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into the Cell Membranes, and Their Association with Gß After Activation of NK Cells with Chemokines1
Department of Anatomy, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway
The role of phosphoinositide 3 kinases (PI 3-K) in
chemokine-induced NK cell chemotaxis was investigated. Pretreatment of
NK cells with wortmannin inhibits the in vitro chemotaxis of NK cells
induced by lymphotactin, monocyte-chemoattractant protein-1, RANTES,
IFN-inducible protein-10, or stromal-derived factor-1
. Introduction
of inhibitory Abs to PI 3-K
but not to PI 3-K into streptolysin
O-permeabilized NK cells also inhibits chemokine-induced NK cell
chemotaxis. Biochemical analysis showed that within 2–3 min of
activating NK cells, pleckstrin is recruited into NK cell membranes,
whereas PI 3-K associates with these membranes 5 min after
stimulation with RANTES. Recruited PI 3-K generates
phosphatidylinositol 3,4,5 trisphosphate, an activity that is inhibited
upon pretreatment of NK cells with wortmannin. Further analysis showed
that a ternary complex containing the ß dimer of G protein,
pleckstrin, and PI 3-K is formed in NK cell membranes after
activation with RANTES. The recruitment of pleckstrin and PI 3-K
into NK cell membranes is only partially inhibited by pertussis toxin,
suggesting that the majority of these molecules form a complex with
pertussis toxin-insensitive G proteins. Our results may have
application for the migration of NK cells toward the sites of
inflammation.
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