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Inhibition of crystal‐induced neutrophil activation by a protein tyrosine kinase inhibitor
Author(s) -
Burt Helen M.,
Jackson John K.,
Salari Hassan
Publication year - 1994
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.55.1.112
Subject(s) - myeloperoxidase , superoxide , tyrosine kinase , protein tyrosine phosphatase , lysozyme , respiratory burst , nadph oxidase , kinase , degranulation , neutrophil extracellular traps , intracellular , biochemistry , tyrosine kinase inhibitor , tyrosine , chemistry , microbiology and biotechnology , biology , reactive oxygen species , signal transduction , medicine , enzyme , immunology , inflammation , receptor , cancer
The objective of this work was to investigate the role of tyrosine kinase in monosodium urate monohydrate (MSUM) and calcium pyrophosphate dihydrate (CPPD) crystal‐induced neutrophil activation using the tyrosine kinase inhibitor lavendustin C (LVC). Human neutrophils pretreated with LVC at concentrations between 10 and 150 μ M or control neutrophils were stimulated by plasma‐coated CPPD or uncoated MSUM, and chemiluminescence, superoxide generation, intracellular calcium concentration, and degranulation (myeloperoxidase and lysozyme release) were monitored with time. LVC strongly inhibited chemiluminescence, superoxide anion generation, myeloperoxidase and lysozyme release, and calcium mobilization. After 1‐min crystal‐neutrophil incubations, neutrophil cytosolic fractions showed extensive inhibition of tyrosine kinase activity by LVC. We conclude that the inhibition of neutrophil responses to crystal stimulation, by the protein tyrosine kinase inhibitor LVC, provides evidence that supports the involvement of tyrosine kinases in crystal‐induced neutrophil activation. J. Leukoc. Biol . 55: 112–119; 1994.