The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Mitochondrial Respiratory Chain and NAD(P)H Oxidase Are Targets for theAntiproliferative Effect of Carbon Monoxide in Human Airway SmoothMuscle
Open accessAbstract
Carbon monoxide (CO), one of the end products of heme oxygenase activity, inhibits smooth muscle proliferation by decreasing ERK1/2 phosphorylation and cyclin D1 expression, a signaling pathway that is known to be modulated by reactive oxygen species (ROS) in airway smooth muscle cells (ASMCs). Two important sources of ROS involved in cell signaling are the membrane NAD(P)H oxidase and the mitochondrial respiratory chain. Thus, that CO could modulate redox signaling in ASMCs by interacting with the heme moiety of NAD(P)H oxidase and/or the respiratory chain is a plausible hypothesis. Here we show that a recently identified carbon monoxide-releasing molecule, [Ru(CO)3Cl2]2 (or CORM-2) 1) inhibits NAD(P)H oxidase cytochrome b558 activity, 2) increases oxidant production by the mitochondria, and 3) inhibits ASMC proliferation and phosphorylation of the ERK1/2 mitogen-activated protein kinase and expression of cyclin D1, two critical pathways involved in muscle proliferation. No such effects were observed with the negative control (Ru(Me2SO)4Cl2), which does not contain CO groups. Because both diphenylene iodinium or apocynin (inhibitors of NAD(P)H oxidase) and rotenone (a molecule that increases mitochondrial ROS production by blocking the respiratory chain) mimicked the effect of CORM-2 on cyclin D1 expression and ASMC proliferation, the antiproliferative effect of CORM-2 is probably related to inhibition of cytochromes on both NAD(P)H oxidase and the respiratory chain. The involvement of increased mitochondria-derived oxidants is substantiated by the findings showing that the antioxidant N-acetylcysteine partially inhibited the effects of CORM-2. This study provides a new mechanism to explain redox signaling by CO.
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“These peptides have been shown to mediate protection in animal models of ischemia/reperfusion (922) and insulin resistance (27).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [922]
In the citing paper
“Furthermore, heme oxygenase-1 (HO-1), an antioxidant enzyme upregulated by Nrf2, inhibited NOX2 activation in smooth muscle cells and LPS-stimulated macrophages [171,172].”
From ROS Generation in Microglia: Understanding Oxidative Stress and Inflammation in Neurodegenerative Disease (2020) · cites this paper as [171]
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Cites
1 retracted
Song, R., Mahidhara, R. S., Liu, F., Ning, W., Otterbein, L. E., & Choi, A. M. K. (2002) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.4851 · Cited by 127
RetractedBoveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626
THE HEME OXYGENASE SYSTEM:A Regulator of Second Messenger Gases
Maines, M. D. (1997) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.37.1.517 · Cited by 2,489
Li, N., Ragheb, K., Lawler, G., Sturgis, J., Rajwa, B. P., Melendez, J. A., & Robinson, J. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210432200 · Cited by 1,465
Heme oxygenase-1: unleashing the protective properties of heme
Otterbein, L. E., Soares, M. P., Yamashita, K., & Bach, F. H. (2003) · Trends in Immunology · doi:10.1016/s1471-4906(03)00181-9 · Cited by 1,166
Carbon Monoxide-Releasing Molecules
Motterlini, R., Clark, J., Foresti, R., Sarathchandra, P., Mann, B. E., & Green, C. J. (2002) · Circulation Research · doi:10.1161/hh0202.104530 · Cited by 999
Self-citationBABIOR, B. M., Lambeth, J. D., & Nauseef, W. M. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2642 · Cited by 911
