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beta 1 Integrin and alpha-dystroglycan binding sites are localized to different laminin-G-domain-like (LG) modules within the laminin alpha 5 chain G domain

Yu, Hao LU and Talts, Jan LU (2003) In Biochemical Journal 371. p.289-299
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 a5LG1-3. Binding... (More)
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 a5LG1-3. Binding of integrins alpha3beta1 and alpha6beta1 was localized to the alpha5LG1-3 modules, and a-dystroglycan binding was localized to the a5LG4-5 modules, thus locating these activities to different LG modules within the laminin a5 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 a-dystroglycan binding could be dependent on specific Ca2+-ion-co-ordinating amino acids absent from alpha5LG4-5. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
recombinant protein, receptor, protein module, basement membrane, cell-matrix interaction
in
Biochemical Journal
volume
371
pages
289 - 299
publisher
Portland Press Limited
external identifiers
  • pmid:12519075
  • wos:000182437200006
  • scopus:0038414615
ISSN
0264-6021
DOI
10.1042/BJ20021500
language
English
LU publication?
yes
id
01287a31-33fa-49ab-b3ce-53933a3f6bf1 (old id 312838)
date added to LUP
2007-09-24 13:47:36
date last changed
2018-01-07 08:42:09
@article{01287a31-33fa-49ab-b3ce-53933a3f6bf1,
  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 a5LG1-3. Binding of integrins alpha3beta1 and alpha6beta1 was localized to the alpha5LG1-3 modules, and a-dystroglycan binding was localized to the a5LG4-5 modules, thus locating these activities to different LG modules within the laminin a5 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 a-dystroglycan binding could be dependent on specific Ca2+-ion-co-ordinating amino acids absent from alpha5LG4-5.},
  author       = {Yu, Hao and Talts, Jan},
  issn         = {0264-6021},
  keyword      = {recombinant protein,receptor,protein module,basement membrane,cell-matrix interaction},
  language     = {eng},
  pages        = {289--299},
  publisher    = {Portland Press Limited},
  series       = {Biochemical Journal},
  title        = {beta 1 Integrin and alpha-dystroglycan binding sites are localized to different laminin-G-domain-like (LG) modules within the laminin alpha 5 chain G domain},
  url          = {http://dx.doi.org/10.1042/BJ20021500},
  volume       = {371},
  year         = {2003},
}