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*
Department of Experimental Medicine and Pathology, Istituto Pasteur-Fondazione Cenci Bolognetti, University of Rome "La Sapienza," Rome, Italy;
Department of Experimental Medicine, University of L’Aquila, L’Aquila, Italy;
Biotechnology Section, Institute for the Study and Cure of Tumors, Genoa, Italy; and
§
Mediterranean Institute of Neuroscience "Neuromed," Pozzilli, Italy
Recent data indicate that integrin-generated signals can modulate
different receptor-stimulated cell functions in both a positive
(costimulation) and a negative (inhibition) fashion. Here we
investigated the ability of ß1 integrins, namely
4ß1 and 5ß1
fibronectin receptors, to modulate CD16-triggered phospholipase
activation in human NK cells. ß1 integrin simultaneous
cross-linking selectively inhibited CD16-induced phospholipase D (PLD)
activation, without affecting either phosphatidylinositol-phospholipase
C or cytosolic phospholipase A2 (PLA2)
enzymatic activity. CD16-induced secretory PLA2
(sPLA2) protein release as well as its enzymatic activity
in both cell-associated and soluble forms were also found to be
inhibited upon ß1 integrin coengagement. The similar
effects exerted by specific PLD pharmacological inhibitors
(2,3-diphosphoglycerate, ethanol) suggest that in our experimental
system, sPLA2 secretion and activation are under the
control of a PLD-dependent pathway. By using pharmacological inhibitors
(2,3-diphosphoglycerate, wortmannin, ethanol) we also demonstrated that
PLD activation is an important step in the CD16-triggered signaling
cascade that leads to NK cytotoxic granule exocytosis. Consistent with
these findings, fibronectin receptor engagement, by either mAbs or
natural ligands, resulted in a selective inhibition of CD16-triggered,
but not of PMA/ionomycin-induced, degranulation that was reversed by
the exogenous addition of purified PLD from Streptomyces
chromofuscus.
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