Expression and characterisation of a very-late antigen-4 (alpha 4 beta 1) integrin-binding fragment of vascular cell-adhesion molecule-1

Eur J Biochem. 1994 Dec 1;226(2):517-23. doi: 10.1111/j.1432-1033.1994.tb20076.x.

Abstract

We have used an Escherichia coli expression system to produce forms of vascular cell-adhesion molecule-1 (VCAM-1) containing the first two and three supposed immunoglobulin-like domains. A form consisting of the first two domains of VCAM-1 is shown to promote very-late antigen-4-dependent spreading of a melanoma cell line comparable to that found for the equivalent region in the full seven-domain form. Preliminary structural analysis by CD and NMR is consistent with an immunoglobulin fold which is predicted from sequence comparison studies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Cell Adhesion
  • Cell Adhesion Molecules / chemistry*
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / pharmacology
  • Circular Dichroism
  • Escherichia coli / genetics
  • Gene Expression*
  • Humans
  • Integrin alpha4beta1
  • Integrins / metabolism*
  • Magnetic Resonance Spectroscopy
  • Melanoma / pathology
  • Peptide Fragments / chemistry*
  • Peptide Fragments / genetics
  • Peptide Fragments / pharmacology
  • Protein Structure, Secondary
  • Receptors, Very Late Antigen / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / pharmacology
  • Structure-Activity Relationship
  • Tumor Cells, Cultured
  • Vascular Cell Adhesion Molecule-1

Substances

  • Cell Adhesion Molecules
  • Integrin alpha4beta1
  • Integrins
  • Peptide Fragments
  • Receptors, Very Late Antigen
  • Recombinant Proteins
  • Vascular Cell Adhesion Molecule-1