Multiple ligand binding functions for VLA-2 (alpha 2 beta 1) and VLA-3 (alpha 3 beta 1) in the integrin family

Cell Differ Dev. 1990 Dec 2;32(3):229-38. doi: 10.1016/0922-3371(90)90035-u.

Abstract

In our studies of VLA-3 we have shown (i) that a single integrin (VLA-3) can bind to multiple ligands by different mechanisms, involving RGD and non-RGD sites, which are regulated differently by divalent cations. Also we showed from the primary sequence of VLA-3 that it is only distantly related to the other cleaved alpha subunits. In our studies of VLA-2 we have shown that a single integrin may have at least three functional forms, depending on the cell type where expressed. In addition, we have expressed functional VLA-2 in RD cells, resulting in both Coll and Lm binding functions in vitro, and increased tumor cell metastasis in vivo in nude mice.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding, Competitive
  • Cations, Divalent / metabolism
  • Cell Adhesion
  • Collagen / metabolism*
  • Fibronectins / metabolism*
  • Humans
  • Laminin / metabolism*
  • Ligands
  • Mice
  • Mice, Nude
  • Molecular Sequence Data
  • Neoplasm Proteins / metabolism
  • Oligopeptides / metabolism
  • Protein Conformation
  • Receptors, Cell Surface / metabolism*
  • Receptors, Collagen
  • Receptors, Fibronectin
  • Receptors, Immunologic / metabolism*
  • Receptors, Laminin
  • Receptors, Peptide*
  • Receptors, Very Late Antigen / metabolism*
  • Recombinant Proteins / metabolism
  • Tumor Cells, Cultured / metabolism

Substances

  • Cations, Divalent
  • Fibronectins
  • Laminin
  • Ligands
  • Neoplasm Proteins
  • Oligopeptides
  • Receptors, Cell Surface
  • Receptors, Collagen
  • Receptors, Fibronectin
  • Receptors, Immunologic
  • Receptors, Laminin
  • Receptors, Peptide
  • Receptors, Very Late Antigen
  • Recombinant Proteins
  • arginyl-glycyl-aspartic acid directed cell adhesion receptor
  • arginyl-glycyl-aspartic acid
  • Collagen
  • glycyl-arginyl-glycyl-aspartyl-seryl-proline
  • glycyl-arginyl-glycyl-glutamyl-seryl-proline