{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T05:49:17Z","timestamp":1778564957223,"version":"3.51.4"},"reference-count":37,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2010,10,1]],"date-time":"2010-10-01T00:00:00Z","timestamp":1285891200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2010,10,1]],"date-time":"2010-10-01T00:00:00Z","timestamp":1285891200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["NS-31622"],"award-info":[{"award-number":["NS-31622"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["NS-41088"],"award-info":[{"award-number":["NS-41088"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["NS-57811"],"award-info":[{"award-number":["NS-57811"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["NS-38146"],"award-info":[{"award-number":["NS-38146"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Experimental Neurology"],"published-print":{"date-parts":[[2010,10]]},"DOI":"10.1016\/j.expneurol.2010.07.021","type":"journal-article","created":{"date-parts":[[2010,7,30]],"date-time":"2010-07-30T04:19:41Z","timestamp":1280463581000},"page":"430-435","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":23,"title":["Calpain inhibition attenuates intracellular changes in muscle cells in response to extracellular inflammatory stimulation"],"prefix":"10.1016","volume":"225","author":[{"given":"Kenkichi","family":"Nozaki","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Arabinda","family":"Das","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Swapan K.","family":"Ray","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Naren L.","family":"Banik","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.expneurol.2010.07.021_bb0005","doi-asserted-by":"crossref","first-page":"S39","DOI":"10.1212\/01.wnl.0000192128.13875.1e","article-title":"Inclusion-body myositis: a myodegenerative conformational disorder associated with A\u03b2, protein misfolding, and proteasome inhibition","volume":"66","author":"Askanas","year":"2006","journal-title":"Neurology"},{"key":"10.1016\/j.expneurol.2010.07.021_bb0010","doi-asserted-by":"crossref","first-page":"1558","DOI":"10.1016\/j.bbrc.2006.05.059","article-title":"TNF-\u03b1-mediated cardiomyocyte apoptosis involves caspase-12 and calpain","volume":"345","author":"Bajaj","year":"2006","journal-title":"Biochem. Biophy. Res. Commun."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0015","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1002\/jnr.490310414","article-title":"Calcium-activated neutral proteinase (calpain) activity in C6 cell line: compartmentation of mu and m calpain","volume":"31","author":"Banik","year":"1992","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0020","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1038\/jcbfm.1994.67","article-title":"Postischemic administration of AK275, a calpain inhibitor, provides substantial protection against focal ischemic brain damage","volume":"14","author":"Bartus","year":"1994","journal-title":"J. Cereb. Blood Flow Metab."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0025","doi-asserted-by":"crossref","first-page":"10191","DOI":"10.1074\/jbc.M007807200","article-title":"Synergistic activation of caspase 3 by m-calpain after neonatal hypoxia-ischemia: a mechanism of \u201cpathological apoptosis\u201d?","volume":"276","author":"Blomgren","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0030","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1093\/brain\/120.1.39","article-title":"Polymyositis with cytochrome oxidase negative muscle fibres Early quadriceps weakness and poor response to immunosuppressive therapy","volume":"120","author":"Blume","year":"1997","journal-title":"Brain"},{"key":"10.1016\/j.expneurol.2010.07.021_bb0035","first-page":"195","article-title":"Regulation of the calcium-activated neutral proteinase (CANP) of bovine brain by myelin lipids","volume":"11038","author":"Chakrabarti","year":"1990","journal-title":"Biochem. Biophys. Acta"},{"key":"10.1016\/j.expneurol.2010.07.021_bb0040","doi-asserted-by":"crossref","first-page":"1816","DOI":"10.1111\/j.1471-4159.1990.tb01241.x","article-title":"Ganglioside-modulated proteolysis by Ca2+- activated neutral proteinase (CANP): a role of glycoconjugates in CANP regulations","volume":"54","author":"Chakrabarti","year":"1990","journal-title":"J. Neurochem."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0045","doi-asserted-by":"crossref","first-page":"11627","DOI":"10.1016\/S0021-9258(20)71248-2","article-title":"Effect of L-\u03b1-phsphatidylinositol on a vascular smooth muscle Ca2+ dependent protease. Reduction of the Ca2+, requirement for autolysis","volume":"259","author":"Coolican","year":"1984","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0050","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1038\/ncprheum0140","article-title":"Mechanism of disease: signaling pathways and immunology of inflammatory myopathies","volume":"2","author":"Dalakas","year":"2006","journal-title":"Nat. Clin. Pract. Rheumatol."