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      Tumor necrosis factor-alpha/cachectin activates the O2(-)-generating system of human neutrophils independently of the hydrolysis of phosphoinositides and the release of arachidonic acid.

      Biochemical and Biophysical Research Communications

      pharmacology, 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine, Alkaloids, Arachidonic Acids, blood, Bucladesine, Humans, Hydrolysis, In Vitro Techniques, Inositol Phosphates, Isoquinolines, Kinetics, Neutrophils, drug effects, metabolism, Pertussis Toxin, Phosphatidic Acids, Phosphatidylinositols, Piperazines, Protein Kinase C, antagonists & inhibitors, Protein Kinase Inhibitors, Staurosporine, Superoxides, Theophylline, Tumor Necrosis Factor-alpha, Virulence Factors, Bordetella

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          Abstract

          We have investigated the mechanisms of transmembrane signalling implicated in the activation of the respiratory burst of adherent neutrophils by tumor necrosis factor-alpha/cachectin (TNF). The activation of the respiratory burst by TNF is insensitive to pertussis toxin and weakly sensitive to protein kinase C inhibitors. Cytochalasin B and dibutyryl cyclic AMP have an inhibitory effect. The activation of the respiratory burst by TNF takes place in the absence of formation of 3H-inositol phosphates, 32P-phosphatidic acid, and 3H-arachidonic acid. These results demonstrate that the activation of the respiratory burst by an endogenous, physiologic stimulus can be independent of the formation of messengers derived from hydrolysis of phosphoinositides.

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          2154202

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