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Journal articles on the topic 'Calpain'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Chhabra, A., H. Fernando, R. E. Mansel, and W. G. Jiang. "Pattern of expression of calpain subunits (large and small) in human breast cancer and the prognostic significance." Journal of Clinical Oncology 25, no. 18_suppl (2007): 21078. http://dx.doi.org/10.1200/jco.2007.25.18_suppl.21078.

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21078 Background: Calpains belongs to family of non-lysosomal calcium dependent cysteine proteases which are known to regulate cellular migration, apoptosis and cell cycle progression in normal and tumour cells. Calpain has also been indicated in the metastatic process of certain tumours like RCC and identified as a potential tumor suppressor for gastric cancer. Little is known about the expression pattern of calpain in human breast cancer. The current study investigated the expression pattern of the large (calpainL) and small (calpainS) subunits of calpain which are encoded by different genes

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2

Upla, Paula, Varpu Marjomäki, Liisa Nissinen, et al. "Calpain 1 and 2 Are Required for RNA Replication of Echovirus 1." Journal of Virology 82, no. 3 (2007): 1581–90. http://dx.doi.org/10.1128/jvi.01375-07.

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ABSTRACT Calpains are calcium-dependent cysteine proteases that degrade cytoskeletal and cytoplasmic proteins. We have studied the role of calpains in the life cycle of human echovirus 1 (EV1). The calpain inhibitors, including calpeptin, calpain inhibitor 1, and calpain inhibitor 2 as well as calpain 1 and calpain 2 short interfering RNAs, completely blocked EV1 infection in the host cells. The effect of the inhibitors was not specific for EV1, because they also inhibited infection by other picornaviruses, namely, human parechovirus 1 and coxsackievirus B3. The importance of the calpains in E

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3

Fontenele, Marcio, Bomyi Lim, Danielle Oliveira та ін. "Calpain A modulates Toll responses by limited Cactus/IκB proteolysis". Molecular Biology of the Cell 24, № 18 (2013): 2966–80. http://dx.doi.org/10.1091/mbc.e13-02-0113.

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Calcium-dependent cysteine proteases of the calpain family are modulatory proteases that cleave their substrates in a limited manner. Among their substrates, calpains target vertebrate and invertebrate IκB proteins. Because proteolysis by calpains potentially generates novel protein functions, it is important to understand how this affects NFκB activity. We investigate the action of Calpain A (CalpA) on the Drosophila melanogaster IκB homologue Cactus in vivo. CalpA alters the absolute amounts of Cactus protein. Our data indicate, however, that CalpA uses additional mechanisms to regulate NFκB

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4

SORIMACHI, Hiroyuki, Shoichi ISHIURA, and Koichi SUZUKI. "Structure and physiological function of calpains." Biochemical Journal 328, no. 3 (1997): 721–32. http://dx.doi.org/10.1042/bj3280721.

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For a long time now, two ubiquitously expressed mammalian calpain isoenzymes have been used to explore the structure and function of calpain. Although these two calpains, μ- and m-calpains, still attract intensive interest because of their unique characteristics, various distinct homologues to the protease domain of μ- and m-calpains have been identified in a variety of organisms. Some of these ‘novel’ calpain homologues are involved in important biological functions. For example, p94 (also called calpain 3), a mammalian calpain homologue predominantly expressed in skeletal muscle, is genetica

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5

Kizhakethil, Reshma V., Ashok K. Varma, Sagar H. Barage та ін. "Repercussions of the Calpain Cleavage-Related Missense Mutations in the Cytosolic Domains of Human Integrin-β Subunits on the Calpain–Integrin Signaling Axis". International Journal of Molecular Sciences 26, № 9 (2025): 4246. https://doi.org/10.3390/ijms26094246.

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Calpains, calcium-dependent cytosolic cysteine proteases, perform controlled proteolysis of their substrates for various cellular and physiological activities. In different cancers, missense mutations accumulate in the genes coding for the calpain cleavage sites in various calpain substrates termed as the calpain cleavage-related mutations (CCRMs). However, the impact of such CCRMs on the calpain–substrate interaction is yet to be explored. This study focuses on the interaction of wild-type and mutant β-integrins with calpain-1 and 2 in uterine corpus endometrial carcinoma (UCEC). A total of 4

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6

Murphy, Robyn M., Rodney J. Snow та Graham D. Lamb. "μ-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans". American Journal of Physiology-Cell Physiology 290, № 1 (2006): C116—C122. http://dx.doi.org/10.1152/ajpcell.00291.2005.

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μ-calpain and calpain-3 are Ca2+-dependent proteases found in skeletal muscle. Autolysis of calpains is observed using Western blot analysis as the cleaving of the full-length proteins to shorter products. Biochemical assays suggest that μ-calpain becomes proteolytically active in the presence of 2–200 μM Ca2+. Although calpain-3 is poorly understood, autolysis is thought to result in its activation, which is widely thought to occur at lower intracellular Ca2+ concentration levels ([Ca2+]i; ∼1 μM) than the levels at which μ-calpain activation occurs. We have demonstrated the Ca2+-dependent aut

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7

Theopold, U., M. Pintér, S. Daffre, et al. "CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells." Molecular and Cellular Biology 15, no. 2 (1995): 824–34. http://dx.doi.org/10.1128/mcb.15.2.824.