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0055","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1093\/jnen\/60.9.847","article-title":"Cathepsins are upregulated by IFN-\u03b3\/STAT1 in human muscle culture: a possible active factor in dermatomyositis","volume":"60","author":"Gallardo","year":"2001","journal-title":"J. Neuropath. Exp. Neurol."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0060","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1002\/1097-4644(20010101)80:1<53::AID-JCB60>3.0.CO;2-E","article-title":"N-terminal cleavage of bax by calpain generates a potent proapoptotic 18-kDa fragment that promotes bcl-2-independent cytochrome c release and apoptotic cell death","volume":"80","author":"Gao","year":"2000","journal-title":"J. Cell. Biochem."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0065","doi-asserted-by":"crossref","first-page":"2008","DOI":"10.1212\/01.WNL.0000291619.17160.b8","article-title":"Proposed immunologic models of the inflammatory myopathies and potential therapeutic implications","volume":"69","author":"Greenberg","year":"2007","journal-title":"Neurology"},{"key":"10.1016\/j.expneurol.2010.07.021_bb0070","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1002\/jnr.20470","article-title":"Upregulation of calpain correlates with increased neurodegeneration in acute experimental auto-immune encephalomyelitis","volume":"81","author":"Guyton","year":"2005","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0075","doi-asserted-by":"crossref","first-page":"2398","DOI":"10.1002\/jnr.22408","article-title":"Calpeptin attenuated inflammation, cell death, and axonal damage in animal model of multiple sclerosis","volume":"88","author":"Guyton","year":"2010","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0080","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1038\/348334a0","article-title":"Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death","volume":"348","author":"Hockenbery","year":"1990","journal-title":"Nature"},{"key":"10.1016\/j.expneurol.2010.07.021_bb0085","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1159\/000117430","article-title":"Calpain and cathepsins in the skeletal muscle of inflammatory myopathies","volume":"37","author":"Kumamoto","year":"1997","journal-title":"Eur. Neurol."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0090","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"10.1016\/j.expneurol.2010.07.021_bb0095","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1016\/S0092-8674(00)80434-1","article-title":"Cytochrome c and dATP-dependent formation of Apaf-1\/caspase-9 complex initiates an apoptotic protease cascade","volume":"91","author":"Li","year":"1997","journal-title":"Cell"},{"key":"10.1016\/j.expneurol.2010.07.021_bb0100","first-page":"149","article-title":"Calcium-dependent proteinases and specific inhibitors: calpain and calpastatin","volume":"49","author":"Murachi","year":"1984","journal-title":"Biochem. Soc. Symp."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0105","doi-asserted-by":"crossref","first-page":"1824","DOI":"10.1002\/art.21103","article-title":"Activation of the endoplasmic reticulum stress response in autoimmune myositis. Potential role in muscle fiber damage and dysfunction","volume":"52","author":"Nagaraju","year":"2005","journal-title":"Arthritis Rheum."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0110","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1083\/jcb.150.4.887","article-title":"Cross-talk between tow cystein protease families. Activation of caspase-12 by calpain in apoptosis. J","volume":"150","author":"Nakagawa","year":"2000","journal-title":"Cell Biol."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0115","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1038\/47513","article-title":"Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-\u03b2","volume":"403","author":"Nakagawa","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.expneurol.2010.07.021_bb0120","doi-asserted-by":"crossref","first-page":"S49","DOI":"10.1212\/01.wnl.0000192127.63013.8d","article-title":"Mitochondrial abnormalities in inclusion-body myositis","volume":"66","author":"Oldfors","year":"2006","journal-title":"Neurology"},{"key":"10.1016\/j.expneurol.2010.07.021_bb0125","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1016\/0092-8674(93)90509-O","article-title":"Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death","volume":"74","author":"Oltvai","year":"1993","journal-title":"Cell"},{"key":"10.1016\/j.expneurol.2010.07.021_bb0130","doi-asserted-by":"crossref","first-page":"173","DOI":"10.2174\/1568007033482887","article-title":"Calpain and its involvement in the pathophysiology of CNS injuries and diseases: therapeutic potential of calpain inhibitors for prevention of neurodegeneration","volume":"2","author":"Ray","year":"2003","journal-title":"Curr. Drug Targets CNS Neurol. Disord."