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Recombinant Human Interleukin‐1 Beta Primes Human Polymorphonuclear Leukocytes for Stimulus‐Induced Myeloperoxidase Release
Author(s) -
Dularay B.,
Elson C.J.,
ClementsJewery S.,
Damais C.,
Lando D.
Publication year - 1990
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.47.2.158
Subject(s) - degranulation , myeloperoxidase , azurophilic granule , respiratory burst , exocytosis , superoxide , granulocyte , biology , granule (geology) , chemotaxis , immunology , endocrinology , inflammation , biochemistry , enzyme , secretion , paleontology , receptor
Recombinant human Interleukin‐1 (rhlL‐1) β was found to enhance stimulus‐induced granule exocytosis from human polymorphonuclear leukocytes (PMNs). PMNs were incubated with rhlL‐1β and then stimulated with either heat‐aggregated IgG (Hagg) or N‐ formyhmethionyl leucylphenylalanine (FMLP). The release of the azurophil enzyme myeloperoxidase (MPO) was measured. Low concentrations of stimuli (10 μg/ml Hagg, 2.5 x 10 ‐9 M FMLP) did not stimulate degranulation in the absence of rhlL‐1β. However, such concentrations elicited marked degranulation from PMNs preincubated with rhlL‐1β (0.2‐100 ng/ml). The enhancement of degranulation was dependent on the concentration of rhIL‐1β employed and on the period of incubation. In other experiments, the effect of rhlL‐1β on the PMN oxidative response was determined. rhlL‐1β did not directly stimulate the production of superoxide anions or enhance the oxidative response to Hagg or FMLP. It is suggested that in rheumatoid joints, IL‐1β may potentiate PMN degranulation, but not their oxidative response.