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J Biol Chem, Vol. 274, Issue 29, 20704-20708, July 16, 1999

Priming of Human Neutrophil Respiratory Burst by Granulocyte/Macrophage Colony-stimulating Factor (GM-CSF) Involves Partial Phosphorylation of p47^phox

From the INSERM U. 479, Centre Hospitalier Universitaire Xavier Bichat, Faculté de Medecine, 16 rue Henri Huchard, 75018 Paris, France

Neutrophil superoxide production can be potentiated by prior exposure to "priming" agents such as granulocyte/macrophage colony stimulating factor (GM-CSF). Because the mechanism underlying GM-CSF-dependent priming is not understood, we investigated the effects of GM-CSF on the phosphorylation of the cytosolic NADPH oxidase components p47^phox and p67^phox. Preincubation of neutrophils with GM-CSF alone increased the phosphorylation of p47^phox but not that of p67^phox. Addition of formyl-methionyl-leucyl-phenylalanine (fMLP) to GM-CSF-pretreated neutrophils resulted in more intense phosphorylation of p47^phox than with GM-CSF alone and fMLP alone. GM-CSF-induced p47^phox phosphorylation was time- and concentration-dependent and ran parallel to the priming effect of GM-CSF on superoxide production. Two-dimensional tryptic peptide mapping of p47^phox showed that GM-CSF induced phosphorylation of one major peptide. fMLP alone induced phosphorylation of several peptides, an effect enhanced by GM-CSF pretreatment. In contrast to fMLP and phorbol 12-myristate 13-acetate, GM-CSF-induced phosphorylation of p47^phox was not inhibited by the protein kinase C inhibitor GF109203X. The protein-tyrosine kinase inhibitor genistein and the phosphatidylinositol 3-kinase inhibitor wortmannin inhibited the phosphorylation of p47^phox induced by GM-CSF and by fMLP but not that induced by phorbol 12-myristate 13-acetate. GM-CSF alone did not induce p47^phox or p67^phox translocation to the membrane, but neutrophils treated consecutively with GM-CSF and fMLP showed an increase (compared with fMLP alone) in membrane translocation of p47^phox and p67^phox. Taken together, these results show that the priming action of GM-CSF on the neutrophil respiratory burst involves partial phosphorylation of p47^phox on specific serines and suggest the involvement of a priming pathway regulated by protein-tyrosine kinase and phosphatidylinositol 3-kinase.

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