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Anti‐inflammatory action of dapsone: inhibition of neutrophil adherence is associated with inhibition of chemoattractant‐induced signal transduction
Author(s) -
Debol Steven M.,
Herron Michael J.,
Nelson Robert D.
Publication year - 1997
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.62.6.827
Subject(s) - chemotaxis , dapsone , signal transduction , biology , immunology , microbiology and biotechnology , pharmacology , in vitro , biochemistry , receptor
Dapsone has clinical utility as an anti‐inflammatory agent but the mechanism of this action remains unknown. We have previously reported that dapsone inhibits β 2 integrin (CD11b/CD18) ‐mediated adherence of human neutrophils in vitro and now describe studies designed to discover how dapsone‐mediated inhibition of this neutrophil function occurs. Results indicate that dapsone interferes with the activation or function of the G‐protein (G i type) that initiates the signal transduction cascade common to chemotactic stimuli. They also show that dapsone‐mediated suppression of this pathway inhibits the generation of second messengers essential to the activation of β 2 integrin molecules, as well as respiratory and secretory functions of neutrophils exposed to chemoattractants. We propose that the inhibition of chemoattractant‐induced signal transduction by dapsone suppresses neutrophil recruitment and local production of toxic respiratory and secretory products in the affected skin of dermatitis herpetiformis and other neutrophilic dermatoses. J. Leukoc. Biol . 62: 827–836; 1997.