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Cited by 31Neutrophil, Myeloperoxidase and Oxidative MechanismsProtein Kinase Regulation and GTPase SignalingRedox biology and oxidative stress

IFN-γ Induces gp91 phox Expression in Human Monocytes via Protein Kinase C-Dependent Phosphorylation of PU.1

Mazzi, Paola, Donini, Marta, Margotto, Daniela, Wientjes, Frans, Dusi, Stefano·2004·The Journal of Immunology
DOI 10.4049/jimmunol.172.8.4941
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Abstract

We previously reported that the stimulation of human blood monocytes with IFN-γ induces the binding of PU.1 to the gp91phox promoter and the consequent expression of gp91phox. In this study, we show that the effect of IFN-γ is reproduced by the serine phosphatase inhibitor, okadaic acid, and this suggests that serine kinases could be involved in gp91phox expression. We also show that IFN-γ induces the serine/threonine phosphorylation of PU.1 in cultured monocytes. This phosphorylation, as well as the IFN-γ-induced PU.1 binding and gp91phox protein synthesis, is slightly affected by the casein kinase II inhibitor, daidzein, but is abrogated by the protein kinase C (PKC) -α and -β inhibitor, Go6976, and by synthetic peptides with sequences based on the endogenous pseudosubstrate region of the classical PKC α and β isoforms. In contrast, peptides reproducing the pseudosubstrate region of PKC ε were without effect. Moreover, we found that the treatment of monocytes with IFN-γ induces the nuclear translocation and the activation of PKC α and βI, but not of PKC βII, and that the IFN-γ-induced phosphorylation of PU.1 was greatly reduced by LY333531, a selective inhibitor of PKC β isoforms. Finally, nuclear run-on assays demonstrated that while the PKC inhibitors, Go6976 and LY333531, decrease the IFN-γ-induced gp91phox transcription, the serine phosphatase inhibitor, okadaic acid, enhances the gp91phox gene transcription. Our results indicate that in cultured monocytes, IFN-γ induces the binding of PU.1 to the gp91phox promoter and the expression of gp91phox by phosphorylation of PU.1 via activation of PKC α and/or βI.

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Authors
Mazzi, P., Donini, M., Margotto, D., Wientjes, F., & Dusi, S.
Affiliations
  • University of Verona (IT)
  • University College London (GB)
ORCID
Venue
The Journal of Immunology
Publisher
Oxford University Press (OUP)
Published
2004-04
Volume
172
Issue
8
Pages
4941-4947
ISSN
  • 0022-1767 (ISSN-L)
  • 1550-6606
DOI
10.4049/jimmunol.172.8.4941
OpenAlex
W1511657657
Semantic Scholar
e1ba8a527aaafd5f06798a331962c76de0d1c716
Cited by
31
References
38
Citations by year
2026: 1 · 2025: 2 · 2016: 1 · 2015: 1 · 2013: 5
FWCI
1.22
Type
journal article
Language
en
Open access
closed
Licence
academic.oup.com/pages/standard-publication-reuse-rights (vor)
Locations
  • The Journal of Immunology (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords
interferon-gamma, gp91phox, NADPH oxidase, PU.1, protein kinase C, serine phosphorylation, monocytes, transcriptional regulation
MeSH terms
NADPH Oxidase 2, Proto-Oncogene Protein Spi-1, Cell Nucleus, Cells, Cultured, Enzyme Activation, Gene Expression Regulation, Humans, Interferon-gamma

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