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0135","doi-asserted-by":"crossref","first-page":"2628","DOI":"10.1073\/pnas.90.7.2628","article-title":"Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration","volume":"90","author":"Saito","year":"1993","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.expneurol.2010.07.021_bb0140","first-page":"1228","article-title":"Interrelation of inflammation and APP in sIBM: IL-1 \u03b2 induces accumulation of \u03b2-amyloid in skeletal muscle","volume":"131","author":"Schmidt","year":"2008","journal-title":"Bain"},{"key":"10.1016\/j.expneurol.2010.07.021_bb0145","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1016\/0006-8993(89)90921-9","article-title":"Ischemia triggers NMDA receptor-linked cytoskeletal proteolysis in hippocampus","volume":"492","author":"Seubert","year":"1989","journal-title":"Brain Res."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0150","doi-asserted-by":"crossref","first-page":"11486","DOI":"10.1073\/pnas.96.20.11486","article-title":"A putative mechanism of demyelination in multiple sclerosis by a proteolytic enzyme, calpain","volume":"96","author":"Shields","year":"1999","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.expneurol.2010.07.021_bb0155","doi-asserted-by":"crossref","first-page":"E762","DOI":"10.1152\/ajpendo.90226.2008","article-title":"Calpain activity and muscle wasting in sepsis","volume":"295","author":"Smith","year":"2008","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0160","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.jns.2008.11.010","article-title":"Inflammatory myopathies with mitochondrial pathology and protein aggregates","volume":"278","author":"Temiz","year":"2009","journal-title":"J. Neurol. Sci."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0165","doi-asserted-by":"crossref","first-page":"4350","DOI":"10.1073\/pnas.76.9.4350","article-title":"Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications","volume":"76","author":"Towbin","year":"1979","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.expneurol.2010.07.021_bb0170","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1006\/abbi.1998.0748","article-title":"Caspase-mediated fragmentation of calpain inhibitor protein calpastatin during apoptosis","volume":"356","author":"Wang","year":"1998","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0175","doi-asserted-by":"crossref","first-page":"R580","DOI":"10.1152\/ajpregu.00341.2004","article-title":"Sepsis stimulates calpain activity in skeletal muscle by decreasing calpastatin activity but does not activate caspase-3","volume":"288","author":"Wei","year":"2005","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0180","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1006\/excr.2000.4859","article-title":"Cleavage of Bax enhances its cell death function","volume":"256","author":"Wood","year":"2000","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.expneurol.2010.07.021_bb0185","doi-asserted-by":"crossref","first-page":"18825","DOI":"10.1074\/jbc.271.31.18825","article-title":"The major calpain isozymes are long-lived proteins","volume":"271","author":"Zhang","year":"1996","journal-title":"J. Biol. Chem."}],"container-title":["Experimental Neurology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0014488610002591?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0014488610002591?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,16]],"date-time":"2025-09-16T05:40:57Z","timestamp":1758001257000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0014488610002591"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,10]]},"references-count":37,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2010,10]]}},"alternative-id":["S0014488610002591"],"URL":"https:\/\/doi.org\/10.1016\/j.expneurol.2010.07.021","relation":{},"ISSN":["0014-4886"],"issn-type":[{"value":"0014-4886","type":"print"}],"subject":[],"published":{"date-parts":[[2010,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Calpain inhibition attenuates intracellular changes in muscle cells in response to extracellular inflammatory stimulation","name":"articletitle","label":"Article Title"},{"value":"Experimental Neurology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.expneurol.2010.07.021","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2010 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}