VLA-4 (alpha(4)beta(1)) engagement defines a novel activation pathway for beta(2) integrin-dependent leukocyte adhesion involving the urokinase receptor

Blood. 2000 Jul 15;96(2):506-13.

Abstract

During acute inflammatory processes, beta(2) and beta(1) integrins sequentially mediate leukocyte recruitment into extravascular tissues. We studied the influence of VLA-4 (very late antigen-4) (alpha(4)beta(1)) engagement on beta(2) integrin activation-dependent cell-to-cell adhesion. Ligation of VLA-4 by the soluble chimera fusion product vascular cell adhesion molecule-1 (VCAM-1)-Fc or by 2 anti-CD29 (beta(1) chain) monoclonal antibodies (mAb) rapidly induced adhesion of myelomonocytic cells (HL60, U937) to human umbilical vein endothelial cells (HUVECs). Cell adhesion was mediated via beta(2) integrin (LFA-1 and Mac-1) activation: induced adhesion to HUVECs was inhibited by blocking mAbs anti-CD18 (70%-90%), anti-CD11a (50%-60%), or anti-CD11b (60%-70%). Adhesion to immobilized ligands of beta(2) integrins (intercellular adhesion molecule-1 [ICAM-1], fibrinogen, keyhole limpet hemocyanin) as well as to ICAM-1-transfected Chinese hamster ovary cells, but not to ligands of beta(1) integrins (VCAM-1, fibronectin, laminin, and collagen), was augmented. VCAM-1-Fc binding provoked the expression of the activation-dependent epitope CBRM1/5 of Mac-1 on leukocytes. Clustering of VLA-4 through dimeric VCAM-1-Fc was required for beta(2) integrin activation and induction of cell adhesion, whereas monovalent VCAM-1 or Fab fragments of anti-beta(1) integrin mAb were ineffective. Activation of beta(2) integrins by alpha(4)beta(1) integrin ligation (VCAM-1-Fc or anti-beta(1) mAb) required the presence of urokinase receptor (uPAR) on leukocytic cells, because the removal of uPAR from the cell surface by phosphatidylinositol-specific phospholipase C reduced cell adhesion to less than 40%. Adhesion was reconstituted when soluble recombinant uPAR was allowed to reassociate with the cells. Finally, VLA-4 engagement by VCAM-1-Fc or anti-beta(1) integrin mAb induced uPAR-dependent adhesion to immobilized vitronectin as well. These results elucidate a novel activation pathway of beta(2) integrin-dependent cell-to-cell adhesion that requires alpha(4)beta(1) integrin ligation for initiation and uPAR as activation transducer. (Blood. 2000;96:506-513)

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal
  • CD18 Antigens / immunology
  • CD18 Antigens / metabolism
  • CD18 Antigens / physiology*
  • Cell Adhesion*
  • Endothelium, Vascular / cytology
  • Humans
  • Integrin alpha4beta1
  • Integrins / physiology*
  • Leukocytes / physiology*
  • Lymphocyte Function-Associated Antigen-1 / physiology
  • Macrophage-1 Antigen / physiology
  • Receptors, Cell Surface / physiology*
  • Receptors, Fc / physiology
  • Receptors, Lymphocyte Homing / physiology*
  • Receptors, Urokinase Plasminogen Activator
  • Tumor Cells, Cultured
  • Umbilical Veins
  • Vascular Cell Adhesion Molecule-1 / immunology
  • Vascular Cell Adhesion Molecule-1 / metabolism

Substances

  • Antibodies, Monoclonal
  • CD18 Antigens
  • Integrin alpha4beta1
  • Integrins
  • Lymphocyte Function-Associated Antigen-1
  • Macrophage-1 Antigen
  • PLAUR protein, human
  • Receptors, Cell Surface
  • Receptors, Fc
  • Receptors, Lymphocyte Homing
  • Receptors, Urokinase Plasminogen Activator
  • Vascular Cell Adhesion Molecule-1