Poderoso, J. J., Carreras, M. C., Lisdero, C., Riobó, N., Schöpfer, F., & Boveris, A. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0146 · Cited by 726
Cardioprotective Actions by a Water-Soluble Carbon Monoxide–Releasing Molecule
Clark, J., NAUGHTON, P. J., Shurey, S., Green, C. J., Johnson, T. R., Mann, B. E., Foresti, R., & Motterlini, R. (2003) · Circulation Research · doi:10.1161/01.res.0000084381.86567.08 · Cited by 676
Self-citationIntracellular hydrogen peroxide and superoxide anion detection in endothelial cells
Carter, W. O., Narayanan, P. K., & Robinson, J. P. (1994) · Journal of Leukocyte Biology · doi:10.1002/jlb.55.2.253 · Cited by 640
Flagged first, then by citations
Research works printed but not linked: 4
- Piantadosi, 2002, Antioxid. RedoxSignal., 4, 259
- Thorup, 1999, Am. J. Physiol., 277, F882
- Johnson, 2003, Am. J. Physiol., 285, R536
- Otterbein, 2002, Antioxid. RedoxSignal., 4, 309
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Sorted by citations
Heme Oxygenase-1/Carbon Monoxide: From Basic Science to Therapeutic Applications
Ryter, S. W., Alam, J., & Choi, A. M. K. (2006) · Physiological Reviews · doi:10.1152/physrev.00011.2005 · Cited by 2,342
The therapeutic potential of carbon monoxide
Motterlini, R., & Otterbein, L. E. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3228 · Cited by 1,643
Self-citationSimpson, D. S. A., & Oliver, P. L. (2020) · Antioxidants · doi:10.3390/antiox9080743 · Cited by 1,044
“Furthermore, heme oxygenase-1 (HO-1), an antioxidant enzyme upregulated by Nrf2, inhibited NOX2 activation in smooth muscle cells and LPS-stimulated macrophages [171,172].”
BackgroundPharmacological and Clinical Aspects of Heme Oxygenase
Abraham, N. G., & Kappas, A. (2008) · Pharmacological Reviews · doi:10.1124/pr.107.07104 · Cited by 1,115
“In particular, CO suppresses the expression of the cdk2 activators, cyclin A and D1, while stimulating the expression of the cdk2 inhibitor, p21 (Taillé et al., 2005; Tulis et al., 2005).”
Sautin, Y. Y., Nakagawa, T., Zharikov, S. I., & Johnson, R. J. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00600.2006 · Cited by 799
“NADPH oxidase activity was measured using the lucigenin-enhanced chemiluminescence method in crude cell homogenates and microsomal membrane fractions by following previously described procedures with minor modifications (15, 54).”
Method
Metadata
- Authors
- Taillé, C., El-Benna, J., Lanone, S., Boczkowski, J., & Motterlini, R.
- Affiliations
- Inserm (FR)
- Northwick Park Institute for Medical Research (GB)
- Corresponding author
- Boczkowski, Jorge
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-07
- Volume
- 280
- Issue
- 27
- Pages
- 25350-25360
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2148052253
- Cited by
- 246
- References
- 44
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 7 · 2023: 4 · 2022: 14 · 2021: 7 · 2020: 7 · 2019: 8 · 2018: 8 · 2017: 11 · 2016: 7 · 2015: 11 · 2014: 6 · 2013: 12 · 2012: 13
- FWCI
- 7.65
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- carbon monoxide, airway smooth muscle, smooth muscle cell proliferation, NADPH oxidase, cytochrome b558, mitochondrial respiratory chain, reactive oxygen species, redox signaling, ERK1/2 phosphorylation, cyclin D1, heme oxygenase, rotenone, apocynin, N-acetylcysteine
- MeSH terms
- Bronchi, Carbon Monoxide, Cell Division, Cells, Cultured, Electron Transport, Humans, Mitochondria, NADH, NADPH Oxidoreductases, Organometallic Compounds, Phosphorylation, Platelet-Derived Growth Factor, NADPH Oxidases, Cyclin D1, Mitogen-Activated Protein Kinase 1, Myocytes, Smooth Muscle, Mitogen-Activated Protein Kinase 3
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