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Calpains are calcium-dependent proteases believed to participate in calcium-regulated signal pathways in cells. Ubiquitous calpains as well as tissue-specific calpains have been found in vertebrates. We isolated cDNA clones for a highly tissue-specific calpain gene from Drosophila melanogaster, CalpA, at 56C-D on the second chromosome. The expression of the CalpA gene product was monitored by using a specific antiserum directed against the product expressed by one cDNA clone. The encoded protein is found in a few neurons in the central nervous system, in scattered endocrine cells in the midgut

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8

Covington, Marisa D., David D. Arrington, and Rick G. Schnellmann. "Calpain 10 is required for cell viability and is decreased in the aging kidney." American Journal of Physiology-Renal Physiology 296, no. 3 (2009): F478—F486. http://dx.doi.org/10.1152/ajprenal.90477.2008.

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Aging is associated with abnormalities in kidney function, but the exact mechanisms are unknown. We examined calpains 1, 2, and 10 protein levels in kidneys from rats, mice, and humans of various ages and determined whether calpain 10 is required for cell viability. Calpain 10 protein expression decreased in the kidney, but not in the liver, of aging Fischer 344 rats, and this decrease was attenuated with caloric restriction. There was no change in calpains 1 or 2 levels in the kidney or liver in control and caloric-restricted aging rats. Aging mice also exhibited decreased calpain 10 protein

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9

Arora, A. S., P. de Groen, Y. Emori, and G. J. Gores. "A cascade of degradative hydrolase activity contributes to hepatocyte necrosis during anoxia." American Journal of Physiology-Gastrointestinal and Liver Physiology 270, no. 2 (1996): G238—G245. http://dx.doi.org/10.1152/ajpgi.1996.270.2.g238.

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Calpain proteases contribute to hepatocyte necrosis during anoxia. Our aim was to ascertain the mechanism causing calpain activation during anoxia. In rat hepatocytes, a twofold increase in calpain activity occurred despite the lack of an increase in cytosolic Ca2+ concentration ([Ca2+]i). The increase in calpain activity was not associated with an increase in calpain mRNA or a decrease in calpastatin mRNA expression. Because phospholipid degradation products generated by phospholipases can activate calpains at physiological [Ca2+]i, we determined the effect of phospholipase inhibitors and act

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10

Sultan, Karim R., Bernd T. Dittrich, and Dirk Pette. "Calpain activity in fast, slow, transforming, and regenerating skeletal muscles of rat." American Journal of Physiology-Cell Physiology 279, no. 3 (2000): C639—C647. http://dx.doi.org/10.1152/ajpcell.2000.279.3.c639.

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Fiber-type transitions in adult skeletal muscle induced by chronic low-frequency stimulation (CLFS) encompass coordinated exchanges of myofibrillar protein isoforms. CLFS-induced elevations in cytosolic Ca2+ could activate proteases, especially calpains, the major Ca2+-regulated cytosolic proteases. Calpain activity determined by a fluorogenic substrate in the presence of unaltered endogenous calpastatin activities increased twofold in low-frequency-stimulated extensor digitorum longus (EDL) muscle, reaching a level intermediate between normal fast- and slow-twitch muscles. μ- and m-calpains w

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11

Miyazaki, Takuro. "Calpain and Cardiometabolic Diseases." International Journal of Molecular Sciences 24, no. 23 (2023): 16782. http://dx.doi.org/10.3390/ijms242316782.

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Calpain is defined as a member of the superfamily of cysteine proteases possessing the CysPC motif within the gene. Calpain-1 and -2, which are categorized as conventional isozymes, execute limited proteolysis in a calcium-dependent fashion. Accordingly, the calpain system participates in physiological and pathological phenomena, including cell migration, apoptosis, and synaptic plasticity. Recent investigations have unveiled the contributions of both conventional and unconventional calpains to the pathogenesis of cardiometabolic disorders. In the context of atherosclerosis, overactivation of

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Pánico, Pablo, Marcia Hiriart, Patricia Ostrosky-Wegman, and Ana María Salazar. "TUG is a calpain-10 substrate involved in the translocation of GLUT4 in adipocytes." Journal of Molecular Endocrinology 65, no. 3 (2020): 45–57. http://dx.doi.org/10.1530/jme-19-0253.

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The calpain-10 (CAPN10) protease is implicated in the translocation of the glucose transporter 4 (GLUT4), which is retained in the Golgi matrix via the Tether containing a UBX domain for GLUT4 (TUG) protein. Insulin stimulation induces the proteolytic processing of TUG, which leads to the translocation of GLUT4 to the cell membrane. We tested whether TUG is a CAPN10 substrate. Proteolysis of TUG by calpains was assessed using a cell-free system containing calpain-1 and TUG. In situ proteolysis of TUG by calpains was demonstrated in 3T3-L1 adipocytes in the presence of insulin or calpain inhibi

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13

Mellgren, Ronald L., and Xinhua Huang. "Fetuin A Stabilizes m-Calpain and Facilitates Plasma Membrane Repair." Journal of Biological Chemistry 282, no. 49 (2007): 35868–77. http://dx.doi.org/10.1074/jbc.m706929200.

