PubMed:10224470 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/10224470","sourcedb":"PubMed","sourceid":"10224470","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/10224470","text":"Signal transduction through interferon-gamma receptor on human eosinophils.\nBACKGROUND: We reported on the constitutive interferon-gamma receptor (IFN-gammaR) expression on eosinophils. But signal transduction through IFN-gammaR on eosinophils remains to be elucidated. In this study, we examined the involvement of the Jak/Stat pathway in the signaling of eosinophils after IFN-gammaR conjugation by the ligand binding.\nMETHODS: Purified peripheral eosinophils were stimulated with IFN-gamma at 37 degrees C for 1-60 min. Tyrosine phosphorylation of IFN-gammaR, Jak1, Jak2, and Stat1alpha was examined by immunoblotting. Gel-shift assay was also examined to show the formation of Stat1alpha-DNA complexes.\nRESULTS: We show that binding of IFN-gamma to human eosinophils initiated a series of events that resulted in the rapid tyrosine phosphorylation of not only the IFN-gammaRalpha chain but also Jak1, Jak2, and Stat1alpha. In addition, IFN-gamma enhanced the DNA-binding activity of Stat1alpha.\nCONCLUSION: These data indicate that IFN-gamma affects eosinophils through its specific receptor and utilizes the Jak/Stat pathway as its mode of 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