El sistema proteolítico calpaina en la tenderización de la carne: Un enfoque molecular.

Autores:: Coria, María S.
Carranza, Pedro G.
Palma, Gustavo A.

Tipo de recurso:: Article of journal

Fecha de publicación:: 2018

Institución:: Universidad de Córdoba

Repositorio:: Repositorio Institucional Unicórdoba

Idioma:: spa

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dc.title.spa.fl_str_mv	El sistema proteolítico calpaina en la tenderización de la carne: Un enfoque molecular.
dc.title.translated.eng.fl_str_mv	Calpain System in meat tenderization: A molecular approach
title	El sistema proteolítico calpaina en la tenderización de la carne: Un enfoque molecular.
spellingShingle	El sistema proteolítico calpaina en la tenderización de la carne: Un enfoque molecular. Bovinae Molecular Markers Tenderness Bovinos marcadores moleculares terneza
title_short	El sistema proteolítico calpaina en la tenderización de la carne: Un enfoque molecular.
title_full	El sistema proteolítico calpaina en la tenderización de la carne: Un enfoque molecular.
title_fullStr	El sistema proteolítico calpaina en la tenderización de la carne: Un enfoque molecular.
title_full_unstemmed	El sistema proteolítico calpaina en la tenderización de la carne: Un enfoque molecular.
title_sort	El sistema proteolítico calpaina en la tenderización de la carne: Un enfoque molecular.
dc.creator.fl_str_mv	Coria, María S. Carranza, Pedro G. Palma, Gustavo A.
dc.contributor.author.spa.fl_str_mv	Coria, María S. Carranza, Pedro G. Palma, Gustavo A.
dc.subject.eng.fl_str_mv	Bovinae Molecular Markers Tenderness
topic	Bovinae Molecular Markers Tenderness Bovinos marcadores moleculares terneza
dc.subject.spa.fl_str_mv	Bovinos marcadores moleculares terneza
publishDate	2018
dc.date.accessioned.none.fl_str_mv	2018-01-10 00:00:00 2022-07-01T21:00:50Z
dc.date.available.none.fl_str_mv	2018-01-10 00:00:00 2022-07-01T21:00:50Z
dc.date.issued.none.fl_str_mv	2018-01-10
dc.type.spa.fl_str_mv	Artículo de revista
dc.type.eng.fl_str_mv	Journal article
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dc.relation.references.spa.fl_str_mv	Henchion MM, McCarthy M, Resconi VC. Beef quality attributes: A systematic review of consumer perspectives. Meat Sci 2017; 128:1–7. https://doi.org/10.1016/j.meatsci.2017.01.006 Destefanis G, Brugiapaglia A, Barge MT, Dal Molin E. Relationship between beef consumer tenderness perception and Warner–Bratzler shear force. Meat Sci 2008; 78(3):153–6. https://doi.org/10.1016/j.meatsci.2007.05.031 Herrera-Mendez CH, Becila S, Boudjellal A, Ouali A. Meat ageing: Reconsideration of the current concept. Trends Food Sci Technol 2006; 17(8):394–405. https://doi.org/10.1016/j.tifs.2006.01.011 Koohmaraie M, Geesink GH. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Sci 2006; 74(1):34–43. https://doi.org/10.1016/j.meatsci.2006.04.025 Goll DE, Thompson VF, Li H, Wei W, Cong J. The Calpain System. Physiol Rev 2003; 83(3):731–801. https://doi.org/10.1152/physrev.00029.2002 Campbell RL, Davies PL. Structure–function relationships in calpains. Biochem J 2012; 447:335–51. https://doi.org/10.1042/BJ20120921 Ono Y, Sorimachi H. Calpains - An elaborate proteolytic system. Biochim Biophys Acta - Proteins Proteomics 2012; 1824(1):224–36. https://doi.org/10.1016/j.bbapap.2011.08.005 Sorimachi H, Hata S, Ono Y. Impact of genetic insights into calpain biology. J Biochem 2011; 150(1):23–37. https://doi.org/10.1093/jb/mvr070 Varricchio E, Russolillo MG, Maruccio L, Velotto S, Campanile G, Paolucci M, et al. Immunological detection of m- and µ-calpains in the skeletal muscle of Marchigiana cattle. Eur J Histochem 2013; 57:10–5. https://doi.org/10.4081/ejh.2013.e2 Raynaud F, Fernandez E, Coulis G, Aubry L, Vignon X, Bleimling N, et al. Calpain 1 – titin