BCR-ABL1 alters SDF-1alpha-mediated adhesive responses through the beta2 integrin LFA-1 in leukemia cells

Blood. 2008 May 15;111(10):5182-6. doi: 10.1182/blood-2007-10-117705. Epub 2008 Mar 13.

Abstract

Stromal-derived factor-1 (SDF-1) and its receptor, CXCR4, are essential for normal hematopoietic progenitor cell movement and adherence within the bone marrow microenvironment. In leukemia, the BCR-ABL1 oncoprotein inhibits SDF-1-dependent cell trafficking within the bone marrow through a mechanism that is not fully understood. Here, we report that BCR-ABL1 in malignant cells constitutively increases expression of activation-dependent epitopes of the beta(2) integrin LFA-1. This is associated with the complete loss of responsiveness of LFA-1 to SDF-1-induced "inside-out" signaling involving CXCR4 and Lyn, leading to aberrant adhesive responses. These data provide a novel, LFA-1-mediated mechanism whereby BCR-ABL1 inhibits SDF-1 action in malignant progenitors.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Cell Adhesion
  • Cell Movement
  • Cells, Cultured
  • Chemokine CXCL12 / physiology*
  • Fusion Proteins, bcr-abl / physiology*
  • Humans
  • Leukemia / pathology*
  • Lymphocyte Function-Associated Antigen-1 / metabolism*
  • Receptors, CXCR4 / metabolism
  • Signal Transduction
  • src-Family Kinases / metabolism

Substances

  • Chemokine CXCL12
  • Lymphocyte Function-Associated Antigen-1
  • Receptors, CXCR4
  • Fusion Proteins, bcr-abl
  • lyn protein-tyrosine kinase
  • src-Family Kinases