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-Induced Lymphocyte Polarization and Chemotaxis1
*
Servicio de Inmunología, Hospital de la Princesa, Universidad Autónoma de Madrid, Madrid, Spain; and
Department of Immunology and Oncology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Universidad Autónoma de Madrid, Campus de Cantoblanco, Madrid, Spain
The role of phosphatidylinositol 3-kinase (PI3-kinase), an
important enzyme involved in signal transduction events, has been
studied in the polarization and chemotaxis of lymphocytes induced by
the chemokine stromal cell-derived factor-1
(SDF-1). This
chemokine was able to directly activate p85/p110 PI3-kinase in whole
human PBL and to induce the association of PI3-kinase to the SDF-1
receptor, CXCR4, in a pertussis toxin-sensitive manner.
Two unrelated chemical inhibitors of PI3-kinase, wortmannin and
Ly294002, prevented ICAM-3 and ERM protein moesin polarization as well
as the chemotaxis of PBL in response to SDF-1. However, they did not
interfere with the reorganization of either tubulin or the actin
cytoskeleton. Moreover, the transient expression of a dominant negative
form of the PI3-kinase 85-kDa regulatory subunit in the constitutively
polarized Peer T cell line inhibited ICAM-3 polarization and markedly
reduced SDF-1-induced chemotaxis. Conversely, overexpression of a
constitutively activated mutant of the PI3-kinase 110-kDa catalytic
subunit in the round-shaped PM-1 T cell line induced ICAM-3
polarization. These results underline the role of PI3-kinase in the
regulation of lymphocyte polarization and motility and indicate that
PI3-kinase plays a selective role in the regulation of adhesion and ERM
proteins redistribution in the plasma membrane of
lymphocytes.
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