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- W2031036359 abstract "Laminins are a group of extracellular-matrix proteins important in development and disease. They are heterotrimers, and specific domains in the different chains have specialized functions. The G domain of the alpha5 chain has now been produced in transfected mammalian cells as single modules and two tandem arrays, alpha5LG1-3 and alpha5LG4-5 (LG is laminin G domain-like). Using these fragments we produced specific polyclonal antibodies functional in immunoblotting and immunofluorescence studies and in solid-phase assays. Both alpha5LG tandem arrays had physiologically relevant affinities for sulphated ligands such as heparin and sulphatides. Cells adhered to these fragments and acquired a spread morphology when plated on alpha5LG1-3. Binding of integrins alpha3beta1 and alpha6beta1 was localized to the alpha5LG1-3 modules, and alpha-dystroglycan binding was localized to the alpha5LG4-5 modules, thus locating these activities to different LG modules within the laminin alpha5 G domain. However, both these activities were of relatively low affinity, indicating that integrin-mediated cell adhesion to the laminin 10/11 alpha5G domain depends on contributions from the other chains of the heterotrimer and that high-affinity alpha-dystroglycan binding could be dependent on specific Ca(2+)-ion-co-ordinating amino acids absent from alpha5LG4-5." @default.
- W2031036359 created "2016-06-24" @default.
- W2031036359 creator A5006485581 @default.
- W2031036359 creator A5036288146 @default.
- W2031036359 date "2003-04-15" @default.
- W2031036359 modified "2023-10-16" @default.
- W2031036359 title "beta1 Integrin and alpha-dystroglycan binding sites are localized to different laminin-G-domain-like (LG) modules within the laminin alpha5 chain G domain" @default.
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- W2031036359 doi "https://doi.org/10.1042/bj20021500" @default.
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