Proteome Changes in Bovine Longissimus Thoracis Muscle during the First 48 h Postmortem: Shifts in Energy Status and Myofibrillar Stability
Changes in the insoluble protein fraction of bovine longissimus thoracis muscle from eight Norwegian Red (NRF) dual-purpose young bulls during the first 48 h postmortem were investigated by two-dimensional gel electrophoresis (2DE) and matrix-assisted laser desorption ionization−time of flight tande...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2010-06, Vol.58 (12), p.7408-7414 |
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| creator | Bjarnadóttir, Stefanía Guđrún Hollung, Kristin Færgestad, Ellen Mosleth Veiseth-Kent, Eva |
| description | Changes in the insoluble protein fraction of bovine longissimus thoracis muscle from eight Norwegian Red (NRF) dual-purpose young bulls during the first 48 h postmortem were investigated by two-dimensional gel electrophoresis (2DE) and matrix-assisted laser desorption ionization−time of flight tandem mass spectrometry (MALDI−TOF MS/MS). Significant changes were observed in a total of 35 proteins, and of those, 26 were identified and divided into three different groups: metabolic enzymes, cellular defense/stress proteins, and structural proteins, according to their predicted function. The majority of the metabolic enzymes identified are involved in the energy metabolism of the cell, while the cellular defense/stress proteins can be related to regulation and stabilization of the myofibrillar proteins. Both easily soluble proteins as well as structural proteins were identified in the insoluble protein fraction. We have studied the changes in solubility during postmortem storage by comparing the postmortem changes in protein composition between the soluble and insoluble protein fractions. We have identified two metabolic enzymes (2,3-bisphosphoglycerat mutase and NADH dehydrogenase) and one protein involved in the stress responses/apoptosis of the cell (Hsp70) that have not been identified previously in the insoluble protein fraction. The occurrence of these easily soluble proteins in the insoluble protein fraction could be due to precipitation or aggregation, thereby going from a soluble to an insoluble state. |
| doi_str_mv | 10.1021/jf100697h |
| format | Article |
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Significant changes were observed in a total of 35 proteins, and of those, 26 were identified and divided into three different groups: metabolic enzymes, cellular defense/stress proteins, and structural proteins, according to their predicted function. The majority of the metabolic enzymes identified are involved in the energy metabolism of the cell, while the cellular defense/stress proteins can be related to regulation and stabilization of the myofibrillar proteins. Both easily soluble proteins as well as structural proteins were identified in the insoluble protein fraction. We have studied the changes in solubility during postmortem storage by comparing the postmortem changes in protein composition between the soluble and insoluble protein fractions. We have identified two metabolic enzymes (2,3-bisphosphoglycerat mutase and NADH dehydrogenase) and one protein involved in the stress responses/apoptosis of the cell (Hsp70) that have not been identified previously in the insoluble protein fraction. The occurrence of these easily soluble proteins in the insoluble protein fraction could be due to precipitation or aggregation, thereby going from a soluble to an insoluble state.</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf100697h</identifier><identifier>PMID: 20515034</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>2,3-bisphosphoglycerate mutase ; animal proteins ; Animals ; Biological and medical sciences ; Cattle - metabolism ; cellular defense/stress proteins ; Electrophoresis, Gel, Two-Dimensional ; Energy ; Energy Metabolism ; enzymes ; Food Chemistry/Biochemistry ; food composition ; Food industries ; food storage ; Fundamental and applied biological sciences. Psychology ; General aspects ; longissimus thoracis ; Male ; metabolic enzymes ; Molecular Sequence Data ; Muscle, Skeletal - chemistry ; Muscle, Skeletal - metabolism ; muscles ; myofibrils ; Myofibrils - chemistry ; Myofibrils - metabolism ; NADH dehydrogenase ; phosphotransferases (phosphomutases) ; Postmortem Changes ; Proteins - chemistry ; Proteins - metabolism ; proteome ; Proteome - chemistry ; Proteome - metabolism ; Proteomics ; solubility ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; storage quality ; structural proteins ; Thoracic Wall - chemistry ; Thoracic Wall - metabolism</subject><ispartof>Journal of agricultural and food chemistry, 2010-06, Vol.58 (12), p.7408-7414</ispartof><rights>Copyright © 2010 American Chemical