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Physical and functional association of LFA-1 with DNAM-1 adhesion molecule.

Whereas ligation of the DNAM-1 adhesion molecule triggers cytotoxicity mediated by normal NK and T cells, this function was defective in NK cell clones from leukocyte adhesion deficiency syndrome. However, genetic reconstitution of cell surface expression of LFA-1 restored the ability of DNAM-1 to initiate anti-DNAM-1 mAb-induced cytotoxicity, indicating a functional relationship between DNAM-1 and LFA-1. Further studies demonstrated that LFA-1 physically associates with DNAM-1 in NK cells and anti-CD3 mAb stimulated T cells, for which serine phosphorylation of DNAM-1 plays a critical role. In addition, cross-linking of LFA-1 induces tyrosine phosphorylation of DNAM-1, for which the Fyn protein tyrosine kinase is responsible. These results indicate that DNAM-1 is involved in the LFA-1-mediated intracellular signals.

Pubmed ID: 10591186

Authors

  • Shibuya K
  • Lanier LL
  • Phillips JH
  • Ochs HD
  • Shimizu K
  • Nakayama E
  • Nakauchi H
  • Shibuya A

Journal

Immunity

Publication Data

November 4, 1999

Associated Grants

None

Mesh Terms

  • Animals
  • Antibodies, Monoclonal
  • Antigens, CD3
  • Antigens, Differentiation, T-Lymphocyte
  • COS Cells
  • Cell Adhesion
  • Cell Adhesion Molecules
  • Cercopithecus aethiops
  • Cytotoxicity, Immunologic
  • Genetic Complementation Test
  • Humans
  • Jurkat Cells
  • Killer Cells, Natural
  • Leukocyte-Adhesion Deficiency Syndrome
  • Lymphocyte Activation
  • Lymphocyte Function-Associated Antigen-1
  • Mice
  • Phosphorylation
  • Phosphoserine
  • Protein Processing, Post-Translational
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-fyn
  • Signal Transduction
  • T-Lymphocytes
  • Tumor Cells, Cultured