department of Biochemistry and Protein Function Discovery at Queen's University, has developed a unique approach to calpain inhibition by mimicking a natural reaction with a synthesized molecule.
The expression of calcium signaling-related molecules showed significant increase in the frontal cortex of mice exposed to repeated blasts, including calpain 3 (1.
Some recent studies have proposed that calpains cleave proteins and thus modify the function of target proteins (i.
Calpain system comprises three molecules: two calcium dependent proteases, u-calpain and m-calpain, and a third polypeptide, calpastatin, whose function is to inhibit the two calpains (Goll et al.
During ageing, naturally occurring enzymes, calpains and cathepsins (proteases) found in muscle, breakdown specific protein strands in the muscle fibre in a process called proteolysis [18,19].
It is widely accepted that the activity of certain protein degradation enzymes, the calpains and calpastatins, are important determinators of tenderness in meat.