Journal article
Laminin isoforms differentially regulate adhesion, spreading, proliferation, and ERK activation of β1 integrin-null cells
Experimental cell research, Vol.300(1), pp.94-108
2004
DOI: 10.1016/j.yexcr.2004.06.031
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.
Details
- Title: Subtitle
- Laminin isoforms differentially regulate adhesion, spreading, proliferation, and ERK activation of β1 integrin-null cells
- Creators
- Yamato Kikkawa - Section for Cell and Developmental Biology, Department of Cell and Molecular Biology, Lund University, SE-22184 Lund, SwedenHao Yu - Section for Cell and Developmental Biology, Department of Cell and Molecular Biology, Lund University, SE-22184 Lund, SwedenElke Genersch - Section for Cell and Developmental Biology, Department of Cell and Molecular Biology, Lund University, SE-22184 Lund, SwedenNoriko Sanzen - Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, JapanKiyotoshi Sekiguchi - Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, JapanReinhard Fässler - Max-Planck-Institute for Biochemistry, Martinsried, GermanyKevin P Campbell - Howard Hughes Medical Institute, Department of Physiology and Biophysics, Department of Neurology, University of Iowa College of Medicine, Iowa City, IA 52242, USAJan F Talts - Section for Cell and Developmental Biology, Department of Cell and Molecular Biology, Lund University, SE-22184 Lund, SwedenPeter Ekblom - Section for Cell and Developmental Biology, Department of Cell and Molecular Biology, Lund University, SE-22184 Lund, Sweden
- Resource Type
- Journal article
- Publication Details
- Experimental cell research, Vol.300(1), pp.94-108
- Publisher
- Elsevier Inc
- DOI
- 10.1016/j.yexcr.2004.06.031
- ISSN
- 0014-4827
- eISSN
- 1090-2422
- Language
- English
- Date published
- 2004
- Academic Unit
- Molecular Physiology and Biophysics; Neurology; Iowa Neuroscience Institute
- Record Identifier
- 9984020888502771
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