interactions concentrate calpain 1 in the Z-band edges and in the N2-line region within the skeletal myofibril. FEBS J 2005; 272:2578–90. https://doi.org/10.1111/j.1742-4658.2005.04683.x Shaikh S, Samanta K, Kar P, Roy S, Chakraborti T, Chakraborti S. m-Calpain-mediated cleavage of Na+/Ca2+ exchanger-1 in caveolae vesicles isolated from pulmonary artery smooth muscle. Mol Cell Biochem 2010; 341:167–80. https://doi.org/10.1007/s11010-010-0448-z Samanta K, Kar P, Chakraborti T, Chakraborti S. An Overview of Endoplasmic Reticulum Calpain System. In: Chakraborti S, Dhalla N, editors. Proteases in Health and Disease Advances in Biochemistry in Health and Disease. New York, NY: Springer; 2013. https://doi.org/10.1007/978-1-4614-9233-7_1 Samanta K, Kar P, Chakraborti T, Shaikh S, Chakraborti S. Characteristic properties of endoplasmic reticulum membrane m-calpain, calpastatin and lumen m-calpain: A comparative study between membrane and lumen m-calpains. J Biochem 2010; 147(5):765–79. https://doi.org/10.1093/jb/mvq009 Kar P, Samanta K, Shaikh S, Chowdhury A, Chakraborti T, Chakraborti S. 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Genet Mol Res 2010; 9(3):1431–42. https://doi.org/10.4238/vol9-3gmr881 Casas E, White SN, Wheeler TL, Shackelford SD, Koohmaraie M, Riley DG, et al. Effects of calpastatin and u - calpain markers in beef cattle on tenderness traits. J Anim Sci 2006; 84:520–5. https://doi.org/10.2527/2006.843520x Mazzucco JP, Melucci LM, Villarreal EL, Mezzadra C a, Soria L, Corva P, et al. Effect of ageing and μ-calpain markers on meat quality from Brangus steers finished on pasture. Meat Sci 2010; 86(3):878–82. https://doi.org/10.1016/j.meatsci.2010.07.015 Curi RA, Chardulo LAL, Mason MC, Arrigoni MDB, Silveira AC, De Oliveira HN. Effect of single nucleotide polymorphisms of CAPN1 and CAST genes on meat traits in Nellore beef cattle (Bos indicus) and in their crosses with Bos taurus. Anim Genet 2009; 40:456–62. https://doi.org/10.1111/j.1365-2052.2009.01859.x Barendse W. DNA markers for meat tenders. Queensland (AU); US 2004/0115678: 2002. 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J Anim Sci 2016; 94(1):412–23. https://doi.org/10.2527/jas.2015-9862 Magolski JD, Berg EP, Hall NL, Anderson VL, Keller WL, Jeske TM, et al. Evaluation of feedlot cattle working chute behavior relative to temperament, tenderness, and postmortem proteolysis. Meat Sci 2013; 95:92–7. https://doi.org/10.1016/j.meatsci.2013.04.001 Kristensen L, Christensen M, Ertbjerg P. Activities of calpastatin, u-calpain and m-calpain are stable during frozen storage of meat. Meat Sci 2006; 72:116–20. https://doi.org/10.1016/j.meatsci.2005.06.010 Cruzen SM, Paulino PVR, Lonergan SM, Huff-Lonergan E. Postmortem proteolysis in three muscles from growing and mature beef cattle. Meat Sci 2014; 96(2):854–61. https://doi.org/10.1016/j.meatsci.2013.09.021 Guillemin N, Jurie C, Cassar-Malek I, Hocquette JF, Renand G, Picard B. Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type. Animal 2011; 5(6):885–94. https://doi.org/10.1017/S1751731110002612 Lee CE, McArdle A, Griffiths RD. The role of hormones, cytokines and heat shock proteins during age-related muscle loss. Clin Nutr 2007; 26(5):524–34. https://doi.org/10.1016/j.clnu.2007.05.005 Kristensen L, Therkildsen M, Riis B, Sørensen MT, Oksbjerg N, Purslow PP, et al. Dietary-induced changes of muscle growth rate in pigs : Effects on in vivo and postmortem muscle proteolysis and meat quality. J Anim Sci 2002; 820:2862–71. https://doi.org/10.2527/2002.80112862x Saccà E, Pizzutti N, Corazzin M, Lippe G, Piasentier E. Assessment of calpain and caspase systems activities during ageing of two bovine muscles by degradation patterns of α II spectrin and PARP-1. Anim Sci J 2016; 87:462–6. https://doi.org/10.1111/asj.12473