Society</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a368t-749dd471be6b8e0d0cbf36938f11f2ca7b94de2284843b71aa92738306021d353</citedby><cites>FETCH-LOGICAL-a368t-749dd471be6b8e0d0cbf36938f11f2ca7b94de2284843b71aa92738306021d353</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf100697h$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf100697h$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22901107$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20515034$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bjarnadóttir, Stefanía Guđrún</creatorcontrib><creatorcontrib>Hollung, Kristin</creatorcontrib><creatorcontrib>Færgestad, Ellen Mosleth</creatorcontrib><creatorcontrib>Veiseth-Kent, Eva</creatorcontrib><title>Proteome Changes in Bovine Longissimus Thoracis Muscle during the First 48 h Postmortem: Shifts in Energy Status and Myofibrillar Stability</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Changes in the insoluble protein fraction of bovine longissimus thoracis muscle from eight Norwegian Red (NRF) dual-purpose young bulls during the first 48 h postmortem were investigated by two-dimensional gel electrophoresis (2DE) and matrix-assisted laser desorption ionization−time of flight tandem mass spectrometry (MALDI−TOF MS/MS). Significant changes were observed in a total of 35 proteins, and of those, 26 were identified and divided into three different groups: metabolic enzymes, cellular defense/stress proteins, and structural proteins, according to their predicted function. The majority of the metabolic enzymes identified are involved in the energy metabolism of the cell, while the cellular defense/stress proteins can be related to regulation and stabilization of the myofibrillar proteins. Both easily soluble proteins as well as structural proteins were identified in the insoluble protein fraction. We have studied the changes in solubility during postmortem storage by comparing the postmortem changes in protein composition between the soluble and insoluble protein fractions. We have identified two metabolic enzymes (2,3-bisphosphoglycerat mutase and NADH dehydrogenase) and one protein involved in the stress responses/apoptosis of the cell (Hsp70) that have not been identified previously in the insoluble protein fraction. The occurrence of these easily soluble proteins in the insoluble protein fraction could be due to precipitation or aggregation, thereby going from a soluble to an insoluble state.</description><subject>2,3-bisphosphoglycerate mutase</subject><subject>animal proteins</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cattle - metabolism</subject><subject>cellular defense/stress proteins</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Energy</subject><subject>Energy Metabolism</subject><subject>enzymes</subject><subject>Food Chemistry/Biochemistry</subject><subject>food composition</subject><subject>Food industries</subject><subject>food storage</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects</subject><subject>longissimus thoracis</subject><subject>Male</subject><subject>metabolic enzymes</subject><subject>Molecular Sequence Data</subject><subject>Muscle, Skeletal - chemistry</subject><subject>Muscle, Skeletal - metabolism</subject><subject>muscles</subject><subject>myofibrils</subject><subject>Myofibrils - chemistry</subject><subject>Myofibrils - metabolism</subject><subject>NADH dehydrogenase</subject><subject>phosphotransferases (phosphomutases)</subject><subject>Postmortem Changes</subject><subject>Proteins - chemistry</subject><subject>Proteins - metabolism</subject><subject>proteome</subject><subject>Proteome - chemistry</subject><subject>Proteome - metabolism</subject><subject>Proteomics</subject><subject>solubility</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>storage quality</subject><subject>structural proteins</subject><subject>Thoracic Wall - chemistry</subject><subject>Thoracic Wall - metabolism</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkMFu1DAQQC0EokvhwA-ALwhxCMzESexwo6sWkLai0rbnyEnsxKvEbm0Hab-hP43LLoUDp5Fmnp5Gj5DXCB8Rcvy00whQ1Xx8QlZY5pCViOIpWUE6ZqKs8IS8CGEHAKLk8Jyc5FBiCaxYkfsr76Jys6LrUdpBBWosPXM_jVV04-xgQjDzEuj16LzsTKCXS-gmRfvFGzvQOCp6YXyItBB0pFcuxNn5qObPdDsaHX_rzq3yw55uo4zJJG1PL_dOm9abaZL-Yd-aycT9S_JMyymoV8d5Sm4uzq_X37LNj6_f1182mWSViBkv6r4vOLaqaoWCHrpWs6pmQiPqvJO8rYte5bkoRMFajlLWOWeCQZVy9Kxkp-T9wXvr3d2iQmxmEzqVnrHKLaHhjLESeQWJ_HAgO-9C8Eo3t97M0u8bhOYhffOYPrFvjtalnVX_SP5pnYB3R0CGTk7aS5uC_uXyGhCBJ-7tgdPSNXLwibnZ5oAMUFQV1v-YZBeanVu8Tbn-89IvZ-eg8w</recordid><startdate>20100623</startdate><enddate>20100623</enddate><creator>Bjarnadóttir, Stefanía Guđrún</creator><creator>Hollung, Kristin</creator><creator>Færgestad, Ellen Mosleth</creator><creator>Veiseth-Kent, Eva</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20100623</creationdate><title>Proteome Changes in Bovine Longissimus Thoracis Muscle during the First 48 h Postmortem: Shifts in Energy Status and Myofibrillar Stability</title><author>Bjarnadóttir, Stefanía Guđrún ; Hollung, Kristin ; Færgestad, Ellen Mosleth ; Veiseth-Kent, Eva</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a368t-749dd471be6b8e0d0cbf36938f11f2ca7b94de2284843b71aa92738306021d353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>2,3-bisphosphoglycerate mutase</topic><topic>animal