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Potentiation of Neutrophil Function by Recombinant DNA‐Produced Interleukin 1a
Author(s) -
Ozaki Yukio,
Ohashi Tatsuya,
Kume Shoji
Publication year - 1987
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.42.6.621
Subject(s) - zymosan , opsonin , phagocytosis , cytochalasin , biology , degranulation , cytochalasin b , antibody opsonization , respiratory burst , chemotaxis , granule (geology) , neutrophile , granulocyte , azurophilic granule , neutrophil extracellular traps , immunology , in vitro , myeloperoxidase , biochemistry , inflammation , cell , paleontology , receptor , cytoskeleton
The effect of interleukin 1a (IL‐1a) produced by E. coli‐derived recombinant DNA was evaluated on various parameters of human neutrophil function. IL‐1 a alone stimulated neutrophil hydrogen peroxide production in a dose‐dependent manner, but the rate was much lower than that of opsonized zymosan. IL‐1 a induced release of specific granule contents, but not azurophilic granule contents. Cytochalasin B did not augment the rate of release. IL‐1 a was chemotactic for neutrophils at the optimal concentrations of 0.1‐10 ng/ml. Pretreatment of the neutrophils with IL‐1 a augmented neutrophil oxygen radical production induced by opsonized zymosan, and this synergistic effect was evident as early as 10 min after IL‐1 a was added to the neutrophil culture. Phagocytosis of opsonized particles by neutrophils, and degranulation induced by opsonized zymosan were also enhanced by IL‐1 a in a dose‐dependent manner. The present results suggest that IL‐1 a is weak as a direct activator of neutrophil function and that IL‐1 a in vivo may augment the response of neutrophils to other stimulators such as foreign bodies.