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spelling	Coria, María S.afd1e3d1-df8b-4787-91db-7210dda2483c-1Carranza, Pedro G.8f3b7852-32b2-45b5-988b-18bcbb928cc8-1Palma, Gustavo A.e905bcaa-d574-44da-a6ce-72285e54af17-12018-01-10 00:00:002022-07-01T21:00:50Z2018-01-10 00:00:002022-07-01T21:00:50Z2018-01-100122-0268https://repositorio.unicordoba.edu.co/handle/ucordoba/593010.21897/rmvz.1247https://doi.org/10.21897/rmvz.12471909-0544application/pdfapplication/xmlspaUniversidad de Córdobahttps://creativecommons.org/licenses/by-nc-sa/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2https://revistamvz.unicordoba.edu.co/article/view/1247BovinaeMolecular MarkersTendernessBovinosmarcadores molecularesternezaEl sistema proteolítico calpaina en la tenderización de la carne: Un enfoque molecular.Calpain System in meat tenderization: A molecular approachArtículo de revistaJournal articleinfo:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1info:eu-repo/semantics/publishedVersionTexthttp://purl.org/redcol/resource_type/ARTREFhttp://purl.org/coar/version/c_970fb48d4fbd8a85Henchion MM, McCarthy M, Resconi VC. Beef quality attributes: A systematic review of consumer perspectives. Meat Sci 2017; 128:1–7. https://doi.org/10.1016/j.meatsci.2017.01.006Destefanis G, Brugiapaglia A, Barge MT, Dal Molin E. Relationship between beef consumer tenderness perception and Warner–Bratzler shear force. Meat Sci 2008; 78(3):153–6. https://doi.org/10.1016/j.meatsci.2007.05.031Herrera-Mendez CH, Becila S, Boudjellal A, Ouali A. Meat ageing: Reconsideration of the current concept. Trends Food Sci Technol 2006; 17(8):394–405. https://doi.org/10.1016/j.tifs.2006.01.011Koohmaraie M, Geesink GH. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Sci 2006; 74(1):34–43. https://doi.org/10.1016/j.meatsci.2006.04.025Goll DE, Thompson VF, Li H, Wei W, Cong J. The Calpain System. Physiol Rev 2003; 83(3):731–801. https://doi.org/10.1152/physrev.00029.2002Campbell RL, Davies PL. Structure–function relationships in calpains. Biochem J 2012; 447:335–51. https://doi.org/10.1042/BJ20120921Ono Y, Sorimachi H. Calpains - An elaborate proteolytic system. Biochim Biophys Acta - Proteins Proteomics 2012; 1824(1):224–36. https://doi.org/10.1016/j.bbapap.2011.08.005Sorimachi H, Hata S, Ono Y. Impact of genetic insights into calpain biology. J Biochem 2011; 150(1):23–37. https://doi.org/10.1093/jb/mvr070Varricchio E, Russolillo MG, Maruccio L, Velotto S, Campanile G, Paolucci M, et al. Immunological detection of m- and µ-calpains in the skeletal muscle of Marchigiana cattle. Eur J Histochem 2013; 57:10–5. https://doi.org/10.4081/ejh.2013.e2Raynaud F, Fernandez E, Coulis G, Aubry L, Vignon X, Bleimling N, et al. Calpain 1 – titin interactions concentrate calpain 1 in the Z-band edges and in the N2-line region within the skeletal myofibril. 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Anim Sci J 2016; 87:462–6. https://doi.org/10.1111/asj.12473https://revistamvz.unicordoba.edu.co/article/download/1247/pdfhttps://revistamvz.unicordoba.edu.co/article/download/1247/2485Núm. 1 , Año 2018 : Revista MVZ Córdoba Volumen 23(1) Enero-abril 201865361652323Revista MVZ CórdobaPublicationOREORE.xmltext/xml2611https://repositorio.unicordoba.edu.co/bitstreams/de597df1-32b4-41da-90f0-04ee9dbc8705/downloadec3d5fce8373158fed7e79b813629170MD51ucordoba/5930oai:repositorio.unicordoba.edu.co:ucordoba/59302023-10-06 00:46:03.235https://creativecommons.org/licenses/by-nc-sa/4.0/metadata.onlyhttps://repositorio.unicordoba.edu.coRepositorio Universidad de Córdobabdigital@metabiblioteca.com

El sistema proteolítico calpaina en la tenderización de la carne: Un enfoque molecular.

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