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Yeast two-hybrid experiments identified α2-Heremans-Schmid glycoprotein (human fetuin A) as a binding partner for calpain domain III (DIII). The tandem DIIIs of calpain-10 interacted under the most selective culture conditions, but DIIIs of m-calpain, calpain-3, and calpain-5 also interacted under less stringent selection. DIIIs of μ-calpain, calpain-6, and the tandem DIII-like domains of the Dictyostelium Cpl protein did not interact with α2-Heremans-Schmid glycoprotein in the yeast two-hybrid system. Bovine fetuin A stabilized proteolytic activity of purified m-calpain incubated in the prese

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14

Weber, Jonasz J., Eva Haas, Yacine Maringer, et al. "Calpain-1 ablation partially rescues disease-associated hallmarks in models of Machado-Joseph disease." Human Molecular Genetics 29, no. 6 (2020): 892–906. http://dx.doi.org/10.1093/hmg/ddaa010.

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Abstract Proteolytic fragmentation of polyglutamine-expanded ataxin-3 is a concomitant and modifier of the molecular pathogenesis of Machado–Joseph disease (MJD), the most common autosomal dominant cerebellar ataxia. Calpains, a group of calcium-dependent cysteine proteases, are important mediators of ataxin-3 cleavage and implicated in multiple neurodegenerative conditions. Pharmacologic and genetic approaches lowering calpain activity showed beneficial effects on molecular and behavioural disease characteristics in MJD model organisms. However, specifically targeting one of the calpain isofo

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Azam, Mohammad, Shaida S. Andrabi, Kenneth E. Sahr, Lakshmi Kamath, Athan Kuliopulos та Athar H. Chishti. "Disruption of the Mouse μ-Calpain Gene Reveals an Essential Role in Platelet Function". Molecular and Cellular Biology 21, № 6 (2001): 2213–20. http://dx.doi.org/10.1128/mcb.21.6.2213-2220.2001.

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ABSTRACT Conventional calpains are ubiquitous calcium-regulated cysteine proteases that have been implicated in cytoskeletal organization, cell proliferation, apoptosis, cell motility, and hemostasis. There are two forms of conventional calpains: the μ-calpain, or calpain I, which requires micromolar calcium for half-maximal activation, and the m-calpain, or calpain II, which functions at millimolar calcium concentrations. We evaluated the functional role of the 80-kDa catalytic subunit of μ-calpain by genetic inactivation using homologous recombination in embryonic stem cells. The μ-calpain-d

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16

Schultz, Bruna, Jéssica Taday, Leonardo Menezes, Anderson Cigerce, Marina C. Leite, and Carlos-Alberto Gonçalves. "Calpain-Mediated Alterations in Astrocytes Before and During Amyloid Chaos in Alzheimer’s Disease." Journal of Alzheimer's Disease 84, no. 4 (2021): 1415–30. http://dx.doi.org/10.3233/jad-215182.

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One of the changes found in the brain in Alzheimer’s disease (AD) is increased calpain, derived from calcium dysregulation, oxidative stress, and/or neuroinflammation, which are all assumed to be basic pillars in neurodegenerative diseases. The role of calpain in synaptic plasticity, neuronal death, and AD has been discussed in some reviews. However, astrocytic calpain changes sometimes appear to be secondary and consequent to neuronal damage in AD. Herein, we explore the possibility of calpain-mediated astroglial reactivity in AD, both preceding and during the amyloid phase. We discuss the ty

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Liu, Xiuli, Juanita J. Rainey, Jay F. Harriman, and Rick G. Schnellmann. "Calpains mediate acute renal cell death: role of autolysis and translocation." American Journal of Physiology-Renal Physiology 281, no. 4 (2001): F728—F738. http://dx.doi.org/10.1152/ajprenal.2001.281.4.f728.

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The goals of this study were to determine 1) the expression of calpain isoforms in rabbit renal proximal tubules (RPT); 2) calpain autolysis and translocation, and calpastatin levels during RPT injury; and 3) the effect of a calpain inhibitor (PD-150606) on calpain levels, mitochondrial function, and ion transport during RPT injury. RT-PCR, immunoblot analysis, and FITC-casein zymography demonstrated the presence of only μ- and m-calpains in rabbit RPT. The mitochondrial inhibitor antimycin A decreased RPT μ- and m-calpain and calpastatin levels in conjunction with cell death and increased pla

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18

Khoutorsky, Arkady, and Micha E. Spira. "Calpain Inhibitors Alter the Excitable Membrane Properties of Cultured Aplysia Neurons." Journal of Neurophysiology 100, no. 5 (2008): 2784–93. http://dx.doi.org/10.1152/jn.90487.2008.

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The calpain superfamily of calcium-dependent papain-like cysteine proteases constitutes highly conserved proteases that function to posttranslationally modify substrates by partial proteolysis. Calpains are known to proteolyze >100 substrates that lack strong sequence homology. Consequently, the calpain superfamily has been implicated in playing a central role in diverse physiological and pathological processes. Investigation of the physiological functions of calpains, on the one hand, and the need to develop pharmacological reagents to inhibit calpain-mediated pathological processes, on th

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Ilian, M. A., and N. E. Forsberg. "Gene expression of calpains and their specific endogenous inhibitor, calpastatin, in skeletal muscle of fed and fasted rabbits." Biochemical Journal 287, no. 1 (1992): 163–71. http://dx.doi.org/10.1042/bj2870163.

