Reference : Quinone compounds regulate the level of ROS production by the NADPH oxidase Nox4

	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/10993/27260

Title :	Quinone compounds regulate the level of ROS production by the NADPH oxidase Nox4
Language :	English
Author, co-author :	Nguyen, Minh Vu Chong [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit]
	Lardy, Bernard [Université Joseph Fourier, GREPI AGIM FRE 3405, CNRS, 38043 Grenoble, France, Laboratoire de Biochimie Enzyme et Protéine-DBTP, Institut de Biologie et de Pathologie, University Hospital CHU-Grenoble, Grenoble, France]
	Rousset, Francis [Université Joseph Fourier, GREPI AGIM FRE 3405, CNRS, 38043 Grenoble, France]
	Hazane-Puch, Florence [Laboratoire de Biochimie Hormonale et Nutritionnelle-DBTP, Institut de Biologie et de Pathologie, University Hospital CHU-Grenoble, Grenoble, France]
	Zhang, Leilei [Université Joseph Fourier, GREPI AGIM FRE 3405, CNRS, 38043 Grenoble, France]
	Trocmé, Candice [Laboratoire de Biochimie Enzyme et Protéine-DBTP, Institut de Biologie et de Pathologie, University Hospital CHU-Grenoble, Grenoble, France]
	Serrander, Lena [Department of Clinical Microbiology, University Hospital, Linkoping, Sweden]
	Krause, Karl-Heinz [Department of Pathology and Immunology, Medical Faculty, University Hospital, Geneva, Switzerland]
	Morel, Françoise [Université Joseph Fourier, GREPI AGIM FRE 3405, CNRS, 38043 Grenoble, France]
Publication date :	2013
Journal title :	Biochemical Pharmacology
Volume :	85
Issue/season :	11
Pages :	1644-1654
Peer reviewed :	Yes (verified by ORBilu)
Audience :	International
ISSN :	00062952
Keywords :	[en] NAD(P)H:quinone oxidoreductase NQO1 ; NADPH oxidase Nox4 ; Quinones ; Reactive oxygen species (ROS) ; Redox regulation of Nox ; Western blotting ; Amino Acid Sequence ; Base Sequence ; Benzoquinones ; Blotting, Western ; Calcium ; Cell Line ; DNA Primers ; Electrophoresis, Polyacrylamide Gel ; Enzyme Activation ; Humans ; L-Lactate Dehydrogenase ; Luminescence ; Molecular Sequence Data ; NADPH Oxidase ; Oxidation-Reduction ; Reactive Oxygen Species ; Real-Time Polymerase Chain Reaction ; Transcription, Genetic
Abstract :	[en] NADPH oxidase Nox4 is expressed in a wide range of tissues and plays a role in cellular signaling by providing reactive oxygen species (ROS) as intracellular messengers. Nox4 oxidase activity is thought to be constitutive and regulated at the transcriptional level; however, we challenge this point of view and suggest that specific quinone derivatives could modulate this activity. In fact, we demonstrated a significant stimulation of Nox4 activity by 4 quinone derivatives (AA-861, tBuBHQ, tBuBQ, and duroquinone) observed in 3 different cellular models, HEK293E, T-REx™, and chondrocyte cell lines. Our results indicate that the effect is specific toward Nox4 versus Nox2. Furthermore, we showed that NAD(P)H:quinone oxidoreductase (NQO1) may participate in this stimulation. Interestingly, Nox4 activity is also stimulated by reducing agents that possibly act by reducing the disulfide bridge (Cys226, Cys270) located in the extracellular E-loop of Nox4. Such model of Nox4 activity regulation could provide new insight into the understanding of the molecular mechanism of the electron transfer through the enzyme, i.e., its potential redox regulation, and could also define new therapeutic targets in diseases in which quinones and Nox4 are implicated. © 2013 Elsevier Inc. All rights reserved.
Permalink :	http://hdl.handle.net/10993/27260
DOI :	10.1016/j.bcp.2013.03.023

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