proteins</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cattle - metabolism</topic><topic>cellular defense/stress proteins</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Energy</topic><topic>Energy Metabolism</topic><topic>enzymes</topic><topic>Food Chemistry/Biochemistry</topic><topic>food composition</topic><topic>Food industries</topic><topic>food storage</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects</topic><topic>longissimus thoracis</topic><topic>Male</topic><topic>metabolic enzymes</topic><topic>Molecular Sequence Data</topic><topic>Muscle, Skeletal - chemistry</topic><topic>Muscle, Skeletal - metabolism</topic><topic>muscles</topic><topic>myofibrils</topic><topic>Myofibrils - chemistry</topic><topic>Myofibrils - metabolism</topic><topic>NADH dehydrogenase</topic><topic>phosphotransferases (phosphomutases)</topic><topic>Postmortem Changes</topic><topic>Proteins - chemistry</topic><topic>Proteins - metabolism</topic><topic>proteome</topic><topic>Proteome - chemistry</topic><topic>Proteome - metabolism</topic><topic>Proteomics</topic><topic>solubility</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>storage quality</topic><topic>structural proteins</topic><topic>Thoracic Wall - chemistry</topic><topic>Thoracic Wall - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bjarnadóttir, Stefanía Guđrún</creatorcontrib><creatorcontrib>Hollung, Kristin</creatorcontrib><creatorcontrib>Færgestad, Ellen Mosleth</creatorcontrib><creatorcontrib>Veiseth-Kent, Eva</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bjarnadóttir, Stefanía Guđrún</au><au>Hollung, Kristin</au><au>Færgestad, Ellen Mosleth</au><au>Veiseth-Kent, Eva</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteome Changes in Bovine Longissimus Thoracis Muscle during the First 48 h Postmortem: Shifts in Energy Status and Myofibrillar Stability</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2010-06-23</date><risdate>2010</risdate><volume>58</volume><issue>12</issue><spage>7408</spage><epage>7414</epage><pages>7408-7414</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>Changes in the insoluble protein fraction of bovine longissimus thoracis muscle from eight Norwegian Red (NRF) dual-purpose young bulls during the first 48 h postmortem were investigated by two-dimensional gel electrophoresis (2DE) and matrix-assisted laser desorption ionization−time of flight tandem mass spectrometry (MALDI−TOF MS/MS). Significant changes were observed in a total of 35 proteins, and of those, 26 were identified and divided into three different groups: metabolic enzymes, cellular defense/stress proteins, and structural proteins, according to their predicted function. The majority of the metabolic enzymes identified are involved in the energy metabolism of the cell, while the cellular defense/stress proteins can be related to regulation and stabilization of the myofibrillar proteins. Both easily soluble proteins as well as structural proteins were identified in the insoluble protein fraction. We have studied the changes in solubility during postmortem storage by comparing the postmortem changes in protein composition between the soluble and insoluble protein fractions. We have identified two metabolic enzymes (2,3-bisphosphoglycerat mutase and NADH dehydrogenase) and one protein involved in the stress responses/apoptosis of the cell (Hsp70) that have not been identified previously in the insoluble protein fraction. The occurrence of these easily soluble proteins in the insoluble protein fraction could be due to precipitation or aggregation, thereby going from a soluble to an insoluble state.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>20515034</pmid><doi>10.1021/jf100697h</doi><tpages>7</tpages></addata></record> |
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| ispartof | Journal of agricultural and food chemistry, 2010-06, Vol.58 (12), p.7408-7414 |
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| subjects | 2,3-bisphosphoglycerate mutase animal proteins Animals Biological and medical sciences Cattle - metabolism cellular defense/stress proteins Electrophoresis, Gel, Two-Dimensional Energy Energy Metabolism enzymes Food Chemistry/Biochemistry food composition Food industries food storage Fundamental and applied biological sciences. Psychology General aspects longissimus thoracis Male metabolic enzymes Molecular Sequence Data Muscle, Skeletal - chemistry Muscle, Skeletal - metabolism muscles myofibrils Myofibrils - chemistry Myofibrils - metabolism NADH dehydrogenase phosphotransferases (phosphomutases) Postmortem Changes Proteins - chemistry Proteins - metabolism proteome Proteome - chemistry Proteome - metabolism Proteomics solubility Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization storage quality structural proteins Thoracic Wall - chemistry Thoracic Wall - metabolism |
| title | Proteome Changes in Bovine Longissimus Thoracis Muscle during the First 48 h Postmortem: Shifts in Energy Status and Myofibrillar Stability |
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