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To investigate the role of calpains in myofibrillar protein degradation in skeletal muscle and the regulation of their activity in vivo, we studied the effects of fasting on gene expression of calpains and calpastatin in the skeletal muscle of rabbits. In response to fasting, myofibrillar protein degradation increased 2-fold and mRNA levels of calpain I, calpain II and calpastatin were also increased. However, calpain and calpastatin activities remained unchanged. To investigate this discrepancy, we analysed polysomal calpain mRNA. Results indicated that fasting caused a 2-fold increase in the

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Ben-Aharon, Irit, Paula R. Brown, Nir Etkovitz, Edward M. Eddy, and Ruth Shalgi. "The expression of calpain 1 and calpain 2 in spermatogenic cells and spermatozoa of the mouse." Reproduction 129, no. 4 (2005): 435–42. http://dx.doi.org/10.1530/rep.1.00255.

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There is some evidence suggesting that Ca2+is involved in processes that occur during the development and function of spermatozoa. Calcium-dependent proteins, such as calmodulin, are expressed during mammalian spermatogenesis further suggesting that Ca2+takes part in its regulation. However, the precise roles of Ca2+in spermatogenesis remain to be elucidated. Calpains are a family of Ca2+-dependent cysteine proteases whose members are expressed ubiquitously or in a tissue-specific manner. Calpain has been demonstrated to mediate specific Ca2+-dependent processes including cell fusion, mitosis

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Nina S. Pestereva, Irina S. Ivleva, Irina M. Kotova, Dmitriy S. Traktirov, and Marina N. Karpenko. "Region-specific changes in expression and activity of calpains in the CNS of native rats." Biomedicine 42, no. 4 (2022): 771–74. http://dx.doi.org/10.51248/.v42i4.1653.

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Introduction and Aim: It has been proposed that µ-calpain is responsible for neuronal survival, while m-calpain – for the degeneration. It can be assumed that the "susceptibility" to the damage factor for neurons in different CNS regions depends on the content/activity of calpain isoforms. We analyzed the mRNA levels and the activity of µ-and m-calpain in the different CNS structures of rats. Materials and Methods: After decapitation intact male Wistar rats the prefrontal cortex, striatum, hippocampus, midbrain, brainstem, cerebellum, and spinal cord were removed. Each structure was divided in

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Seremwe, Mutsa, Rick G. Schnellmann, and Wendy B. Bollag. "Calpain-10 Activity Underlies Angiotensin II-Induced Aldosterone Production in an Adrenal Glomerulosa Cell Model." Endocrinology 156, no. 6 (2015): 2138–49. http://dx.doi.org/10.1210/en.2014-1866.

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Abstract Aldosterone is a steroid hormone important in the regulation of blood pressure. Aberrant production of aldosterone results in the development and progression of diseases including hypertension and congestive heart failure; therefore, a complete understanding of aldosterone production is important for developing more effective treatments. Angiotensin II (AngII) regulates steroidogenesis, in part through its ability to increase intracellular calcium levels. Calcium can activate calpains, proteases classified as typical or atypical based on the presence or absence of penta-EF-hands, whic

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Zhang, Mengxiao, Grace Wang, and Tianqing Peng. "Calpain-Mediated Mitochondrial Damage: An Emerging Mechanism Contributing to Cardiac Disease." Cells 10, no. 8 (2021): 2024. http://dx.doi.org/10.3390/cells10082024.

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Calpains belong to the family of calcium-dependent cysteine proteases expressed ubiquitously in mammals and many other organisms. Activation of calpain is observed in diseased hearts and is implicated in cardiac cell death, hypertrophy, fibrosis, and inflammation. However, the underlying mechanisms remain incompletely understood. Recent studies have revealed that calpains target and impair mitochondria in cardiac disease. The objective of this review is to discuss the role of calpains in mediating mitochondrial damage and the underlying mechanisms, and to evaluate whether targeted inhibition o

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ELCE, John S., Peter L. DAVIES, Carol HEGADORN, Donald H. MAURICE, and J. Simon C. ARTHUR. "The effects of truncations of the small subunit on m-calpain activity and heterodimer formation." Biochemical Journal 326, no. 1 (1997): 31–38. http://dx.doi.org/10.1042/bj3260031.

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In order to study subunit interactions in calpain, the effects of small subunit truncations on m-calpain activity and heterodimer formation have been measured. It has been shown previously that active calpain is formed by co-expression of the large subunit (80 kDa) of rat m-calpain with a δ86 form (21 kDa) of the small subunit. cDNA for the full-length 270 amino acid (28.5 kDa) rat calpain small subunit has now been cloned, both with and without an N-terminal histidine tag (NHis10). The full-length small subunit constructs yielded active calpains on co-expression with the large subunit, and th

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Piper, Ann-Katrin, Reece A. Sophocleous, Samuel E. Ross, et al. "Loss of calpains-1 and -2 prevents repair of plasma membrane scrape injuries, but not small pores, and induces a severe muscular dystrophy." American Journal of Physiology-Cell Physiology 318, no. 6 (2020): C1226—C1237. http://dx.doi.org/10.1152/ajpcell.00408.2019.

