Cited by 127Redox biology and oxidative stressNitric Oxide and Endothelin EffectsAngiogenesis and VEGF in Cancer

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Role of Redox Signaling in the Autonomous Proliferative Response of Endothelial Cells to Hypoxia

Schäfer, M., Schäfer, C., Ewald, N., Piper, H.M., Noll, Th.·2003·Circulation Research

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Abstract

Endothelial cells exhibit an autonomous proliferative response to hypoxia, independent of paracrine effectors. In cultured endothelial cells of porcine aorta, we analyzed the signaling of this response, with a focus on the roles of redox signaling and the MEK/ERK pathway. Transient hypoxia (1 hour) stimulated proliferation by 61±4% (n=16; P <0.05 versus control), quantified after 24 hours normoxic postincubation. Hypoxia induced an activation of ERK2 and of NAD(P)H oxidase and a burst of reactive oxygen species (ROS), determined by DCF fluorescence. To inhibit the MEK/ERK pathway, we used PD 98059 (PD, 20 μmol/L); to downregulate NAD(P)H oxidase, we applied p22 phox antisense oligonucleotides; and to inhibit mitochondrial ROS generation, we used the ubiquinone derivate mitoQ (MQ, 10 μmol/L). All three inhibitions suppressed the proliferative response: PD inhibited NAD(P)H oxidase activation; p22 phox antisense transfection did not inhibit ERK2 activation, but suppressed ROS production; and MQ inhibited ERK2 activation and ROS production. The autonomous proliferative response depends on the MEK/ERK pathway and redox signaling steps upstream and downstream of ERK. Located upstream is ROS generation by mitochondria, downstream is NAD(P)H oxidase.

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Chandel, N. S., Maltepe, E., Goldwasser, E., Mathieu, C. E., Simon, M. C., & Schumacker, P. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11715 · Cited by 1,926
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Baas, A. S., & Berk, B. C. (1995) · Circulation Research · doi:10.1161/01.res.77.1.29 · Cited by 415
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Authors: Schäfer, M., Schäfer, C., Ewald, N., Piper, H. M., & Noll, T.
Affiliations: Justus-Liebig-Universität Gießen (DE)
From the Physiologisches Institut, Justus-Liebig-Universität, Giessen, Germany.
Venue: Circulation Research
Publisher: Ovid Technologies (Wolters Kluwer Health)
Published: 2003-05-16
Volume: 92
Issue: 9
Pages: 1010-1015
ISSN: 0009-7330 (ISSN-L)
1524-4571
DOI: 10.1161/01.res.0000070882.81508.fc
OpenAlex: W2142734267
Cited by: 127
References: 23
Citations by year: 2024: 5 · 2022: 2 · 2020: 4 · 2019: 2 · 2017: 6 · 2016: 7 · 2015: 2 · 2014: 8 · 2013: 5 · 2012: 5
FWCI: 4.27
Type: journal article
Language: en
Open access: closed
Locations: Circulation Research (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
Keywords: endothelial cell proliferation, hypoxia, redox signaling, MEK/ERK signaling, ERK2 activation, NADPH oxidase, reactive oxygen species, mitochondrial reactive oxygen species, p22phox, MitoQ, PD98059, porcine aorta
MeSH terms: Animals, Cell Division, Cells, Cultured, Endothelium, Vascular, Flavonoids, Mitochondria, NAD, NADPH Dehydrogenase, Organophosphorus Compounds, Oxidation-Reduction, Phosphoproteins, Swine, Ubiquinone, Cell Hypoxia, Free Radical Scavengers, Oligonucleotides, Antisense, Reactive Oxygen Species, NADPH Oxidases, Mitogen-Activated Protein Kinase 1, MAP Kinase Signaling System, Membrane Transport Proteins

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Role of Redox Signaling in the Autonomous Proliferative Response of Endothelial Cells to Hypoxia

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