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(Received for publication, January 27, 1997)
From the Departments of Intercellular adhesion molecule 1 (ICAM-1) (CD54)
is an adhesion molecule of the immunoglobulin superfamily. The
interaction between ICAM-1 on B lymphocytes and leukocyte
function-associated antigen 1 on T cells plays a major role in several
aspects of the immune response, including T-dependent B
cell activation. While it was originally believed that ICAM-1 played a
purely adhesive role, recent evidence suggests that it can itself
transduce biochemical signals. We demonstrate that cross-linking of
ICAM-1 results in the up-regulation of class II major
histocompatibility complex, and we investigate the biochemical
mechanism for the signaling role of ICAM-1. We show that cross-linking
of ICAM-1 on the B lymphoma line A20 induces an increase in tyrosine
phosphorylation of several cellular proteins, including the Src family
kinase p53/p56lyn. In vitro kinase assays
showed that Lyn kinase was activated within 1 min after ICAM-1
cross-linking. In addition, ICAM-1 cross-linking resulted in activation
of Raf-1 and mitogen-activated protein kinases, as determined by gel
mobility shift. Activation of these kinases may represent important
components in the cascade of signals that link ICAM-1 to various
ICAM-1-elicited cellular responses. These data confirm the important
role of ICAM-1 as a signaling molecule in B cell activation.
Volume 272, Number 14,
Issue of April 4, 1997
pp. 9108-9112
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
THE ACTIVATION OF Lyn TYROSINE KINASE AND THE
MITOGEN-ACTIVATED PROTEIN KINASE PATHWAY
and
Microbiology and Immunology,
and § Neurology and Neurosurgery, McGill University,
Neuroimmunology Unit, Montreal Neurological Institute, 3801 University,
Montreal, Quebec, Canada H3A 2B4
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