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The ubiquitous calpains, calpain-1 and -2, play important roles in Ca2+-dependent membrane repair. Mechanically active tissues like skeletal muscle are particularly reliant on mechanisms to repair and remodel membrane injury, such as those caused by eccentric damage. We demonstrate that calpain-1 and -2 are master effectors of Ca2+-dependent repair of mechanical plasma membrane scrape injuries, although they are dispensable for repair/removal of small wounds caused by pore-forming agents. Using CRISPR gene-edited human embryonic kidney 293 (HEK293) cell lines, we established that loss of both

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Blanc, Fany, Laetitia Furio, Dorothée Moisy, et al. "Targeting host calpain proteases decreases influenza A virus infection." American Journal of Physiology-Lung Cellular and Molecular Physiology 310, no. 7 (2016): L689—L699. http://dx.doi.org/10.1152/ajplung.00314.2015.

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Influenza A viruses (IAV) trigger contagious acute respiratory diseases. A better understanding of the molecular mechanisms of IAV pathogenesis and host immune responses is required for the development of more efficient treatments of severe influenza. Calpains are intracellular proteases that participate in diverse cellular responses, including inflammation. Here, we used in vitro and in vivo approaches to investigate the role of calpain signaling in IAV pathogenesis. Calpain expression and activity were found altered in IAV-infected bronchial epithelial cells. With the use of small-interferin

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Kuchay, Shafi, Rafael Nunez, Amelia M. Bartholomew, and Athar H. Chishti. "Calpain I Null Mice Display Lymphoid Hyperplasia." Blood 104, no. 11 (2004): 1268. http://dx.doi.org/10.1182/blood.v104.11.1268.1268.

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Abstract Calpains are ubiquitous calcium-regulated cysteine proteases that have been implicated in cytoskeletal organization, homeostasis, cell proliferation, cell motility, and apoptosis. The conventional calpains include mu-calpain (calpain I) that requires micromolar calcium for half maximal activation and m-calpain (calpain II) that functions at millimolar calcium concentration in vitro. To evaluate the physiological function(s) of mu-calpain, we utilized genetically altered mu-calpain null mice as the model system. Spleen biopsy of mu-calpain null adult mice showed consistent expansion of

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Bevers, Matthew B., and Robert W. Neumar. "Mechanistic Role of Calpains in Postischemic Neurodegeneration." Journal of Cerebral Blood Flow & Metabolism 28, no. 4 (2007): 655–73. http://dx.doi.org/10.1038/sj.jcbfm.9600595.

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The calpain family of proteases is causally linked to postischemic neurodegeneration. However, the precise mechanisms by which calpains contribute to postischemic neuronal death have not been fully elucidated. This review outlines the key features of the calpain system, and the evidence for its causal role in postischemic neuronal pathology. Furthermore, the consequences of specific calpain substrate cleavage at various subcellular locations are explored. Calpain substrates within synapses, plasma membrane, endoplasmic reticulum, lysosomes, mitochondria, and the nucleus, as well as the overall

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Ou, B. R., and N. E. Forsberg. "Determination of skeletal muscle calpain and calpastatin activities during maturation." American Journal of Physiology-Endocrinology and Metabolism 261, no. 6 (1991): E677—E683. http://dx.doi.org/10.1152/ajpendo.1991.261.6.e677.

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Our objectives were to characterize events underlying changes in skeletal muscle calpain and calpastatin activities, using maturation as a model. Muscle samples were taken from rabbits of four ages (newborn and 1, 2, and 5 mo old). Concentrations of RNA and protein and activities of calpains I and II and calpastatin were determined. Steady-state concentrations of mRNAs encoding calpain I, calpain II, calpastatin, alpha- and beta-tubulin, and beta-actin were determined using Northern blot analysis. Calpain and calpastatin activities declined markedly between birth and 1 mo of age and remained u

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Sorimachi, Hiroyuki, Hiroshi Mamitsuka, and Yasuko Ono. "Understanding the substrate specificity of conventional calpains." Biological Chemistry 393, no. 9 (2012): 853–71. http://dx.doi.org/10.1515/hsz-2012-0143.

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Abstract: Calpains are intracellular Ca2+-dependent Cys proteases that play important roles in a wide range of biological phenomena via the limited proteolysis of their substrates. Genetic defects in calpain genes cause lethality and/or functional deficits in many organisms, including humans. Despite their biological importance, the mechanisms underlying the action of calpains, particularly of their substrate specificities, remain largely unknown. Studies show that certain sequence preferences influence calpain substrate recognition, and some properties of amino acids have been related success

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McCartney, Christian-Scott E., Qilu Ye, Robert L. Campbell, and Peter L. Davies. "Insertion sequence 1 from calpain-3 is functional in calpain-2 as an internal propeptide." Journal of Biological Chemistry 293, no. 46 (2018): 17716–30. http://dx.doi.org/10.1074/jbc.ra118.004803.

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Calpains are intracellular, calcium-activated cysteine proteases. Calpain-3 is abundant in skeletal muscle, where its mutation-induced loss of function causes limb-girdle muscular dystrophy type 2A. Unlike the small subunit–containing calpain-1 and -2, the calpain-3 isoform homodimerizes through pairing of its C-terminal penta-EF-hand domain. It also has two unique insertion sequences (ISs) not found in the other calpains: IS1 within calpain-3's protease core and IS2 just prior to the penta-EF-hand domain. Production of either native or recombinant full-length calpain-3 to characterize the fun

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Baudry, Michel. "Calpain-1 and Calpain-2 in the Brain: Dr. Jekill and Mr Hyde?" Current Neuropharmacology 17, no. 9 (2019): 823–29. http://dx.doi.org/10.2174/1570159x17666190228112451.

