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

Abstract
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.
AuthorsK Shibuya, L L Lanier, J H Phillips, H D Ochs, K Shimizu, E Nakayama, H Nakauchi, A Shibuya
JournalImmunity (Immunity) Vol. 11 Issue 5 Pg. 615-23 (Nov 1999) ISSN: 1074-7613 [Print] United States
PMID10591186 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Antibodies, Monoclonal
  • Antigens, Differentiation, T-Lymphocyte
  • CD226 antigen
  • CD3 Complex
  • Cell Adhesion Molecules
  • Lymphocyte Function-Associated Antigen-1
  • Proto-Oncogene Proteins
  • Phosphoserine
  • FYN protein, human
  • Fyn protein, mouse
  • Proto-Oncogene Proteins c-fyn
Topics
  • Animals
  • Antibodies, Monoclonal (immunology)
  • Antigens, Differentiation, T-Lymphocyte
  • CD3 Complex (immunology)
  • COS Cells
  • Cell Adhesion
  • Cell Adhesion Molecules (chemistry, immunology, physiology)
  • Chlorocebus aethiops
  • Cytotoxicity, Immunologic
  • Genetic Complementation Test
  • Humans
  • Jurkat Cells
  • Killer Cells, Natural (immunology)
  • Leukocyte-Adhesion Deficiency Syndrome (immunology, pathology)
  • Lymphocyte Activation
  • Lymphocyte Function-Associated Antigen-1 (chemistry, physiology)
  • Mice
  • Phosphorylation
  • Phosphoserine (metabolism)
  • Protein Processing, Post-Translational
  • Proto-Oncogene Proteins (physiology)
  • Proto-Oncogene Proteins c-fyn
  • Signal Transduction (physiology)
  • T-Lymphocytes (immunology)
  • Tumor Cells, Cultured

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