Defining extracellular integrin alpha-chain sites that affect cell adhesion and adhesion strengthening without altering soluble ligand binding

Mol Biol Cell. 1997 Dec;8(12):2647-57. doi: 10.1091/mbc.8.12.2647.

Abstract

It was previously shown that mutations of integrin alpha4 chain sites, within putative EF-hand-type divalent cation-binding domains, each caused a marked reduction in alpha4beta1-dependent cell adhesion. Some reports have suggested that alpha-chain "EF-hand" sites may interact directly with ligands. However, we show here that mutations of three different alpha4 "EF-hand" sites each had no effect on binding of soluble monovalent or bivalent vascular cell adhesion molecule 1 whether measured indirectly or directly. Furthermore, these mutations had minimal effect on alpha4beta1-dependent cell tethering to vascular cell adhesion molecule 1 under shear. However, EF-hand mutants did show severe impairments in cellular resistance to detachment under shear flow. Thus, mutation of integrin alpha4 "EF-hand-like" sites may impair 1) static cell adhesion and 2) adhesion strengthening under shear flow by a mechanism that does not involve alterations of initial ligand binding.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution / genetics
  • Antigens, CD / chemistry*
  • Antigens, CD / genetics
  • Antigens, CD / metabolism*
  • Binding Sites
  • Cations, Divalent / metabolism
  • Cations, Divalent / pharmacology
  • Cell Adhesion / drug effects
  • EF Hand Motifs
  • Fibronectins / chemistry
  • Fibronectins / metabolism
  • Humans
  • Immunoglobulin G / metabolism
  • Integrin alpha4
  • Integrin alpha4beta1
  • Integrins / chemistry
  • Integrins / genetics
  • Integrins / metabolism
  • K562 Cells
  • Ligands
  • Manganese / metabolism
  • Manganese / pharmacology
  • Mutation / genetics
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Protein Binding / drug effects
  • Receptors, Lymphocyte Homing / chemistry
  • Receptors, Lymphocyte Homing / genetics
  • Receptors, Lymphocyte Homing / metabolism
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism
  • Solubility
  • Transfection
  • Vascular Cell Adhesion Molecule-1 / chemistry
  • Vascular Cell Adhesion Molecule-1 / metabolism

Substances

  • Antigens, CD
  • Cations, Divalent
  • Fibronectins
  • Immunoglobulin G
  • Integrin alpha4beta1
  • Integrins
  • Ligands
  • Peptide Fragments
  • Receptors, Lymphocyte Homing
  • Recombinant Fusion Proteins
  • Vascular Cell Adhesion Molecule-1
  • Integrin alpha4
  • Manganese