Capillary Supply in Relation to Myosin Heavy Chain Fibre Composition of Human Intrinsic Tongue Muscles
The capillary supply and myosin heavy chain (MyHC) composition of three different intrinsic tongue muscles was analysed in the anterior and posterior regions of the human tongue with biochemical and immunohistochemical techniques. Mean capillary density for the whole tongue was 796 ± 82 cap/mm 2 , w...
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description | The capillary supply and myosin heavy chain (MyHC) composition of three different intrinsic tongue muscles was analysed in the anterior and posterior regions of the human tongue with biochemical and immunohistochemical techniques. Mean capillary density for the whole tongue was 796 ± 82 cap/mm 2 , without regional differences. The overall number of capillaries around each fibre (CAF) was higher in the posterior than in the anterior region (2.5 vs. 2.1, p = 0.009). However, correcting for regional differences in fibre size, CAF per fibre area was higher in the anterior region (4.3 vs. 3.0, p < 0.001). Muscle fibres containing fast MyHCs predominated in the anterior region (78.7%), consisting of MyHCIIa (58.5%), MyHCIIx (1.0%), MyHCIIa+MyHCIIx (11.3%) and MyHCI+MyHCIIa (7.9%). Fibres containing slow MyHC predominated in the posterior region (65.2%), consisting of MyHCI (45.5%) and MyHCI+MyHCIIa (19.7%). A minor fibre population ( |
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Mean capillary density for the whole tongue was 796 ± 82 cap/mm 2 , without regional differences. The overall number of capillaries around each fibre (CAF) was higher in the posterior than in the anterior region (2.5 vs. 2.1, p = 0.009). However, correcting for regional differences in fibre size, CAF per fibre area was higher in the anterior region (4.3 vs. 3.0, p < 0.001). Muscle fibres containing fast MyHCs predominated in the anterior region (78.7%), consisting of MyHCIIa (58.5%), MyHCIIx (1.0%), MyHCIIa+MyHCIIx (11.3%) and MyHCI+MyHCIIa (7.9%). Fibres containing slow MyHC predominated in the posterior region (65.2%), consisting of MyHCI (45.5%) and MyHCI+MyHCIIa (19.7%). A minor fibre population (<2%) contained unusual MyHC isoforms, namely MyHC foetal, MyHC slow-tonic, MyHC α-cardiac or MyHC embryonic. The microvascularization of the human tongue was twice as high as in human limb muscles. Regional similarities in capillary supply, but differences in fibre phenotype composition, suggest that human tongue muscle fibres are fatigue resistant independently of MyHC content. High frequency of hybrid fibres, that is fibres co-expressing two or more MyHC isoforms, indicates a wider spectrum of fibre contractile properties than in limb muscles. In conclusion, human intrinsic tongue muscles showed internal specialization in distribution of MyHC isoforms and capillary supply, but not in the expression of unusual MyHCs.</description><identifier>ISSN: 1422-6405</identifier><identifier>ISSN: 1422-6421</identifier><identifier>EISSN: 1422-6421</identifier><identifier>DOI: 10.1159/000318645</identifier><identifier>PMID: 20616532</identifier><language>eng</language><publisher>Basel, Switzerland: S. Karger AG</publisher><subject>Adult ; anatomi ; Capillaries ; Capillaries - anatomy & histology ; Female ; Fibre types ; Human ; Human Anatomy ; Humans ; Male ; Middle Aged ; Muscle ; Muscle Fibers, Fast-Twitch - chemistry ; Muscle Fibers, Skeletal - chemistry ; Muscle Fibers, Slow-Twitch - chemistry ; Muscle, Skeletal - blood supply ; Muscle, Skeletal - chemistry ; Myosin heavy chain ; Myosin Heavy Chains - analysis ; Original Paper ; Protein Isoforms - analysis ; Skeletal Muscle Myosins - analysis ; Tongue ; Tongue - anatomy & histology ; Tongue - blood supply ; Tongue - chemistry</subject><ispartof>Cells, tissues, organs, 2010-01, Vol.192 (5), p.303-313</ispartof><rights>2010 S. Karger AG, Basel</rights><rights>Copyright © 2010 S. Karger AG, Basel.</rights><rights>Copyright (c) 2010 S. Karger AG, Basel</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c369t-f5ece1cacc0c61805a377ae6a1a8f90aeb121af73aa336f7dd2ffd0f080f0d5f3</citedby><cites>FETCH-LOGICAL-c369t-f5ece1cacc0c61805a377ae6a1a8f90aeb121af73aa336f7dd2ffd0f080f0d5f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,2422,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20616532$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-39530$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Granberg, I.