Relationships between structural characteristics of bovine intramuscular connective tissue assessed by image analysis and collagen and proteoglycan content
Three muscles (Longissimus thoracis, Semimembranosus, Biceps femoris) of 40 young bulls from 3 breeds were used to quantify structural characteristics of bovine connective tissue by image analysis, with both macroscopic and microscopic approaches. Collagen and proteoglycan content was also investiga...
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| Veröffentlicht in: | Meat science 2013-03, Vol.93 (3), p.378-386 |
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| creator | Dubost, Annabelle Micol, Didier Meunier, Bruno Lethias, Claire Listrat, Anne |
| description | Three muscles (Longissimus thoracis, Semimembranosus, Biceps femoris) of 40 young bulls from 3 breeds were used to quantify structural characteristics of bovine connective tissue by image analysis, with both macroscopic and microscopic approaches. Collagen and proteoglycan content was also investigated. Perimysium occupied a greater area (8 vs 6%), and was wider (42 vs 2μm) and shorter per unit area (1.9 vs 30mmmm−2) than endomysium. Perimysium and endomysium from Longissimus were thinner, less ramified than in Biceps. Longissimus showed less total collagen and cross-linking and more proteoglycans (P |
| doi_str_mv | 10.1016/j.meatsci.2012.09.020 |
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Collagen and proteoglycan content was also investigated. Perimysium occupied a greater area (8 vs 6%), and was wider (42 vs 2μm) and shorter per unit area (1.9 vs 30mmmm−2) than endomysium. Perimysium and endomysium from Longissimus were thinner, less ramified than in Biceps. Longissimus showed less total collagen and cross-linking and more proteoglycans (P<0.0001) than Biceps muscle. Blond d'Aquitaine perimysium occupied less area, was more ramified and muscles contained less collagen, cross-linking and more proteoglycans than Angus (P<0.001). Limousin was intermediate. High proteoglycan content in muscle containing less total collagen suggested a complementarity between these molecules. They might influence mechanical properties of intramuscular connective tissue. This was especially true given that proteoglycans and total collagen were negatively and positively linked with structural parameters, respectively.</description><identifier>ISSN: 0309-1740</identifier><identifier>EISSN: 1873-4138</identifier><identifier>DOI: 10.1016/j.meatsci.2012.09.020</identifier><identifier>PMID: 23273440</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Animals ; Beef breed ; Cattle ; Collagen ; Collagen - analysis ; Collagen - ultrastructure ; Connective Tissue - anatomy & histology ; Connective Tissue - ultrastructure ; Endomysium ; Food and Nutrition ; Life Sciences ; Male ; Meat - analysis ; Muscle ; Muscle, Skeletal - anatomy & histology ; Muscle, Skeletal - chemistry ; Muscle, Skeletal - ultrastructure ; Perimysium ; Proteoglycans ; Proteoglycans - analysis</subject><ispartof>Meat science, 2013-03, Vol.93 (3), p.378-386</ispartof><rights>2012 Elsevier Ltd</rights><rights>Copyright © 2012 Elsevier Ltd. All rights reserved.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c446t-ad738b5782cbcfce64d455e9da1ec28f929713a890a601260e45a4fcd13a31ff3</citedby><cites>FETCH-LOGICAL-c446t-ad738b5782cbcfce64d455e9da1ec28f929713a890a601260e45a4fcd13a31ff3</cites><orcidid>0000-0002-8188-405X ; 0000-0002-6182-1764</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.meatsci.2012.09.020$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,780,784,885,3541,27915,27916,45986</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23273440$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02647008$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Dubost, Annabelle</creatorcontrib><creatorcontrib>Micol, Didier</creatorcontrib><creatorcontrib>Meunier, Bruno</creatorcontrib><creatorcontrib>Lethias, Claire</creatorcontrib><creatorcontrib>Listrat, Anne</creatorcontrib><title>Relationships between structural characteristics of bovine intramuscular connective tissue assessed by image analysis and collagen and proteoglycan content</title><title>Meat science</title><addtitle>Meat Sci</addtitle><description>Three muscles (Longissimus thoracis, Semimembranosus, Biceps femoris) of 40 young bulls from 3 breeds were used to quantify structural characteristics of bovine connective tissue by image analysis, with both macroscopic and microscopic approaches. Collagen and proteoglycan content was also investigated. Perimysium occupied a greater area (8 vs 6%), and was wider (42 vs 2μm) and shorter per unit area (1.9 vs 30mmmm−2) than