| pubmed-article:19633189 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19633189 | lifeskim:mentions | umls-concept:C0022984 | lld:lifeskim |
| pubmed-article:19633189 | lifeskim:mentions | umls-concept:C0085872 | lld:lifeskim |
| pubmed-article:19633189 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:19633189 | lifeskim:mentions | umls-concept:C1312042 | lld:lifeskim |
| pubmed-article:19633189 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:19633189 | lifeskim:mentions | umls-concept:C1947912 | lld:lifeskim |
| pubmed-article:19633189 | pubmed:issue | 31 | lld:pubmed |
| pubmed-article:19633189 | pubmed:dateCreated | 2009-8-11 | lld:pubmed |
| pubmed-article:19633189 | pubmed:abstractText | Skeletal muscle basal lamina is linked to the sarcolemma through transmembrane receptors, including integrins and dystroglycan. The function of dystroglycan relies critically on posttranslational glycosylation, a common target shared by a genetically heterogeneous group of muscular dystrophies characterized by alpha-dystroglycan hypoglycosylation. Here we show that both dystroglycan and integrin alpha7 contribute to force-production of muscles, but that only disruption of dystroglycan causes detachment of the basal lamina from the sarcolemma and renders muscle prone to contraction-induced injury. These phenotypes of dystroglycan-null muscles are recapitulated by Large(myd) muscles, which have an intact dystrophin-glycoprotein complex and lack only the laminin globular domain-binding motif on alpha-dystroglycan. Compromised sarcolemmal integrity is directly shown in Large(myd) muscles and similarly in normal muscles when arenaviruses compete with matrix proteins for binding alpha-dystroglycan. These data provide direct mechanistic insight into how the dystroglycan-linked basal lamina contributes to the maintenance of sarcolemmal integrity and protects muscles from damage. | lld:pubmed |
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| pubmed-article:19633189 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19633189 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19633189 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19633189 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19633189 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19633189 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:19633189 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:MayerUlrikeU | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:McNeilPaul... | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:MooreSteven... | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:CampbellKevin... | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:IannacconeSus... | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:MuirheadDavid... | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:OldstoneMicha... | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:KunzStefanS | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:MicheleDaniel... | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:KanagawaMotoi... | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:FaulknerJohn... | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:HanRenzhiR | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:MiyakeKatsuya... | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:Yoshida-Morig... | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:RaderErik PEP | lld:pubmed |
| pubmed-article:19633189 | pubmed:author | pubmed-author:NgRainer ARA | lld:pubmed |
| pubmed-article:19633189 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19633189 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:19633189 | pubmed:volume | 106 | lld:pubmed |
| pubmed-article:19633189 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19633189 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19633189 | pubmed:pagination | 12573-9 | lld:pubmed |
| pubmed-article:19633189 | pubmed:dateRevised | 2010-5-20 | lld:pubmed |
| pubmed-article:19633189 | pubmed:meshHeading | pubmed-meshheading:19633189... | lld:pubmed |
| pubmed-article:19633189 | pubmed:meshHeading | pubmed-meshheading:19633189... | lld:pubmed |
| pubmed-article:19633189 | pubmed:meshHeading | pubmed-meshheading:19633189... | lld:pubmed |
| pubmed-article:19633189 | pubmed:meshHeading | pubmed-meshheading:19633189... | lld:pubmed |
| pubmed-article:19633189 | pubmed:meshHeading | pubmed-meshheading:19633189... | lld:pubmed |
| pubmed-article:19633189 | pubmed:meshHeading | pubmed-meshheading:19633189... | lld:pubmed |
| pubmed-article:19633189 | pubmed:meshHeading | pubmed-meshheading:19633189... | lld:pubmed |
| pubmed-article:19633189 | pubmed:meshHeading | pubmed-meshheading:19633189... | lld:pubmed |
| pubmed-article:19633189 | pubmed:meshHeading | pubmed-meshheading:19633189... | lld:pubmed |
| pubmed-article:19633189 | pubmed:meshHeading | pubmed-meshheading:19633189... | lld:pubmed |
| pubmed-article:19633189 | pubmed:meshHeading | pubmed-meshheading:19633189... | lld:pubmed |
| pubmed-article:19633189 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19633189 | pubmed:articleTitle | Basal lamina strengthens cell membrane integrity via the laminin G domain-binding motif of alpha-dystroglycan. | lld:pubmed |
| pubmed-article:19633189 | pubmed:affiliation | Howard Hughes Medical Institute, Department of Molecular Physiology, The University of Iowa, Iowa City, IA 52242, USA. | lld:pubmed |
