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

Research output: Contribution to journalArticle

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

Authors
  • Yamato Kikkawa
  • Hao Yu
  • Elke Genersch
  • Noriko Sanzen
  • Kiyotoshi Sekiguchi
  • Reinhard Fässler
  • Kevin P Campbell
  • Jan Talts
  • Peter Ekblom
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Basic Medicine

Keywords

  • Laminin, Integrin, Dystroglycan, Extracellular signal-regulated kinase
Original languageEnglish
Pages (from-to)94-108
JournalExperimental Cell Research
Volume300
Issue number1
Publication statusPublished - 2004
Publication categoryResearch
Peer-reviewedYes