Cytokine priming of the respiratory burst in human eosinophils is Ca2+ independent and accompanied by induction of tyrosine kinase activity
Autor: | P.T.M. Kok, R. G. C. Kessels, T. Van Der Bruggen, Leo Koenderman, J. A. M. Raaijmakers, Arthur J. Verhoeven, Jan Willem J. Lammers |
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Rok vydání: | 1993 |
Předmět: |
medicine.medical_specialty
Immunology Priming (immunology) In Vitro Techniques Biology chemistry.chemical_compound Oxygen Consumption Internal medicine medicine Humans Immunology and Allergy Platelet Activating Factor Tyrosine Dose-Response Relationship Drug Kinase Ionomycin Zymosan Granulocyte-Macrophage Colony-Stimulating Factor Tyrosine phosphorylation Cell Biology Protein-Tyrosine Kinases Phosphoproteins Molecular biology Recombinant Proteins Respiratory burst Eosinophils Molecular Weight Kinetics Endocrinology chemistry Enzyme Induction Phosphorylation Calcium Interleukin-3 Interleukin-5 Signal transduction Tyrosine kinase |
Zdroj: | Scopus-Elsevier |
ISSN: | 1938-3673 0741-5400 |
DOI: | 10.1002/jlb.53.4.347 |
Popis: | We report that pretreatment of human eosinophils with GM-CSF, IL-3, or IL-5 enhanced the respiratory burst induced by opsonized particles. In order to gain more insight into the intracellular mechanism(s) involved in cytokine priming, the role of [Ca2+], and tyrosine kinases was studied. Optimal priming concentrations of GM-CSF, IL-3, and IL-5 did not induce a rise in [Ca2+]i, and Ca2+-depleted eosinophils ([Ca2+]i < 20 nM) were still primed after preincubation with these cytokines. GM-CSF, IL-3, and IL-5 induced phosphorylation of two proteins (102 and 122 kd) on tyrosine residues, as deduced from Western blot analysis with an antiphospho- tyrosine monoclonal antibody (4G10). This cytokine- stimulated tyrosine phosphorylation was not inhibited under Ca2+-depleted conditions. In conclusion, this study demonstrates that GM-CSF, IL-3, and IL-5 priming of the opsonized particle-induced respiratory burst in human eosinophils is completely Ca2+ independent. Moreover the tyrosine phosphorylation of a 102-kd and a 122-kd protein is Ca2+ independent, suggesting that this event might be involved in cytokine priming. J. Leukoc. Biol. 53: 347–353; 1993. |
Databáze: | OpenAIRE |
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