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Laminin isoforms differentially regulate adhesion, spreading, proliferation, and ERK activation of beta1 integrin-null cells.

Kikkawa, Yamato; Yu, Hao LU ; Genersch, Elke; Sanzen, Noriko; Sekiguchi, Kiyotoshi; Fässler, Reinhard; Campbell, Kevin P; Talts, Jan LU and Ekblom, Peter LU (2004) In Experimental Cell Research 300(1). p.94-108
Abstract
The presence of many laminin receptors of the β1 integrin family on most cells makes it difficult to define the biological functions of other major laminin receptors such as integrin α6β4 and dystroglycan. We therefore tested the binding of a β1 integrin-null cell line GD25 to four different laminin variants. The cells were shown to produce dystroglycan, which based on affinity chromatography bound to laminin-1, -2/4, and -10/11, but not to laminin-5. The cells also expressed the integrin α6Aβ4A variant. GD25 β1 integrin-null cells are known to bind poorly to laminin-1, but we demonstrate here that these cells bind avidly to laminin-2/4, -5, and -10/11. The initial binding at 20 min to each of these laminins could be inhibited by an... (More)
The presence of many laminin receptors of the β1 integrin family on most cells makes it difficult to define the biological functions of other major laminin receptors such as integrin α6β4 and dystroglycan. We therefore tested the binding of a β1 integrin-null cell line GD25 to four different laminin variants. The cells were shown to produce dystroglycan, which based on affinity chromatography bound to laminin-1, -2/4, and -10/11, but not to laminin-5. The cells also expressed the integrin α6Aβ4A variant. GD25 β1 integrin-null cells are known to bind poorly to laminin-1, but we demonstrate here that these cells bind avidly to laminin-2/4, -5, and -10/11. The initial binding at 20 min to each of these laminins could be inhibited by an integrin α6 antibody, but not by a dystroglycan antibody. Hence, integrin α6Aβ4A of GD25 cells was identified as a major receptor for initial GD25 cell adhesion to three out of four tested laminin isoforms. Remarkably, cell adhesion to laminin-5 failed to promote cell spreading, proliferation, and extracellular signal-regulated kinase (ERK) activation, whereas all these responses occurred in response to adhesion to laminin-2/4 or -10/11. The data establish GD25 cells as useful tools to define the role integrin α6Aβ4A and suggest that laminin isoforms have distinctly different capacities to promote cell adhesion and signaling via integrin α6Aβ4A. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Laminin, Integrin, Dystroglycan, Extracellular signal-regulated kinase
in
Experimental Cell Research
volume
300
issue
1
pages
94 - 108
publisher
Academic Press
external identifiers
  • pmid:15383318
  • wos:000224228200010
  • scopus:4644240551
ISSN
1090-2422
DOI
10.1016/j.yexcr.2004.06.031
language
English
LU publication?
yes
id
fbff011c-7a17-4a61-b144-4621cb303cc7 (old id 127243)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=15383318&dopt=Abstract
date added to LUP
2007-07-16 12:27:11
date last changed
2017-03-12 03:32:52
@article{fbff011c-7a17-4a61-b144-4621cb303cc7,
  abstract     = {The presence of many laminin receptors of the β1 integrin family on most cells makes it difficult to define the biological functions of other major laminin receptors such as integrin α6β4 and dystroglycan. We therefore tested the binding of a β1 integrin-null cell line GD25 to four different laminin variants. The cells were shown to produce dystroglycan, which based on affinity chromatography bound to laminin-1, -2/4, and -10/11, but not to laminin-5. The cells also expressed the integrin α6Aβ4A variant. GD25 β1 integrin-null cells are known to bind poorly to laminin-1, but we demonstrate here that these cells bind avidly to laminin-2/4, -5, and -10/11. The initial binding at 20 min to each of these laminins could be inhibited by an integrin α6 antibody, but not by a dystroglycan antibody. Hence, integrin α6Aβ4A of GD25 cells was identified as a major receptor for initial GD25 cell adhesion to three out of four tested laminin isoforms. Remarkably, cell adhesion to laminin-5 failed to promote cell spreading, proliferation, and extracellular signal-regulated kinase (ERK) activation, whereas all these responses occurred in response to adhesion to laminin-2/4 or -10/11. The data establish GD25 cells as useful tools to define the role integrin α6Aβ4A and suggest that laminin isoforms have distinctly different capacities to promote cell adhesion and signaling via integrin α6Aβ4A.},
  author       = {Kikkawa, Yamato and Yu, Hao and Genersch, Elke and Sanzen, Noriko and Sekiguchi, Kiyotoshi and Fässler, Reinhard and Campbell, Kevin P and Talts, Jan and Ekblom, Peter},
  issn         = {1090-2422},
  keyword      = {Laminin,Integrin,Dystroglycan,Extracellular signal-regulated kinase},
  language     = {eng},
  number       = {1},
  pages        = {94--108},
  publisher    = {Academic Press},
  series       = {Experimental Cell Research},
  title        = {Laminin isoforms differentially regulate adhesion, spreading, proliferation, and ERK activation of beta1 integrin-null cells.},
  url          = {http://dx.doi.org/10.1016/j.yexcr.2004.06.031},
  volume       = {300},
  year         = {2004},
}