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  • Title: Utility of staurosporine in uncovering differences in the signal transduction pathways for superoxide production in neutrophils.
    Author: Robinson JM, Heyworth PG, Badwey JA.
    Journal: Biochim Biophys Acta; 1990 Oct 15; 1055(1):55-62. PubMed ID: 2171676.
    Abstract:
    Neutrophils exhibit an intense phosphorylation of a 47 kDa protein and release large quantities of superoxide (O2-) upon stimulation with phorbol 12-myristate 13-acetate (PMA) or fMet-Leu-Phe (fMLP). Antagonists of protein kinases (e.g., 200 microM 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H-7); 15 nM staurosporine) inhibited these phenomena when the stimulus was PMA (Badwey, J.A. et al. (1989) J. Biol. Chem. 264, 14947-14953). In this paper, we now report that while neutrophils treated with 15 nM staurosporine and PMA release little O2-, cells in the presence of these compounds can be stimulated to release near normal quantities of O2- by the subsequent addition of fMLP. Surprisingly, staurosporine (15 nM) reduced the incorporation of 32P into the 47 kDa protein in fMLP stimulated cells at least as effectively as H-7, yet, while the staurosporine treated cells released substantial amounts of O2-, the cells treated with H-7 did not. These data suggest that a stimulatory pathway exists in neutrophils that contains a protein kinase 'distinct' from that which is activated when PMA is the stimulus and that this pathway may enable the O2- producing system to become functional with little or no phosphorylation of the 47 kDa protein. They further suggest that the steps which are sensitive to H-7 in the signal-transduction pathways utilized by PMA and fMLP may be different.
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