endomysium. Perimysium and endomysium from Longissimus were thinner, less ramified than in Biceps. Longissimus showed less total collagen and cross-linking and more proteoglycans (P<0.0001) than Biceps muscle. Blond d'Aquitaine perimysium occupied less area, was more ramified and muscles contained less collagen, cross-linking and more proteoglycans than Angus (P<0.001). Limousin was intermediate. High proteoglycan content in muscle containing less total collagen suggested a complementarity between these molecules. They might influence mechanical properties of intramuscular connective tissue. This was especially true given that proteoglycans and total collagen were negatively and positively linked with structural parameters, respectively.</description><subject>Animals</subject><subject>Beef breed</subject><subject>Cattle</subject><subject>Collagen</subject><subject>Collagen - analysis</subject><subject>Collagen - ultrastructure</subject><subject>Connective Tissue - anatomy & histology</subject><subject>Connective Tissue - ultrastructure</subject><subject>Endomysium</subject><subject>Food and Nutrition</subject><subject>Life Sciences</subject><subject>Male</subject><subject>Meat - analysis</subject><subject>Muscle</subject><subject>Muscle, Skeletal - anatomy & histology</subject><subject>Muscle, Skeletal - chemistry</subject><subject>Muscle, Skeletal - ultrastructure</subject><subject>Perimysium</subject><subject>Proteoglycans</subject><subject>Proteoglycans - analysis</subject><issn>0309-1740</issn><issn>1873-4138</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUV2LFDEQDKJ46-lPUPKoD7N2MpmvJzkOvRMWBNHnkMn03GaZSdZ0ZmV_i3_W7O16r0Ig6aK6qtPF2FsBawGi_rhbz2gSWbeWIOQaujVIeMZWom3KQomyfc5WUEJXiEbBFXtFtAMAUcr2JbuSpWxKpWDF_nzHySQXPG3dnniP6Tei55TiYtMSzcTt1kRjE0ZHyVniYeR9ODiP3PkUzbyQXSYTuQ3eo03ugDw5ogW5IcJ8Bt4fuZvNQ0a8mY7kKD-G3DBNGfSPxT6GhOFhOlrjT1IJfXrNXoxmInxzua_Zzy-ff9zeF5tvd19vbzaFVapOhRmasu2rppW2t6PFWg2qqrAbjEAr27GTXSNK03Zg6ryqGlBVRo12yGApxrG8Zh_Oulsz6X3Mo8ajDsbp-5uNPmEga9UAtAeRue_P3DzwrwUp6dmRxfwTj2EhLfJiG1V1SmVqdabaGIgijk_aAvQpQ73Tlwz1KUMNXXaC3PfuYrH0Mw5PXf9Cy4RPZwLmpRwcRp0l0FscXMwJ6CG4_1j8BUkVtJw</recordid><startdate>20130301</startdate><enddate>20130301</enddate><creator>Dubost, Annabelle</creator><creator>Micol, Didier</creator><creator>Meunier, Bruno</creator><creator>Lethias, Claire</creator><creator>Listrat, Anne</creator><general>Elsevier Ltd</general><general>Elsevier</general><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><scope>1XC</scope><scope>VOOES</scope><orcidid>https://orcid.org/0000-0002-8188-405X</orcidid><orcidid>https://orcid.org/0000-0002-6182-1764</orcidid></search><sort><creationdate>20130301</creationdate><title>Relationships between structural characteristics of bovine intramuscular connective tissue assessed by image analysis and collagen and proteoglycan content</title><author>Dubost, Annabelle ; 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Collagen and proteoglycan content was also investigated. Perimysium occupied a greater area (8 vs 6%), and was wider (42 vs 2μm) and shorter per unit area (1.9 vs 30mmmm−2) than endomysium. Perimysium and endomysium from Longissimus were thinner, less ramified than in Biceps. Longissimus showed less total collagen and cross-linking and more proteoglycans (P<0.0001) than Biceps muscle. Blond d'Aquitaine perimysium occupied less area, was more ramified and muscles contained less collagen, cross-linking and more proteoglycans than Angus (P<0.001). Limousin was intermediate. High proteoglycan content in muscle containing less total collagen suggested a complementarity between these molecules. They might influence mechanical properties of intramuscular connective tissue. This was especially true given that proteoglycans and total collagen were negatively and positively linked with structural parameters, respectively.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>23273440</pmid><doi>10.1016/j.meatsci.2012.09.020</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-8188-405X</orcidid><orcidid>https://orcid.org/0000-0002-6182-1764</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Beef breed Cattle Collagen Collagen - analysis Collagen - ultrastructure Connective Tissue - anatomy & histology Connective Tissue - ultrastructure Endomysium Food and Nutrition Life Sciences Male Meat - analysis Muscle Muscle, Skeletal - anatomy & histology Muscle, Skeletal - chemistry Muscle, Skeletal - ultrastructure Perimysium Proteoglycans Proteoglycans - analysis |
| title | Relationships between structural characteristics of bovine intramuscular connective tissue assessed by image analysis and collagen and proteoglycan content |
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