The calpastatin/calpain system in trout Salmo trutta trutta muscle
Identifieur interne : 000F28 ( Istex/Corpus ); précédent : 000F27; suivant : 000F29The calpastatin/calpain system in trout Salmo trutta trutta muscle
Auteurs : E. Varricchio ; T. Rubino ; S. Paino ; T. Di Lascio ; O. Paciello ; M. LangellaSource :
- Journal of Fish Biology [ 0022-1112 ] ; 2004-12.
Abstract
Many recent reports suggest that the calpastatin/calpain system plays a role in cellular growth and differentiation. Defects of the calpastatin/calpain system have been linked to cellular dysfunctions, apoptosis, myocardial infarct, and dystrophies. The calpastatin/calpain system has also been implicated in post‐mortem tenderization of skeletal muscle through degradation of key myofibrillar and associated proteins, a process of key importance to meat quality. In the present study we investigate the presence and activity of the calpastatin/calpain system in trout muscle samples, collected at 0, 3, 18 and 28 h post‐mortem, by immunohistochemistry method. Calpastatin is a specific endogenous enzyme of cytosol, modulating the ubiquitous calpains. Calpastatin was found in samples obtained in vivo and immediately post‐mortem, but its concentration declined rapidly in samples obtained 3, 18 and 28 h post‐mortem. The ubiquitous m e m‐calpains, which are localized on Z line proteins and activated by intracellular Ca2+ increase, showed a rapid decline within 3 h post‐mortem. By contrast p94 calpain, which is specific to skeletal muscle, showed a slow decrease post‐mortem which was independent of intracellular Ca2+ increase. Our results suggest that the mechanism of activation and activity of the calpastatin/calpain system in trout is similar to that described in mammals.
Url:
DOI: 10.1111/j.0022-1112.2004.559av.x
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ISTEX:A6DE03AA7A4E2DBD8AB2F15E6B824623213D4236Le document en format XML
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Varricchio</name><affiliation><mods:affiliation>(Department of Animal Production Sciences, University of Basilicata, Potenza, Italy;</mods:affiliation></affiliation></author><author><name sortKey="Rubino, T" sort="Rubino, T" uniqKey="Rubino T" first="T." last="Rubino">T. Rubino</name><affiliation><mods:affiliation>(Department of Animal Production Sciences, University of Basilicata, Potenza, Italy;</mods:affiliation></affiliation></author><author><name sortKey="Paino, S" sort="Paino, S" uniqKey="Paino S" first="S." last="Paino">S. Paino</name><affiliation><mods:affiliation>(Department of Animal Production Sciences, University of Basilicata, Potenza, Italy;</mods:affiliation></affiliation></author><author><name sortKey="Di Lascio, T" sort="Di Lascio, T" uniqKey="Di Lascio T" first="T." last="Di Lascio">T. 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Langella</name><affiliation><mods:affiliation>(Department of Animal Production Sciences, University of Basilicata, Potenza, Italy;</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Fish Biology</title><idno type="ISSN">0022-1112</idno><idno type="eISSN">1095-8649</idno><imprint><publisher>Blackwell Science Ltd</publisher><pubPlace>Oxford, UK; Malden, USA</pubPlace><date type="published" when="2004-12">2004-12</date><biblScope unit="volume">65</biblScope><biblScope unit="supplement">s1</biblScope><biblScope unit="page" from="335">335</biblScope><biblScope unit="page" to="335">335</biblScope></imprint><idno type="ISSN">0022-1112</idno></series><idno type="istex">A6DE03AA7A4E2DBD8AB2F15E6B824623213D4236</idno><idno type="DOI">10.1111/j.0022-1112.2004.559av.x</idno><idno type="ArticleID">JFB559AV</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-1112</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Many recent reports suggest that the calpastatin/calpain system plays a role in cellular growth and differentiation. Defects of the calpastatin/calpain system have been linked to cellular dysfunctions, apoptosis, myocardial infarct, and dystrophies. The calpastatin/calpain system has also been implicated in post‐mortem tenderization of skeletal muscle through degradation of key myofibrillar and associated proteins, a process of key importance to meat quality. In the present study we investigate the presence and activity of the calpastatin/calpain system in trout muscle samples, collected at 0, 3, 18 and 28 h post‐mortem, by immunohistochemistry method. Calpastatin is a specific endogenous enzyme of cytosol, modulating the ubiquitous calpains. Calpastatin was found in samples obtained in vivo and immediately post‐mortem, but its concentration declined rapidly in samples obtained 3, 18 and 28 h post‐mortem. The ubiquitous m e m‐calpains, which are localized on Z line proteins and activated by intracellular Ca2+ increase, showed a rapid decline within 3 h post‐mortem. By contrast p94 calpain, which is specific to skeletal muscle, showed a slow decrease post‐mortem which was independent of intracellular Ca2+ increase. Our results suggest that the mechanism of activation and activity of the calpastatin/calpain system in trout is similar to that described in mammals.