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(Journal of Leukocyte Biology. 2002;71:695-700.)
© 2002 by Society for Leukocyte Biology

Contribution of phopholipase D and a brefeldin A-sensitive ARF to chemoattractant-induced superoxide production and secretion of human neutrophils

Krisztina Káldi^*, Júlia Szeberényi^*, Balázs K. Rada^*, Péter Kovács, Miklós Geiszt^*, Attila Mócsai^* and Erzsébet Ligeti^*

Departments of
^* Physiology, and
Genetics, Cell and Immunobiology, Semmelweis University, Budapest, Hungary

Correspondence: Dr. Erzsébet Ligeti, Department of Physiology, Semmelweis University, Puskin u.9., H-1088 Budapest, Hungary. E-mail: ligeti{at}puskin.sote.hu

We show that blockers of phospholipase D (PLD) reduce fMLP-triggered exocytosis of secretory vesicles effectively. In accordance with this, the PLD product phosphatidic acid (PA) was able to induce mobilization of secretory vesicles. Although PLD seems to play a role in the release of all neutrophil granule types, exogenous PA alone was not sufficient to activate the exocytosis of primary and secondary granules, suggesting that in the case of these granules, additional signaling factors are required to initiate the secretory responses. The ADP-ribosylation factor (ARF)-inhibitor brefeldin A (BFA) inhibited the fMLP-stimulated O₂^·- production strongly, whereas it did not influence any of the exocytic responses, and no significant effect of BFA was detected on the O₂^·- generation induced by other stimuli. On the basis of these results, we propose that upon chemoattractant stimulation, PLD activity is involved in induction of degranulation and O₂^·- production, but a BFA-sensitive ARF is only required to the activation of the NADPH oxidase. This ARF action seems to participate exclusively in the signaling pathway between the fMLP receptor and the oxidase.

Key Words: phagocytes • NADPH oxidase • fMLP receptor • secretory vesicles

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