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While the calpain system has now been discovered for over 50 years, there is still a paucity of information regarding the organization and functions of the signaling pathways regulated by these proteases, although calpains play critical roles in many cell functions. Moreover, calpain overactivation has been shown to be involved in numerous diseases. Among the 15 calpain isoforms identified, calpain-1 (aka &#181;-calpain) and calpain-2 (aka m-calpain) are ubiquitously distributed in most tissues and organs, including the brain. We have recently proposed that calpain-1 and calpain- 2 play op

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Moraczewski, J., E. Piekarska, M. Zimowska, and M. Sobolewska. "Activity of mu- and m-calpain in regenerating fast and slow twitch skeletal muscles." Acta Biochimica Polonica 43, no. 4 (1996): 693–700. http://dx.doi.org/10.18388/abp.1996_4466.

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Calpains--non-lysosomal intracellular calcium-activated neutral proteinases, form a family consisting of several distinct members. Two of the isoenzymes: mu (calpain I) and m (calpain II) responded differently to the injury during complete regeneration of Extensor digitorum longus (EDL) muscle and partial regeneration of Soleus muscle. In the crushed EDL the level of m-calpain on the 3rd and 7th day of regeneration was higher than in non-operated muscles, whereas the activity of this calpain in injured Soleus decreased. The level of mu-calpain in EDL oscillated irregularly during regeneration

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Kashiwagi, Aki, Ernestina Schipani, Mikaela J. Fein, Peter A. Greer, and Masako Shimada. "Targeted Deletion of Capn4 in Cells of the Chondrocyte Lineage Impairs Chondrocyte Proliferation and Differentiation." Molecular and Cellular Biology 30, no. 11 (2010): 2799–810. http://dx.doi.org/10.1128/mcb.00157-10.

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ABSTRACT Calpains are calcium-dependent intracellular cysteine proteases, which include ubiquitously expressed μ- and m-calpains. Both calpains are heterodimers consisting of a large catalytic subunit and a small regulatory subunit. The calpain small subunit encoded by the gene Capn4 directly binds to the intracellular C-terminal tail of the receptor for the parathyroid hormone (PTH) and PTH-related peptide and modulates cellular functions in cells of the osteoblast lineage in vitro and in vivo. To investigate a physiological role of the calpain small subunit in cells of the chondrocyte lineag

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Moshal, Karni S., Mahavir Singh, Utpal Sen, et al. "Homocysteine-mediated activation and mitochondrial translocation of calpain regulates MMP-9 in MVEC." American Journal of Physiology-Heart and Circulatory Physiology 291, no. 6 (2006): H2825—H2835. http://dx.doi.org/10.1152/ajpheart.00377.2006.

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Hyperhomocysteinemia (HHcy) is associated with atherosclerosis, stroke, and dementia. Hcy causes extracellular matrix remodeling by the activation of matrix metalloproteinase-9 (MMP-9), in part, by inducing redox signaling and modulating the intracellular calcium dynamics. Calpains are the calcium-dependent cysteine proteases that are implicated in mitochondrial damage via oxidative burst. Mitochondrial abnormalities have been identified in HHcy. The mechanism of Hcy-induced extracellular matrix remodeling by MMP-9 activation via mitochondrial pathway is largely unknown. We report a novel role

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Wang, Yubin, Yan Liu, Xiaoning Bi, and Michel Baudry. "Calpain-1 and Calpain-2 in the Brain: New Evidence for a Critical Role of Calpain-2 in Neuronal Death." Cells 9, no. 12 (2020): 2698. http://dx.doi.org/10.3390/cells9122698.

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Calpains are a family of soluble calcium-dependent proteases that are involved in multiple regulatory pathways. Our laboratory has focused on the understanding of the functions of two ubiquitous calpain isoforms, calpain-1 and calpain-2, in the brain. Results obtained over the last 30 years led to the remarkable conclusion that these two calpain isoforms exhibit opposite functions in the brain. Calpain-1 activation is required for certain forms of synaptic plasticity and corresponding types of learning and memory, while calpain-2 activation limits the extent of plasticity and learning. Calpain

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Ben-Aharon, Irit, Karin Haim, Ruth Shalgi, and Dalit Ben-Yosef. "Expression and possible involvement of calpain isoforms in mammalian egg activation." Reproduction 130, no. 2 (2005): 165–75. http://dx.doi.org/10.1530/rep.1.00602.

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At fertilization in mammals, the spermatozoon triggers a unique signal transduction mechanism within the egg, leading to its activation. It is well accepted that the earliest event observed in all activated eggs is an abrupt rise in intracellular calcium concentrations. However, little is known regarding the downstream proteins that are activated by this rise in calcium. Calpains constitute a family of intracellular calcium-dependent cysteine proteases whose members are expressed widely in a variety of cells. We investigated the expression and possible role of the calpain isoforms μ and m thro

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Gafni, Juliette, Evan Hermel, Jessica E. Young, Cheryl L. Wellington, Michael R. Hayden, and Lisa M. Ellerby. "Inhibition of Calpain Cleavage of Huntingtin Reduces Toxicity." Journal of Biological Chemistry 279, no. 19 (2004): 20211–20. http://dx.doi.org/10.1074/jbc.m401267200.

