{"PubmedArticle":{"MedlineCitation":{"@attributes":{"Status":"MEDLINE","Owner":"NLM","IndexingMethod":"Manual"},"PMID":{"@attributes":{"Version":"1"},"@text":"8349731"},"DateCompleted":{"Year":"1993","Month":"09","Day":"16"},"DateRevised":{"Year":"2022","Month":"04","Day":"08"},"Article":{"@attributes":{"PubModel":"Print"},"Journal":{"ISSN":{"@attributes":{"IssnType":"Print"},"@text":"0021-9525"},"JournalIssue":{"@attributes":{"CitedMedium":"Print"},"Volume":"122","Issue":"4","PubDate":{"Year":"1993","Month":"Aug"}},"Title":"The Journal of cell biology","ISOAbbreviation":"J Cell Biol"},"ArticleTitle":"A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin.","Pagination":{"StartPage":"809","EndPage":"823","MedlinePgn":"809-23"},"Abstract":{"AbstractText":["The dystrophin-glycoprotein complex was tested for interaction with several components of the extracellular matrix as well as actin. The 156-kD dystrophin-associated glycoprotein (156-kD dystroglycan) specifically bound laminin in a calcium-dependent manner and was inhibited by NaCl (IC50 = 250 mM) but was not affected by 1,000-fold (wt\/wt) excesses of lactose, IKVAV, or YIGSR peptides. Laminin binding was inhibited by heparin (IC50 = 100 micrograms\/ml), suggesting that one of the heparin-binding domains of laminin is involved in binding dystroglycan while negatively charged oligosaccharide moieties on dystroglycan were found to be necessary for its laminin-binding activity. No interaction between any component of the dystrophin-glycoprotein complex and fibronectin, collagen I, collagen IV, entactin, or heparan sulfate proteoglycan was detected by 125I-protein overlay and\/or extracellular matrix protein-Sepharose precipitation. In addition, laminin-Sepharose quantitatively precipitated purified dystrophin-glycoprotein complex, demonstrating that the laminin-binding site is accessible when dystroglycan is associated with the complex. Dystroglycan of nonmuscle tissues also bound laminin. However, the other proteins of the striated muscle dystrophin-glycoprotein complex appear to be absent, antigenically dissimilar or less tightly associated with dystroglycan in nonmuscle tissues. Finally, we show that the dystrophin-glycoprotein complex cosediments with F-actin but does not bind calcium or calmodulin. Our results support a role for the striated muscle dystrophin-glycoprotein complex in linking the actin-based cytoskeleton with the extracellular matrix. Furthermore, our results suggest that dystrophin and dystroglycan may play substantially different functional roles in nonmuscle tissues."]},"AuthorList":{"@attributes":{"CompleteYN":"Y"},"Author":[{"@attributes":{"ValidYN":"Y"},"LastName":"Ervasti","ForeName":"J M","Initials":"JM","AffiliationInfo":[{"Affiliation":"Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City 52242."}]},{"@attributes":{"ValidYN":"Y"},"LastName":"Campbell","ForeName":"K P","Initials":"KP"}]},"Language":["eng"],"PublicationTypeList":{"PublicationType":[{"@attributes":{"UI":"D016428"},"@text":"Journal Article"},{"@attributes":{"UI":"D013485"},"@text":"Research Support, Non-U.S. Gov't"}]}},"MedlineJournalInfo":{"Country":"United States","MedlineTA":"J Cell Biol","NlmUniqueID":"0375356","ISSNLinking":"0021-9525"},"ChemicalList":{"Chemical":[{"RegistryNumber":"0","NameOfSubstance":{"@attributes":{"UI":"D000199"},"@text":"Actins"}},{"RegistryNumber":"0","NameOfSubstance":{"@attributes":{"UI":"D000911"},"@text":"Antibodies, Monoclonal"}},{"RegistryNumber":"0","NameOfSubstance":{"@attributes":{"UI":"D002147"},"@text":"Calmodulin"}},{"RegistryNumber":"0","NameOfSubstance":{"@attributes":{"UI":"D003598"},"@text":"Cytoskeletal Proteins"}},{"RegistryNumber":"0","NameOfSubstance":{"@attributes":{"UI":"D016189"},"@text":"Dystrophin"}},{"RegistryNumber":"0","NameOfSubstance":{"@attributes":{"UI":"D006023"},"@text":"Glycoproteins"}},{"RegistryNumber":"0","NameOfSubstance":{"@attributes":{"UI":"D007797"},"@text":"Laminin"}},{"RegistryNumber":"0","NameOfSubstance":{"@attributes":{"UI":"D046911"},"@text":"Macromolecular Substances"}},{"RegistryNumber":"0","NameOfSubstance":{"@attributes":{"UI":"D008562"},"@text":"Membrane 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