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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
31
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pubmed:dateCreated |
2009-8-11
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-10022829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-10199978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-10616209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-10678176,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-10714587,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-11381262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-11604425,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-11964072,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-12076680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-12140558,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-12230980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-12556453,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-12556454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-12556455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-12736685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-12757935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-15184894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-15473841,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-15928713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-15944456,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-16098969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-16293150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-16971897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-1741056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-17452335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-17488283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-17607357,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-17662592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-19019316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-3253447,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-8205617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-8349731,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-8851045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-9175728,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-9354797,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-9415431,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-9590299,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-9851927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19633189-9851928
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1091-6490
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pubmed:author |
pubmed-author:CampbellKevin PKP,
pubmed-author:FaulknerJohn AJA,
pubmed-author:HanRenzhiR,
pubmed-author:IannacconeSusan TST,
pubmed-author:KanagawaMotoiM,
pubmed-author:KunzStefanS,
pubmed-author:MayerUlrikeU,
pubmed-author:McNeilPaul LPL,
pubmed-author:MicheleDaniel EDE,
pubmed-author:MiyakeKatsuyaK,
pubmed-author:MooreSteven ASA,
pubmed-author:MuirheadDavid EDE,
pubmed-author:NgRainer ARA,
pubmed-author:OldstoneMichael B AMB,
pubmed-author:RaderErik PEP,
pubmed-author:Yoshida-MoriguchiTakakoT
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pubmed:issnType |
Electronic
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pubmed:day |
4
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pubmed:volume |
106
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12573-9
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pubmed:dateRevised |
2010-5-20
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pubmed:meshHeading |
pubmed-meshheading:19633189-Animals,
pubmed-meshheading:19633189-Basement Membrane,
pubmed-meshheading:19633189-Binding Sites,
pubmed-meshheading:19633189-Dystroglycans,
pubmed-meshheading:19633189-Glycosylation,
pubmed-meshheading:19633189-Integrins,
pubmed-meshheading:19633189-Laminin,
pubmed-meshheading:19633189-Lymphocytic choriomeningitis virus,
pubmed-meshheading:19633189-Mice,
pubmed-meshheading:19633189-Muscular Dystrophy, Animal,
pubmed-meshheading:19633189-Sarcolemma
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pubmed:year |
2009
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pubmed:articleTitle |
Basal lamina strengthens cell membrane integrity via the laminin G domain-binding motif of alpha-dystroglycan.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Molecular Physiology, The University of Iowa, Iowa City, IA 52242, USA.
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