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Huntington's disease (HD) is a neurodegenerative disorder caused by a polyglutamine (polyQ) tract expansion near the N terminus of huntingtin (Htt). Proteolytic processing of mutant Htt and abnormal calcium signaling may play a critical role in disease progression and pathogenesis. Recent work indicates that calpains may participate in the increased and/or altered patterns of Htt proteolysis leading to the selective toxicity observed in HD striatum. Here, we identify two calpain cleavage sites in Htt and show that mutation of these sites renders the polyQ expanded Htt less susceptible to prote

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Arrington, David D., Terry R. Van Vleet, and Rick G. Schnellmann. "Calpain 10: a mitochondrial calpain and its role in calcium-induced mitochondrial dysfunction." American Journal of Physiology-Cell Physiology 291, no. 6 (2006): C1159—C1171. http://dx.doi.org/10.1152/ajpcell.00207.2006.

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Calpains, Ca2+-activated cysteine proteases, are cytosolic enzymes implicated in numerous cellular functions and pathologies. We identified a mitochondrial Ca2+-inducible protease that hydrolyzed a calpain substrate (SLLVY-AMC) and was inhibited by active site-directed calpain inhibitors as calpain 10, an atypical calpain lacking domain IV. Immunoblot analysis and activity assays revealed calpain 10 in the mitochondrial outer membrane, intermembrane space, inner membrane, and matrix fractions. Mitochondrial staining was observed when COOH-terminal green fluorescent protein-tagged calpain 10 wa

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Ennes-Vidal, Vítor, Marta Helena Branquinha, André Luis Souza dos Santos, and Claudia Masini d’Avila-Levy. "The Diverse Calpain Family in Trypanosomatidae: Functional Proteins Devoid of Proteolytic Activity?" Cells 10, no. 2 (2021): 299. http://dx.doi.org/10.3390/cells10020299.

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Calpains are calcium-dependent cysteine peptidases that were originally described in mammals and, thereafter, their homologues were identified in almost all known living organisms. The deregulated activity of these peptidases is associated with several pathologies and, consequently, huge efforts have been made to identify selective inhibitors. Trypanosomatids, responsible for life-threatening human diseases, possess a large and diverse family of calpain sequences in their genomes. Considering that the current therapy to treat trypanosomatid diseases is limited to a handful of drugs that suffer

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Rose, Aaron, Huang Zhi, Fukun Hoffmann, Robert Norton, and Peter Hoffamann. "Selenoprotein K is a novel target of m-calpain, and cleavage is regulated by toll-like receptor-induced calpastatin in macrophages (54.22)." Journal of Immunology 188, no. 1_Supplement (2012): 54.22. http://dx.doi.org/10.4049/jimmunol.188.supp.54.22.

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Abstract Calpains are calcium (Ca2+)-activated cysteine proteases that modulate cellular function through cleavage of a variety of intra-cellular targets. Two major isoforms of calpain, u- and m-calpain, are expressed in different tissues and cell-types. Selenoprotein K (SelK) is a selenocysteine containing transmembrane ER protein involved in Ca2+ flux, and western blot analyses revealed one SelK band in mouse lymphocytes (both B and T cells) and two bands for SelK in mouse myeloid cells (macrophages, dendritic cells, and neutrophils). This led us to investigate cleavage of SelK and we found

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Nakagawa, Toshiyuki, and Junying Yuan. "Cross-Talk between Two Cysteine Protease Families." Journal of Cell Biology 150, no. 4 (2000): 887–94. http://dx.doi.org/10.1083/jcb.150.4.887.

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Calpains and caspases are two cysteine protease families that play important roles in regulating pathological cell death. Here, we report that m-calpain may be responsible for cleaving procaspase-12, a caspase localized in the ER, to generate active caspase-12. In addition, calpain may be responsible for cleaving the loop region in Bcl-xL and, therefore, turning an antiapoptotic molecule into a proapoptotic molecule. We propose that disturbance to intracellular calcium storage as a result of ischemic injury or amyloid β peptide cytotoxicity may induce apoptosis through calpain- mediated caspas

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Kalbe, L., A. Leunda, T. Sparre, et al. "Nutritional regulation of proteases involved in fetal rat insulin secretion and islet cell proliferation." British Journal of Nutrition 93, no. 3 (2005): 309–16. http://dx.doi.org/10.1079/bjn20041313.

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Epidemiological studies have indicated that malnutrition during early life may programme chronic degenerative disease in adulthood. In an animal model of fetal malnutrition, rats received an isoenergetic, low-protein (LP) diet during gestation. This reduced fetal β-cell proliferation and insulin secretion. Supplementation during gestation with taurine prevented these alterations. Since proteases are involved in secretion and proliferation, we investigated which proteases were associated with these alterations and their restoration in fetal LP islets. Insulin secretion and proliferation of feta

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Potter, David A., Jennifer S. Tirnauer, Richard Janssen, et al. "Calpain Regulates Actin Remodeling during Cell Spreading." Journal of Cell Biology 141, no. 3 (1998): 647–62. http://dx.doi.org/10.1083/jcb.141.3.647.

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Previous studies suggest that the Ca2+-dependent proteases, calpains, participate in remodeling of the actin cytoskeleton during wound healing and are active during cell migration. To directly test the role that calpains play in cell spreading, several NIH-3T3– derived clonal cell lines were isolated that overexpress the biological inhibitor of calpains, calpastatin. These cells stably overexpress calpastatin two- to eightfold relative to controls and differ from both parental and control cell lines in morphology, spreading, cytoskeletal structure, and biochemical characteristics. Morphologic

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Belhadj, Soumaya, Nina Sofia Hermann, Yu Zhu, Gustav Christensen, Torsten Strasser, and François Paquet-Durand. "Visualizing Cell Death in Live Retina: Using Calpain Activity Detection as a Biomarker for Retinal Degeneration." International Journal of Molecular Sciences 23, no. 7 (2022): 3892. http://dx.doi.org/10.3390/ijms23073892.

