{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T15:03:38Z","timestamp":1791212618879,"version":"4.1.0"},"reference-count":41,"publisher":"National Academy of Sciences","issue":"31","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2009,8,4]]},"abstract":"<jats:p>\n                    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 \u03b1-dystroglycan hypoglycosylation. Here we show that both dystroglycan and integrin \u03b17 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\n                    <jats:italic>\n                      Large\n                      <jats:sup>myd<\/jats:sup>\n                    <\/jats:italic>\n                    muscles, which have an intact dystrophin\u2013glycoprotein complex and lack only the laminin globular domain-binding motif on \u03b1-dystroglycan. Compromised sarcolemmal integrity is directly shown in\n                    <jats:italic>\n                      Large\n                      <jats:sup>myd<\/jats:sup>\n                    <\/jats:italic>\n                    muscles and similarly in normal muscles when arenaviruses compete with matrix proteins for binding \u03b1-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.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0906545106","type":"journal-article","created":{"date-parts":[[2009,7,24]],"date-time":"2009-07-24T21:39:06Z","timestamp":1248471546000},"page":"12573-12579","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":146,"title":["Basal lamina strengthens cell membrane integrity via the laminin G domain-binding motif of \u03b1-dystroglycan"],"prefix":"10.1073","volume":"106","author":[{"given":"Renzhi","family":"Han","sequence":"first","affiliation":[{"name":"Howard Hughes Medical Institute, Departments of Molecular Physiology and Biophysics, Neurology, Internal Medicine, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Motoi","family":"Kanagawa","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Departments of Molecular Physiology and Biophysics, Neurology, Internal Medicine, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takako","family":"Yoshida-Moriguchi","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Departments of Molecular Physiology and Biophysics, Neurology, Internal Medicine, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erik P.","family":"Rader","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Departments of Molecular Physiology and Biophysics, Neurology, Internal Medicine, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rainer A.","family":"Ng","sequence":"additional","affiliation":[{"name":"Departments of bMolecular and Integrative Physiology and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel E.","family":"Michele","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Departments of Molecular Physiology and Biophysics, Neurology, Internal Medicine, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David E.","family":"Muirhead","sequence":"additional","affiliation":[{"name":"Texas Scottish Rite Hospital for Children, Dallas, TX 75219;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefan","family":"Kunz","sequence":"additional","affiliation":[{"name":"Departments of dNeuropharmacology and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven A.","family":"Moore","sequence":"additional","affiliation":[{"name":"Pathology, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, Iowa City, IA 52242;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susan T.","family":"Iannaccone","sequence":"additional","affiliation":[{"name":"Department of Pediatric Neurology, Children's Medical Center, University of Texas Southwestern Medical Center, Dallas, TX 75390;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katsuya","family":"Miyake","sequence":"additional","affiliation":[{"name":"Institute of Molecular Medicine and Genetics, The Medical College of Georgia, Augusta, GA 30912; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul L.","family":"McNeil","sequence":"additional","affiliation":[{"name":"Department of Cellular Biology and Anatomy,"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulrike","family":"Mayer","sequence":"additional","affiliation":[{"name":"Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester M13 9PT, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael B. A.","family":"Oldstone","sequence":"additional","affiliation":[{"name":"Departments of dNeuropharmacology and"},{"name":"Infectiology, The Scripps Research Institute, La Jolla, CA 92037;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John A.","family":"Faulkner","sequence":"additional","affiliation":[{"name":"Departments of bMolecular and Integrative Physiology and"},{"name":"Biomedical Engineering, University of Michigan, Ann Arbor, MI 48109-0622;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kevin P.","family":"Campbell","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Departments of Molecular Physiology and Biophysics, Neurology, Internal Medicine, and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2009,8,4]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrm2024"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0959-437X(02)00309-X"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1177\/095952875203500108"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.R200027200"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1742-4658.2007.05823.x"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1600-0838.2005.00467.x"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1002\/bies.950180208"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.cellbio.20.010403.094555"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/355696a0"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1007\/s004410051279"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/18.4.863"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(94)90052-3"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.R200031200"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature00837"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1038\/nm1059"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.282.5396.2079"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.282.5396.2076"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1093\/hmg\/6.6.831"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.R200022200"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1038\/ng1197-318"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.1038\/ng0598-94"},{"key":"e_1_3_3_22_2","doi-asserted-by":"publisher","DOI":"10.1113\/jphysiol.1988.sp017279"},{"key":"e_1_3_3_23_2","doi-asserted-by":"publisher","DOI":"10.1023\/A:1014587918367"},{"key":"e_1_3_3_24_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-8966(99)00077-2"},{"key":"e_1_3_3_25_2","doi-asserted-by":"publisher","DOI":"10.1038\/88865"},{"key":"e_1_3_3_26_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.febslet.2005.07.059"},{"key":"e_1_3_3_27_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1097-2765(00)80410-4"},{"key":"e_1_3_3_28_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.C700061200"},{"key":"e_1_3_3_29_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0925-4439(03)00040-1"},{"key":"e_1_3_3_30_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(02)00907-8"},{"key":"e_1_3_3_31_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature01573"},{"key":"e_1_3_3_32_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ceb.2007.07.001"},{"key":"e_1_3_3_33_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI30848"},{"key":"e_1_3_3_34_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.200104103"},{"key":"e_1_3_3_35_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrm1665"},{"key":"e_1_3_3_36_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.nurt.2008.08.005"},{"key":"e_1_3_3_37_2","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.69.2.262-291.2005"},{"key":"e_1_3_3_38_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.122.4.809"},{"key":"e_1_3_3_39_2","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-0177(199712)210:4<472::AID-AJA10>3.0.CO;2-9"},{"key":"e_1_3_3_40_2","first-page":"1591","article-title":"Organization of the myotendinous junction is dependent on the presence of alpha7beta1 integrin","volume":"79","author":"Miosge N","year":"1999","unstructured":"N Miosge, C Klenczar, R Herken, M Willem, U Mayer, Organization of the myotendinous junction is dependent on the presence of alpha7beta1 integrin. 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