Domain IVa of laminin alpha5 chain is cell-adhesive and binds beta1 and alphaVbeta3 integrins through Arg-Gly-Asp

FEBS Lett. 2001 Dec 7;509(2):181-5. doi: 10.1016/s0014-5793(01)03167-2.


The globular domain IVa from the short arm region of mouse laminin alpha5 chain was obtained by recombinant production and shown to be a cell-adhesive substrate and to bind alphaVbeta3 integrin in solid-phase assays. These interactions were blocked by RGD peptides and a restricted panel of anti-integrin antibodies. The two RGD sequences present in alpha5IVa were shown by site-directed mutagenesis to make different contributions to cell adhesion but were equivalent in binding alphaVbeta3 integrin. A quantitative radioimmuno-inhibition assay was established based on domain alpha5IVa which demonstrated distinct amounts of alpha5 chain in various tissues, particularly in vessel walls. There it could play a role in angiogenesis steps requiring RGD-dependent integrins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Cell Adhesion
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / isolation & purification
  • Cell Adhesion Molecules / metabolism*
  • Humans
  • Integrin beta1 / metabolism*
  • Kidney / cytology
  • Laminin / genetics
  • Laminin / isolation & purification
  • Laminin / metabolism*
  • Melanoma, Experimental
  • Mice
  • Muscle, Skeletal / cytology
  • Oligopeptides / metabolism*
  • Peptide Fragments / genetics
  • Peptide Fragments / isolation & purification
  • Peptide Fragments / metabolism
  • Protein Structure, Tertiary
  • Receptors, Vitronectin / metabolism*
  • Recombinant Proteins / metabolism


  • Cell Adhesion Molecules
  • Integrin beta1
  • Laminin
  • Oligopeptides
  • Peptide Fragments
  • Receptors, Vitronectin
  • Recombinant Proteins
  • laminin alpha5
  • arginyl-glycyl-aspartic acid