Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases

Martyn, Kendra D.; Frederick, Linda M.; von Loehneysen, Katharina; Dinauer, Mary C.; Knaus, Ulla G.

doi:10.1016/j.cellsig.2005.03.023

Cited by 784Redox biology and oxidative stressNeutrophil, Myeloperoxidase and Oxidative MechanismsNitric Oxide and Endothelin Effects

Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases

Martyn, Kendra D., Frederick, Linda M., von Loehneysen, Katharina, Dinauer, Mary C., Knaus, Ulla G.·2006·Cellular Signalling

DOI 10.1016/j.cellsig.2005.03.023

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Abstract

Reactive oxygen species (ROS) are important signal transduction molecules in ligand-induced signaling, regulation of cell growth, differentiation, apoptosis and motility. Recently NADPH oxidases (Nox) homologous to Nox2 (gp91phox) of phagocyte cytochrome b558 have been identified, which are an enzymatic source for ROS generation in epithelial cells. This study was undertaken to delineate the requirements for ROS generation by Nox4. Nox4, in contrast to other Nox proteins, produces large amounts of hydrogen peroxide constitutively. Known cytosolic oxidase proteins or the GTPase Rac are not required for this activity. Nox4 associates with the protein p22phox on internal membranes, where ROS generation occurs. Knockdown and gene transfection studies confirmed that Nox4 requires p22phox for ROS generation. Mutational analysis revealed structural requirements affecting expression of the p22phox protein and Nox activity. Mechanistic insight into ROS regulation is significant for understanding fundamental cell biology and pathophysiological conditions.

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NOX4 is distinct from NOX2 in its ability to generate directly both O2•− and H2O2.
“NOX4 is distinct from NOX2 in its ability to generate directly both O2•− and H2O2 (25).”
From Skeletal muscle NOX4 is required for adaptive responses that prevent insulin resistance (2021) · cites this paper as [25]

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Authors: Martyn, K. D., Frederick, L. M., von Loehneysen, K., Dinauer, M. C., & Knaus, U. G.
Affiliations: Scripps Research Institute (US)
Indiana University Indianapolis (US)
Corresponding author: Knaus, Ulla G.
ORCID: Dinauer, Mary C.
Knaus, Ulla G.
Venue: Cellular Signalling
Publisher: Elsevier BV
Published: 2006-01
Volume: 18
Issue: 1
Pages: 69-82
ISSN: 0898-6568 (ISSN-L)
DOI: 10.1016/j.cellsig.2005.03.023
OpenAlex: W1971215115
Cited by: 783
References: 53
Citations by year: 2026: 14 · 2025: 17 · 2024: 20 · 2023: 29 · 2022: 22 · 2021: 18 · 2020: 27 · 2019: 38 · 2018: 32 · 2017: 36 · 2016: 40 · 2015: 44 · 2014: 52 · 2013: 62 · 2012: 50
FWCI: 16.75
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cellular Signalling (publishedVersion)
PubMed (publishedVersion)
Funders: National Heart, Lung, and Blood Institute (HL 45635, R01HL045635)
National Cancer Institute (CA-84138, R01CA084138)
National Institute of General Medical Sciences (GM 37696, P01GM037696)
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: NOX4, NADPH oxidase, reactive oxygen species, hydrogen peroxide, p22phox, gp91phox, epithelial cells, protein association, gene knockdown, mutation analysis
MeSH terms: NADPH Oxidase 4, Animals, Cell Line, Cell Membrane, Chlorocebus aethiops, Cytosol, DNA Mutational Analysis, Epithelial Cells, Gene Expression Regulation, Humans, Hydrogen Peroxide, Phosphoproteins, Signal Transduction, Reactive Oxygen Species, NADPH Oxidases, COS Cells, rac GTP-Binding Proteins, Membrane Transport Proteins

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Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases

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