Premium
Lineage‐specific activation of STAT3 by interferon‐γ in human neutrophils
Author(s) -
Caldenhoven Eric,
Buitenhuis Miranda,
Djk Thamar B.,
Raaijmakers Jan A. M.,
Lammers JanWillem J.,
Koenderman Leo,
Groot Rolf P.
Publication year - 1999
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.65.3.391
Subject(s) - biology , stat1 , tyrosine phosphorylation , stat3 , interferon , receptor tyrosine kinase , microbiology and biotechnology , jak stat signaling pathway , receptor , stat , phosphorylation , immunology , biochemistry
Binding of interferon‐γ (IFN‐γ) to its heterodimeric receptor induces activation of the tyrosine kinases JAK1 and JAK2 followed by tyrosine phosphorylation of STAT1α. Selective activation of STAT1α at the IFN‐γ receptor is achieved by specific interaction between a cytosolic tyrosine motif including Y440 in the IFN‐γ receptor α‐chain and the SH2 domain of STAT1α. We demonstrate that, in addition to STAT1α, STAT3 is also activated by IFN‐γ in human neutrophils. The activation of STAT3 was not found in human eosinophils, monocytes, and HL‐60 cells, although the STAT3 protein was expressed in these cells. The cell type‐specific activation of STAT3 by IFN‐γ was also observed in neutrophils that are differentiated in vitro from human CD34 + hematopoietic stem cells. These results indicate that a single cytokine receptor can activate different STAT family members in a cell‐specific manner, which might result in cell‐specific gene transcription. J. Leukoc. Biol. 65: 391–396; 1999.