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Vol. 10, Issue 6, 1891-1907, June 1999
and
*Departamento de Bioquímica y Biología Molecular,
Facultad de Medicina, Universidad Complutense, 28040 Madrid, Spain;
Integrin receptors play a central role in the biology of
lymphocytes, mediating crucial functional aspects of these cells, including adhesion, activation, polarization, migration, and signaling. Here we report that induction of activation of the
Servicio de Inmunología, Hospital de la Princesa,
28006 Madrid, Spain; and Leukocyte Adhesion Laboratory,
Imperial Cancer Research Fund, London WC2A 3PX, United Kingdom
2-integrin lymphocyte function-associated antigen 1 (LFA-1)
in T lymphocytes with divalent cations, phorbol esters, or stimulatory
antibodies is followed by a dramatic polarization, resulting in a
characteristic elongated morphology of the cells and the arrest of
migrating lymphoblasts. This cellular polarization was prevented by
treatment of cells with the specific tyrosine kinase inhibitor
genistein. Furthermore, the interaction of the activated
integrin LFA-1 with its ligand intercellular adhesion
molecule 1 induced the activation of the cytoplasmic tyrosine
kinases focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (PYK-2). FAK activation reached a maximum after 45 min of stimulation;
in contrast, PYK-2 activation peaked at 30 min, declining after 60 min.
Upon polarization of lymphoblasts, FAK and PYK-2 redistributed from a
diffuse localization in the cytoplasm to a region close to the
microtubule-organizing center in these cells. FAK and PYK-2 activation
was blocked when lymphoblasts were pretreated with actin and tubulin
cytoskeleton-interfering agents, indicating its cytoskeletal
dependence. Our results demonstrate that interaction of the
2-integrin LFA-1 with its ligand intercellular adhesion
molecule 1 induces remodeling of T lymphocyte morphology and activation
and redistribution of the cytoplasmic tyrosine kinases FAK and
PYK-2.
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