</creatorcontrib><creatorcontrib>Lindell, B.</creatorcontrib><creatorcontrib>Eriksson, P.-O.</creatorcontrib><creatorcontrib>Pedrosa-Domellöf, F.</creatorcontrib><creatorcontrib>Stål, P.</creatorcontrib><title>Capillary Supply in Relation to Myosin Heavy Chain Fibre Composition of Human Intrinsic Tongue Muscles</title><title>Cells, tissues, organs</title><addtitle>Cells Tissues Organs</addtitle><description>The capillary supply and myosin heavy chain (MyHC) composition of three different intrinsic tongue muscles was analysed in the anterior and posterior regions of the human tongue with biochemical and immunohistochemical techniques. Mean capillary density for the whole tongue was 796 ± 82 cap/mm 2 , without regional differences. The overall number of capillaries around each fibre (CAF) was higher in the posterior than in the anterior region (2.5 vs. 2.1, p = 0.009). However, correcting for regional differences in fibre size, CAF per fibre area was higher in the anterior region (4.3 vs. 3.0, p < 0.001). Muscle fibres containing fast MyHCs predominated in the anterior region (78.7%), consisting of MyHCIIa (58.5%), MyHCIIx (1.0%), MyHCIIa+MyHCIIx (11.3%) and MyHCI+MyHCIIa (7.9%). Fibres containing slow MyHC predominated in the posterior region (65.2%), consisting of MyHCI (45.5%) and MyHCI+MyHCIIa (19.7%). A minor fibre population (<2%) contained unusual MyHC isoforms, namely MyHC foetal, MyHC slow-tonic, MyHC α-cardiac or MyHC embryonic. The microvascularization of the human tongue was twice as high as in human limb muscles. Regional similarities in capillary supply, but differences in fibre phenotype composition, suggest that human tongue muscle fibres are fatigue resistant independently of MyHC content. High frequency of hybrid fibres, that is fibres co-expressing two or more MyHC isoforms, indicates a wider spectrum of fibre contractile properties than in limb muscles. In conclusion, human intrinsic tongue muscles showed internal specialization in distribution of MyHC isoforms and capillary supply, but not in the expression of unusual MyHCs.</description><subject>Adult</subject><subject>anatomi</subject><subject>Capillaries</subject><subject>Capillaries - anatomy & histology</subject><subject>Female</subject><subject>Fibre types</subject><subject>Human</subject><subject>Human Anatomy</subject><subject>Humans</subject><subject>Male</subject><subject>Middle Aged</subject><subject>Muscle</subject><subject>Muscle Fibers, Fast-Twitch - chemistry</subject><subject>Muscle Fibers, Skeletal - chemistry</subject><subject>Muscle Fibers, Slow-Twitch - chemistry</subject><subject>Muscle, Skeletal - blood supply</subject><subject>Muscle, Skeletal - chemistry</subject><subject>Myosin heavy chain</subject><subject>Myosin Heavy Chains - analysis</subject><subject>Original Paper</subject><subject>Protein Isoforms - analysis</subject><subject>Skeletal Muscle Myosins - analysis</subject><subject>Tongue</subject><subject>Tongue - anatomy & histology</subject><subject>Tongue - blood supply</subject><subject>Tongue - chemistry</subject><issn>1422-6405</issn><issn>1422-6421</issn><issn>1422-6421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpd0Utv1DAQAGCrAtEHHHqvKosLQmKpH-s8jlVo2UqtkKDt1Zp1xluXJA52DNp_j2GXHDhYHnk-jzUeQk45-8i5qi8YY5JXxVIdkCO-FGJRLAV_McdMHZLjGJ8zEznxihwKVvBCSXFEbAOj6zoIW_otjWO3pW6gX7GDyfmBTp7ebX3MRyuEn1vaPEGOr906IG18P-bUX-ctXaUeBnozTMEN0Rl674dNQnqXoukwviYvLXQR3-z3E_JwfXXfrBa3Xz7fNJe3CyOLelpYhQa5AWOYKXjFFMiyBCyAQ2VrBrjmgoMtJYCUhS3bVljbMsuqvFpl5Qn5sKsbf-GY1noMrs-9aQ9Of3KPl9qHjU590rJWkmX-bsfH4H8kjJPuXTSY_2NAn6IuVVXJUlYyy7f_yWefwpB7yagWiqlSZfR-h0zwMQa08_uc6T-T0vOksj3fF0zrHttZ_htNBmc78B3CBsMM9vd_A_26l6g</recordid><startdate>20100101</startdate><enddate>20100101</enddate><creator>Granberg, I.</creator><creator>Lindell, B.</creator><creator>Eriksson, P.-O.</creator><creator>Pedrosa-Domellöf, F.</creator><creator>Stål, P.</creator><general>S. 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Lindell, B. ; Eriksson, P.