Cited by 329Neutrophil, Myeloperoxidase and Oxidative MechanismsImmunotherapy and Immune ResponsesRedox biology and oxidative stress

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NADPH oxidase controls phagosomal pH and antigen cross-presentation in human dendritic cells

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Mantegazza, Adriana R., Savina, Ariel, Vermeulen, Mónica, Pérez, Laura, Geffner, Jorge, Hermine, Olivier, Rosenzweig, Sergio D., Faure, Florence, Amigorena, Sebastián·2008·Blood

DOI 10.1182/blood-2008-01-134791PMC PMC2597138

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Abstract

The phagocyte NADPH oxidase (NOX2) is critical for the bactericidal activity of phagocytic cells and plays a major role in innate immunity. We showed recently that NOX2 activity in mouse dendritic cells (DCs) prevents acidification of phagosomes, promoting antigen cross-presentation. Inorder to investigate the role of NOX2 in the regulation of the phagosomal pH in human DCs, we analyzed the production of reactive oxygen species (ROS) and the phagosomal/endosomal pH in monocyte-derived DCs and macrophages (MØs) from healthy donors or patients with chronic granulomatous disease (CGD). As expected, we found that human MØs acidify their phagosomes more efficiently than human DCs. Accordingly, the expression of the vacuolar proton ATPase (V-H+-ATPase) was higher in MØs than in DCs. Phagosomal ROS production, however, was also higher in MØs than in DCs, due to higher levels of gp91phox expression and recruitment to phagosomes. In contrast, in the absence of active NOX2, the phagosomal and endosomal pH decreased. Both in the presence of a NOX2 inhibitor and in DCs derived from patients with CGD, the cross-presentation of 2 model tumor antigens was impaired. We conclude that NOX2 activity participates in the regulation of the phagosomal and endosomal pH in human DCs, and is required for efficient antigen cross-presentation.

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Differential Lysosomal Proteolysis in Antigen-Presenting Cells Determines Antigen Fate
Delamarre, L., Pack, M., Chang, H. C., Mellman, I., & Trombetta, E. S. (2005) · Science · doi:10.1126/science.1108003 · Cited by 776
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Authors: Mantegazza, A. R., Savina, A., Vermeulen, M., Pérez, L., Geffner, J., Hermine, O., Rosenzweig, S. D., Faure, F., & Amigorena, S.
Affiliations: Inserm (FR)
Instituto de Investigaciones Hematológicas, Academia Nacional de Medicina, Buenos Aires, Argentina;
Garrahan Hospital (AR)
Academia Nacional de Medicina (AR)
Hôpital Necker-Enfants Malades (FR)
ORCID: Mantegazza, Adriana R.
Pérez, Laura
Geffner, Jorge
Hermine, Olivier
Rosenzweig, Sergio D.
Faure, Florence
Amigorena, Sebastián
Venue: Blood
Publisher: American Society of Hematology
Published: 2008-12-01
Volume: 112
Issue: 12
Pages: 4712-4722
ISSN: 0006-4971 (ISSN-L)
1528-0020
DOI: 10.1182/blood-2008-01-134791
PMC: PMC2597138
OpenAlex: W2093168274
Cited by: 329
References: 34
Citations by year: 2026: 14 · 2025: 16 · 2024: 17 · 2023: 26 · 2022: 23 · 2021: 22 · 2020: 28 · 2019: 17 · 2018: 22 · 2017: 18 · 2016: 15 · 2015: 18 · 2014: 8 · 2013: 15 · 2012: 28
FWCI: 5.84
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Blood (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion)
CONICET Digital (CONICET) (submittedVersion, cc-by-nc-sa)
Funders: Institut National de la Santé et de la Recherche Médicale
Consejo Nacional de Investigaciones Científicas y Técnicas
National Institutes of Health
Directorate for Biological Sciences
Fogarty International Center (R01TW006644)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: NADPH oxidase, NOX2, dendritic cells, phagosomal pH, cross-presentation, reactive oxygen species, gp91phox, vacuolar ATPase, chronic granulomatous disease, monocyte-derived macrophages, endosomal pH, innate immunity
MeSH terms: NADPH Oxidase 2, Acid-Base Equilibrium, Adolescent, Adult, Cells, Cultured, Child, Child, Preschool, Dendritic Cells, Humans, Hydrogen-Ion Concentration, Macrophages, Membrane Glycoproteins, Phagosomes, Antigen Presentation, NADPH Oxidases, Cross-Priming, Young Adult

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NADPH oxidase controls phagosomal pH and antigen cross-presentation in human dendritic cells

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