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A proteolytic enzyme regulated by the concentration of calcium ions.

[Probably cal(cium) + p(rote)a(se) + -in.]
American Heritage® Dictionary of the English Language, Fifth Edition. Copyright © 2016 by Houghton Mifflin Harcourt Publishing Company. Published by Houghton Mifflin Harcourt Publishing Company. All rights reserved.


any of various enzymes in mammals and other organisms that are involved in the proteolysis of endogenous proteins and are regulated by the concentration of calcium ions
[C20: from cal(modulin) + (pa)pain]
Collins English Dictionary – Complete and Unabridged, 12th Edition 2014 © HarperCollins Publishers 1991, 1994, 1998, 2000, 2003, 2006, 2007, 2009, 2011, 2014
References in periodicals archive ?
Immunohistochemical findings show that SE leads to caspase-3 and calpain 1-mediated neuronal damage, that SE-mediated cell damage increases with increasing age and that caspase-dependent apoptotic morphology is more evident in immature rats and calpain-1 mediated cell necrosis in mature groups.
Calpain, also known as calcium-dependent protease system, is an effective molecule reacting to an intracellular calcium signal, calpain-1, which has been shown to selectively cleave some apoptotic proteins (e.g.
In cell culture experiments with cardiomyocytes, it was shown that cTnT is cleaved between the R68/S69 amino acid residues, and it was suggested that the cytosolic enzyme [mu]-calpain (calpain-1) is responsible for this degradation (11, 12).
Targeted gene inactivation of calpain-1 suppresses cortical degeneration due to traumatic brain injury and neuronal apoptosis induced by oxidative stress.
Weaver, "Calpain-1 activity in bovine muscle is primarily influenced by temperature, not pH decline" Journal of Animal Science, vol.
[81] very elegantly showed that [alpha] subunit is a target for calpain-1 in diabetic hearts, leading to its proteolytic degradation, reduction in ATP synthase activity, increase in mitochondrial superoxide formation, and diabetic cardiomyopathy in mice.
falciparum parasites, the research team infected human red blood cells, using pharmacological and biochemical evidence to discover that parasites activate the host protease calpain-1.
Interaction between calpain-1 and HSP90: New insights into the regulation of localization and activity of the protease.
Monticone et al., "Calpain-1 regulation of matrix metalloproteinase 2 activity in vascular smooth muscle cells facilitates age-associated aortic wall calcification and fibrosis," Hypertension, vol.
Powers, "Calpain-1 is required for hydrogen peroxide-induced myotube atrophy," American Journal of Physiology--Cell Physiology, vol.
Western blot analysis was performed using 50 [micro]g samples of protein to evaluate calpain-1 expression.