-O. ; Pedrosa-Domellöf, F. ; Stål, P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c369t-f5ece1cacc0c61805a377ae6a1a8f90aeb121af73aa336f7dd2ffd0f080f0d5f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Adult</topic><topic>anatomi</topic><topic>Capillaries</topic><topic>Capillaries - anatomy & histology</topic><topic>Female</topic><topic>Fibre types</topic><topic>Human</topic><topic>Human Anatomy</topic><topic>Humans</topic><topic>Male</topic><topic>Middle Aged</topic><topic>Muscle</topic><topic>Muscle Fibers, Fast-Twitch - chemistry</topic><topic>Muscle Fibers, Skeletal - chemistry</topic><topic>Muscle Fibers, Slow-Twitch - chemistry</topic><topic>Muscle, Skeletal - blood supply</topic><topic>Muscle, Skeletal - chemistry</topic><topic>Myosin heavy chain</topic><topic>Myosin Heavy Chains - analysis</topic><topic>Original Paper</topic><topic>Protein Isoforms - analysis</topic><topic>Skeletal Muscle Myosins - analysis</topic><topic>Tongue</topic><topic>Tongue - anatomy & histology</topic><topic>Tongue - blood supply</topic><topic>Tongue - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Granberg, I.</creatorcontrib><creatorcontrib>Lindell, B.</creatorcontrib><creatorcontrib>Eriksson, P.-O.</creatorcontrib><creatorcontrib>Pedrosa-Domellöf, F.</creatorcontrib><creatorcontrib>Stål, P.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>SwePub</collection><collection>SwePub Articles</collection><collection>SWEPUB Umeå universitet</collection><jtitle>Cells, tissues, organs</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Granberg, I.</au><au>Lindell, B.</au><au>Eriksson, P.-O.</au><au>Pedrosa-Domellöf, F.</au><au>Stål, P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Capillary Supply in Relation to Myosin Heavy Chain Fibre Composition of Human Intrinsic Tongue Muscles</atitle><jtitle>Cells, tissues, organs</jtitle><addtitle>Cells Tissues Organs</addtitle><date>2010-01-01</date><risdate>2010</risdate><volume>192</volume><issue>5</issue><spage>303</spage><epage>313</epage><pages>303-313</pages><issn>1422-6405</issn><issn>1422-6421</issn><eissn>1422-6421</eissn><abstract>The capillary supply and myosin heavy chain (MyHC) composition of three different intrinsic tongue muscles was analysed in the anterior and posterior regions of the human tongue with biochemical and immunohistochemical techniques. Mean capillary density for the whole tongue was 796 ± 82 cap/mm 2 , without regional differences. The overall number of capillaries around each fibre (CAF) was higher in the posterior than in the anterior region (2.5 vs. 2.1, p = 0.009). However, correcting for regional differences in fibre size, CAF per fibre area was higher in the anterior region (4.3 vs. 3.0, p < 0.001). Muscle fibres containing fast MyHCs predominated in the anterior region (78.7%), consisting of MyHCIIa (58.5%), MyHCIIx (1.0%), MyHCIIa+MyHCIIx (11.3%) and MyHCI+MyHCIIa (7.9%). Fibres containing slow MyHC predominated in the posterior region (65.2%), consisting of MyHCI (45.5%) and MyHCI+MyHCIIa (19.7%). A minor fibre population (<2%) contained unusual MyHC isoforms, namely MyHC foetal, MyHC slow-tonic, MyHC α-cardiac or MyHC embryonic. The microvascularization of the human tongue was twice as high as in human limb muscles. Regional similarities in capillary supply, but differences in fibre phenotype composition, suggest that human tongue muscle fibres are fatigue resistant independently of MyHC content. High frequency of hybrid fibres, that is fibres co-expressing two or more MyHC isoforms, indicates a wider spectrum of fibre contractile properties than in limb muscles. In conclusion, human intrinsic tongue muscles showed internal specialization in distribution of MyHC isoforms and capillary supply, but not in the expression of unusual MyHCs.</abstract><cop>Basel, Switzerland</cop><pub>S. Karger AG</pub><pmid>20616532</pmid><doi>10.1159/000318645</doi><tpages>11</tpages></addata></record> |
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subjects | Adult anatomi Capillaries Capillaries - anatomy & histology Female Fibre types Human Human Anatomy Humans Male Middle Aged Muscle Muscle Fibers, Fast-Twitch - chemistry Muscle Fibers, Skeletal - chemistry Muscle Fibers, Slow-Twitch - chemistry Muscle, Skeletal - blood supply Muscle, Skeletal - chemistry Myosin heavy chain Myosin Heavy Chains - analysis Original Paper Protein Isoforms - analysis Skeletal Muscle Myosins - analysis Tongue Tongue - anatomy & histology Tongue - blood supply Tongue - chemistry |
title | Capillary Supply in Relation to Myosin Heavy Chain Fibre Composition of Human Intrinsic Tongue Muscles |
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