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Biochemical Mechanisms Involved in the Priming of Neutrophils by Tumor Necrosis Factor
Author(s) -
Berkow Roger L.,
Dodson Mary R.
Publication year - 1988
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.44.5.345
Subject(s) - biology , pertussis toxin , tumor necrosis factor alpha , superoxide , protein kinase c , chemotaxis , phorbol , arachidonic acid , n formylmethionine leucyl phenylalanine , protein kinase a , biochemistry , neutrophile , kinase , microbiology and biotechnology , g protein , receptor , immunology , in vitro , enzyme
Preincubation of human neutrophils with recombinant tumor necrosis factor alpha has previously been shown by us to enhance superoxide production of neutrophils in response to the chemotactic peptide formyl‐methionyl‐leucyl‐phenylalanine, and the phorbol ester, phorbol myristate acetate. In this study, we further investigate the biochemical basis for this enhancement. We found that in neutrophils, TNF by itself does not induce: (1) an influx of sodium, (2) an alteration in activity or translocation of the calcium and phospholipid dependent protein kinase (C‐kinase), or (3) a release of arachidonic acid from preloaded cells. TNF did, however, induce a time‐ and concentration‐dependent increase in the phosphorylation of several neutrophil proteins, with the most dramatic concentration dependent increase in a 64,000 Da protein. Finally, the enhancement of O 2 production by pretreatment of neutrophils with TNF was found to be independent of a pertussis toxin‐sensitive guanine nucleotide regulatory protein.