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.
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
Immunity
Date: Nov. 01, 1999
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