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>E. Varricchio</name><affiliations><json:string>(Department of Animal Production Sciences, University of Basilicata, Potenza, Italy;</json:string></affiliations></json:item><json:item><name>T. Rubino</name><affiliations><json:string>(Department of Animal Production Sciences, University of Basilicata, Potenza, Italy;</json:string></affiliations></json:item><json:item><name>S. Paino</name><affiliations><json:string>(Department of Animal Production Sciences, University of Basilicata, Potenza, Italy;</json:string></affiliations></json:item><json:item><name>T. 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Defects of the calpastatin/calpain system have been linked to cellular dysfunctions, apoptosis, myocardial infarct, and dystrophies. The calpastatin/calpain system has also been implicated in post‐mortem tenderization of skeletal muscle through degradation of key myofibrillar and associated proteins, a process of key importance to meat quality. In the present study we investigate the presence and activity of the calpastatin/calpain system in trout muscle samples, collected at 0, 3, 18 and 28 h post‐mortem, by immunohistochemistry method. Calpastatin is a specific endogenous enzyme of cytosol, modulating the ubiquitous calpains. Calpastatin was found in samples obtained <i>in vivo</i> and immediately post‐mortem, but its concentration declined rapidly in samples obtained 3, 18 and 28 h post‐mortem. The ubiquitous m e m‐calpains, which are localized on Z line proteins and activated by intracellular Ca<sup>2+</sup> increase, showed a rapid decline within 3 h post‐mortem. By contrast p94 calpain, which is specific to skeletal muscle, showed a slow decrease post‐mortem which was independent of intracellular Ca<sup>2+</sup> increase. 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Defects of the calpastatin/calpain system have been linked to cellular dysfunctions, apoptosis, myocardial infarct, and dystrophies. The calpastatin/calpain system has also been implicated in post‐mortem tenderization of skeletal muscle through degradation of key myofibrillar and associated proteins, a process of key importance to meat quality. In the present study we investigate the presence and activity of the calpastatin/calpain system in trout muscle samples, collected at 0, 3, 18 and 28 h post‐mortem, by immunohistochemistry method. Calpastatin is a specific endogenous enzyme of cytosol, modulating the ubiquitous calpains. Calpastatin was found in samples obtained in vivo and immediately post‐mortem, but its concentration declined rapidly in samples obtained 3, 18 and 28 h post‐mortem. The ubiquitous m e m‐calpains, which are localized on Z line proteins and activated by intracellular Ca2+ increase, showed a rapid decline within 3 h post‐mortem. By contrast p94 calpain, which is specific to skeletal muscle, showed a slow decrease post‐mortem which was independent of intracellular Ca2+ increase. Our results suggest that the mechanism of activation and activity of the calpastatin/calpain system in trout is similar to that described in mammals.</abstract><relatedItem type="host"><titleInfo><title>Journal of Fish Biology</title></titleInfo><genre type="journal">journal</genre><identifier type="ISSN">0022-1112</identifier><identifier type="eISSN">1095-8649</identifier><identifier type="DOI">10.1111/(ISSN)1095-8649</identifier><identifier type="PublisherID">JFB</identifier><part><date>2004</date><detail type="volume"><caption>vol.</caption><number>65</number></detail><detail type="supplement"><caption>Suppl. no.</caption><number>s1</number></detail><extent unit="pages"><start>335</start><end>335</end><total>1</total></extent></part></relatedItem><identifier type="istex">A6DE03AA7A4E2DBD8AB2F15E6B824623213D4236</identifier><identifier type="DOI">10.1111/j.0022-1112.2004.559av.x</identifier><identifier type="ArticleID">JFB559AV</identifier><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Blackwell Science Ltd</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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