A Ca2+-activated NADPH Oxidase in Testis, Spleen, and Lymph Nodes
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Superoxide and its derivatives are increasingly implicated in the regulation of physiological functions from oxygen sensing and blood pressure regulation to lymphocyte activation and sperm-oocyte fusion. Here we describe a novel superoxide-generating NADPH oxidase referred to as NADPH oxidase 5 (NOX5). NOX5 is distantly related to the gp91(phox) subunit of the phagocyte NADPH oxidase with conserved regions crucial for the electron transport (NADPH, FAD and heme binding sites). However, NOX5 has a unique N-terminal extension that contains three EF hand motifs. The mRNA of NOX5 is expressed in pachytene spermatocytes of testis and in B- and T-lymphocyte-rich areas of spleen and lymph nodes. When heterologously expressed, NOX5 was quiescent in unstimulated cells. However, in response to elevations of the cytosolic Ca(2+) concentration it generated large amounts of superoxide. Upon Ca(2+) activation, NOX5 also displayed a second function: it became a proton channel, presumably to compensate charge and pH alterations due to electron export. In summary, we have identified a novel NADPH oxidase that generates superoxide and functions as a H(+) channel in a Ca(2+)-dependent manner. NOX5 is likely to be involved in Ca(2+)-activated, redox-dependent processes of spermatozoa and lymphocytes such as sperm-oocyte fusion, cell proliferation, and cytokine secretion.
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NOX5 is the last discovered NOX isoform.
“NOX5 is the last discovered NOX isoform (62).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [62]
The particular architecture of NOX5 indicates a regulation of its activity through Ca2+ levels.
“As indicated above, the particular architecture of NOX5 indicates a regulation of its activity through Ca2+ levels (62, 469).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [62]
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- Authors
- Bánfi, B., Molnár, G., Maturana, A., Steger, K., Hegedûs, B., Demaurex, N., & Krause, K.-H.
- Affiliations
- Semmelweis University (HU)
- Justus-Liebig-Universität Gießen (DE)
- University Hospital of Geneva (CH)
- Corresponding author
- Krause, Karl-Heinz
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-10
- Volume
- 276
- Issue
- 40
- Pages
- 37594-37601
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2073241455
- Cited by
- 622
- References
- 56
- Citations by year
- 2026: 9 · 2025: 7 · 2024: 22 · 2023: 20 · 2022: 19 · 2021: 27 · 2020: 24 · 2019: 24 · 2018: 24 · 2017: 17 · 2016: 23 · 2015: 22 · 2014: 24 · 2013: 25 · 2012: 36
- FWCI
- 8.96
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Funders
- National Institute on Aging (R01AG019519, AG19519)
- National Institute of Allergy and Infectious Diseases (AI 20866, R01AI020866, R37AI020866)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- NADPH oxidase 5, superoxide production, EF-hand motifs, proton channel, pachytene spermatocytes, testis, spleen, lymph nodes, lymphocytes, sperm-oocyte fusion, redox signaling
- MeSH terms
- NADPH Oxidase 5, Amino Acid Sequence, Animals, Calcium, Cytosol, Electrophysiology, HeLa Cells, Humans, Lymph Nodes, Male, Membrane Proteins, Molecular Sequence Data, Protons, Spleen, Superoxides, Testis, Polymerase Chain Reaction, Genome, Ion Transport, Sequence Homology, Amino Acid, In Situ Hybridization, NADPH Oxidases, COS Cells
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