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Integrin alpha 8 beta 1 promotes attachment, cell spreading, and neurite outgrowth on fibronectin

Academic Article
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Overview

authors

  • Mueller, Ulrich
  • Bossy, B.
  • Venstrom, K.
  • Reichardt, L. F.

publication date

  • April 1995

journal

  • Molecular Biology of the Cell  Journal

abstract

  • The integrin alpha 8 subunit, isolated by low stringency hybridization, is a novel integrin subunit that associates with beta 1. To identify ligands, we have prepared a function-blocking antiserum to the extracellular domain of alpha 8, and we have established by transfection K562 cell lines that stably express alpha 8 beta 1 heterodimers on the cell surface. We demonstrate here by cell adhesion and neurite outgrowth assays that alpha 8 beta 1 is a fibronectin receptor. Studies on fibronectin fragments using RGD peptides as inhibitors show that alpha 8 beta 1 binds to the RGD site of fibronectin. In contrast to the endogenous alpha 5 beta 1 fibronectin receptor in K562 cells, alpha 8 beta 1 not only promotes cell attachment but also extensive cell spreading, suggesting functional differences between the two receptors. In chick embryo fibroblasts, alpha 8 beta 1 is localized to focal adhesions. We conclude that alpha 8 beta 1 is a receptor for fibronectin and can promote attachment, cell spreading, and neurite outgrowth on fibronectin.

subject areas

  • Amino Acid Sequence
  • Animals
  • Antibodies
  • Antibody Specificity
  • Cell Adhesion
  • Cell Differentiation
  • Chick Embryo
  • Fibronectins
  • Humans
  • Integrins
  • Ligands
  • Neurites
  • Oligopeptides
  • Receptors, Fibronectin
  • Receptors, Immunologic
  • Tumor Cells, Cultured
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Identity

PubMed Central ID

  • PMC301202

International Standard Serial Number (ISSN)

  • 1059-1524

PubMed ID

  • 7626807
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Additional Document Info

start page

  • 433

end page

  • 448

volume

  • 6

issue

  • 4

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