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Calpains are a family of calcium-activated proteases involved in numerous disorders. Notably, previous studies have shown that calpain activity was substantially increased in various models for inherited retinal degeneration (RD). In the present study, we tested the capacity of the calpain-specific substrate t-BOC-Leu-Met-CMAC to detect calpain activity in living retina, in organotypic retinal explant cultures derived from wild-type mice, as well as from rd1 and RhoP23H/+ RD-mutant mice. Test conditions were refined until the calpain substrate readily detected large numbers of cells in the pho

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Belhadj, Soumaya, Nina Sofia Hermann, Yu Zhu, Gustav Christensen, Torsten Strasser, and François Paquet-Durand. "Visualizing Cell Death in Live Retina: Using Calpain Activity Detection as a Biomarker for Retinal Degeneration." International Journal of Molecular Sciences (Int. J. Mol. Sci.) 23, no. 7 (2022): 3892. https://doi.org/10.3390/ijms23073892.

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Calpains are a family of calcium-activated proteases involved in numerous disorders. Notably, previous studies have shown that calpain activity was substantially increased in various models for inherited retinal degeneration (RD). In the present study, we tested the capacity of the calpain-specific substrate t-BOC-Leu-Met-CMAC to detect calpain activity in living retina, in organotypic retinal explant cultures derived from wild-type mice, as well as from rd1 and RhoP23H/+ RD-mutant mice. Test conditions were refined until the calpain substrate readily detected large numbers of cells in the pho

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GOLL, DARREL E., VALERY F. THOMPSON, HONGQI LI, WEI WEI, and JINYANG CONG. "The Calpain System." Physiological Reviews 83, no. 3 (2003): 731–801. http://dx.doi.org/10.1152/physrev.00029.2002.

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Goll, Darrel E., Valery F. Thompson, Hongqi Li, Wei Wei, and Jinyang Cong. The Calpain System. Physiol Rev 83: 731–801, 2003; 10.1152/physrev.00029.2002.—The calpain system originally comprised three molecules: two Ca2+-dependent proteases, μ-calpain and m-calpain, and a third polypeptide, calpastatin, whose only known function is to inhibit the two calpains. Both μ- and m-calpain are heterodimers containing an identical 28-kDa subunit and an 80-kDa subunit that shares 55–65% sequence homology between the two proteases. The crystallographic structure of m-calpain reveals six “domains” in the 8

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Wang, Lijing, Ligong Duan, Xukun Li, and Guoping Li. "Acute-Exercise-Induced Alterations in Calpain and Calpastatin Expression in Rat Muscle." Journal of Sport Rehabilitation 18, no. 2 (2009): 213–28. http://dx.doi.org/10.1123/jsr.18.2.213.

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Context:Calpains and calpastatin can degrade muscle proteins, but no research has investigated the expression pattern of calpains and calpastatin after exhaustive exercise.Objective:To investigate the alterations in expression of μ-, m-, and n-calpain and calpastatin after exhaustive exercise and its association with muscle injury.Method:64 rats divided into 2 groups, a nonexercise control group and an acute-exhaustive-exercise (AEE) group. Biopsies in the AEE group were taken at different times after exercise.Results:Calpastatin protein expression and m-calpain activity increased early after

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Lee, Wing-Kee, Blazej Torchalski, and Frank Thévenod. "Cadmium-induced ceramide formation triggers calpain-dependent apoptosis in cultured kidney proximal tubule cells." American Journal of Physiology-Cell Physiology 293, no. 3 (2007): C839—C847. http://dx.doi.org/10.1152/ajpcell.00197.2007.

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A major target of cadmium (Cd2+) toxicity is the kidney proximal tubule (PT) cell. Cd2+-induced apoptosis of PT cells is mediated by sequential activation of calpains at 3–6 h and caspases-9 and -3 after 24-h exposure. Calpains also partly contribute to caspase activation, which emphasizes the importance of calpains for PT apoptosis by Cd2+. Upstream processes underlying Cd2+-induced calpain activation remain unclear. We describe for the first time that 10–50 μM Cd2+ causes a significant increase in ceramide formation by ∼22% (3 h) and ∼72% (24 h), as measured by diacylglycerol kinase assay. I

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Macqueen, Daniel J., and Alexander H. Wilcox. "Characterization of the definitive classical calpain family of vertebrates using phylogenetic, evolutionary and expression analyses." Open Biology 4, no. 4 (2014): 130219. http://dx.doi.org/10.1098/rsob.130219.

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The calpains are a superfamily of proteases with extensive relevance to human health and welfare. Vast research attention is given to the vertebrate ‘classical’ subfamily, making it surprising that the evolutionary origins, distribution and relationships of these genes is poorly characterized. Consequently, there exists uncertainty about the conservation of gene family structure, function and expression that has been principally defined from work with mammals. Here, more than 200 vertebrate classical calpains were incorporated in phylogenetic analyses spanning an unprecedented range of taxa, i

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