The CD49d/CD29 complex is physically and functionally associated with CD38 in B-cell chronic lymphocytic leukemia cells

Leukemia. 2012 Jun;26(6):1301-12. doi: 10.1038/leu.2011.369. Epub 2012 Jan 6.

Abstract

CD49d and CD38 are independent negative prognostic markers in chronic lymphocytic leukemia (CLL). Their associated expression marks a disease subset with a highly aggressive clinical course. Here, we demonstrate a constitutive physical association between the CD49d/CD29 integrin complex and CD38 in primary CLL cells and B-cell lines by (i) cocapping, (ii) coimmunoprecipitation and (iii) cell adhesion experiments using CD49d-specific substrates (vascular-cell adhesion molecule-1 or CS-1/H89 fibronectin fragments). The role of CD38 in CD49d-mediated cell adhesion was studied in CD49d(+)CD38(+) and CD49d(+)CD38(-) primary CLL cells, and confirmed using CD38 transfectants of the originally CD49d(+)CD38(-) CLL-derived cell line Mec-1. Results indicate that CD49d(+)CD38(+) cells adhered more efficiently onto CD49d-specific substrates than CD49d(+)CD38(-) cells (P < 0.001). Upon adhesion, CD49d(+)CD38(+) cells underwent distinctive changes in cell shape and morphology, with higher levels of phosphorylated Vav-1 than CD49d(+)CD38(-) cells (P = 0.0006) and a more complex distribution of F-actin to the adhesion sites. Lastly, adherent CD49d(+)CD38(+) cells were more resistant to serum-deprivation-induced (P < 0.001) and spontaneous (P = 0.03) apoptosis than the CD49d(+)CD38(-) counterpart. Altogether, our results point to a direct role for CD38 in enhancing CD49d-mediated adhesion processes in CLL, thus providing an explanation for the negative clinical impact exerted by these molecules when coexpressed in neoplastic cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ADP-ribosyl Cyclase 1 / metabolism*
  • Actins / metabolism
  • Apoptosis*
  • Blotting, Western
  • Cell Adhesion / physiology*
  • Cell Proliferation
  • Culture Media, Serum-Free
  • Flow Cytometry
  • Fluorescent Antibody Technique
  • Humans
  • Immunoprecipitation
  • Integrin alpha4 / metabolism
  • Integrin alpha4beta1 / metabolism*
  • Leukemia, Lymphocytic, Chronic, B-Cell / metabolism*
  • Leukemia, Lymphocytic, Chronic, B-Cell / pathology*
  • Membrane Microdomains / metabolism
  • Phosphorylation
  • Proto-Oncogene Proteins c-vav / metabolism
  • Tumor Cells, Cultured

Substances

  • Actins
  • Culture Media, Serum-Free
  • Integrin alpha4beta1
  • Proto-Oncogene Proteins c-vav
  • VAV1 protein, human
  • Integrin alpha4
  • ADP-ribosyl Cyclase 1