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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Szeto-Schiller peptides mediate protection in animal models of ischemia/reperfusion and insulin resistance.
“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]
HO-1, an antioxidant enzyme upregulated by Nrf2, inhibited NOX2 activation in smooth muscle cells and LPS-stimulated macrophages.
“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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“Other heme-dependent proteins have been shown to be a plausible target of CO, such as nitric oxide synthase (44), cytochrome P-450 (75), NADPH oxidase (115), and fibrinogen (20), but further experiments need to be conducted to confirm their functional role in response to endogenously generated CO.”
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“In airway smooth muscle cells (ASMCs), CO inhibits platelet-derived growth factor (PDGF)-induced proliferation via an increase in mitochondrial ROS and subsequent inhibition of extracellular signal-regulated kinase (ERK) 1/2 phosphorylation and cyclin D1 expression, known to regulate proliferation [22].”
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“The high levels of CO inhibit NOS activity and NO generation, whereas the low concentration of CO induces NO release from either eNOS stimulation or a large intracellular pool of NO (254, 262) (Fig.”
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“Both these potential mechanisms are supported by a recent study in smooth muscle cells showing that CORM increased mitochondrial oxidant production, but at the same time inhibited cytosolic ROS production by inhibiting NADPH oxidase activity at plasma membrane (126).”
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“Heme degradation by HO-1 in microglia generates CO (33), a gasotransmitter that can inhibit NADPH oxidase (55), the main enzyme responsible for microglial ROS production (4) promoting microglial activation during neuroinflammation (7).”
Induction of Heme Oxygenase-1 In Vivo Suppresses NADPH Oxidase–Derived Oxidative Stress
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Self-citationDavidge, K. S., Sanguinetti, G., Yee, C. H., Cox, A. G., McLeod, C. W., Monk, C. E., Mann, B. E., Motterlini, R., & Poole, R. K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808210200 · Cited by 163 · see citing works
Self-citationGalkin, A. S., & Brandt, U. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504709200 · Cited by 162 · see citing works
Iacono, L. L., Boczkowski, J., Zini, R., Salouage, I., Berdeaux, A., Motterlini, R., & Morin, D. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.02.033 · Cited by 160 · see citing works
“Lo Iacono et al. 22”
Self-citationRoderique, J. D., Josef, C. S., Feldman, M. J., & Spiess, B. D. (2015) · Toxicology · doi:10.1016/j.tox.2015.05.004 · Cited by 160 · see citing works
Desmard, M., Davidge, K. S., Bouvet, O. M. M., Morin, D., Roux, D., Foresti, R., Ricard, J. D., Denamur, É., Poole, R. K., Montravers, P., et al. (2008) · The FASEB Journal · doi:10.1096/fj.08-122804 · Cited by 155 · see citing works
Self-citationA Central Role of Heme Oxygenase-1 in Cardiovascular Protection
Wu, M., Ho, Y., & Yet, S. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3726 · Cited by 154 · see citing works
“Since nicotinamide adenine di-nucleotide phosphate oxidase is an important source of ROS generation (84), it is not surprising that the effect of HO-1/CO on inhibiting PDGF-induced VSMC migration is mediated by inhibition of nicotinamide adenine dinucleotide phosphate oxidase (74).”
Carbon monoxide: Mechanisms of action and potential clinical implications
Rochette, L., Cottin, Y., Zeller, M., & Vergely, C. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.09.007 · Cited by 145 · see citing works
Role of carbon monxide in cardiovascular function
Durante, W., Johnson, F. K., & Johnson, R. A. (2006) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2006.tb00427.x · Cited by 145 · see citing works
“CO blocks the phosphorylation and activation of the mitogen-activated protein kinase (MAPK), ERK1/2, via its inhibitory effect on the mitochondrial respiratory chain [34].”
BackgroundProtective effect of carbon monoxide in transplantation
Nakao, A., Choi, A. M. K., & Murase, N. (2006) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2006.tb00426.x · Cited by 141 · see citing works
McCarty, M. F. (2007) · Medical Hypotheses · doi:10.1016/j.mehy.2006.12.069 · Cited by 137 · see citing works
“Moreover, the concurrently generated CO may contribute at least modestly to this inhibition of NADPH oxidase [106].”
BackgroundCarbon monoxide in lung cell physiology and disease
Ryter, S. W., Ma, K. C., & Choi, A. M. K. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00022.2017 · Cited by 135 · see citing works
“Inhibition of NOXdependent reactive oxygen species (ROS) generation has been attributed to anti-inflammatory (109), antiproliferative (161), and antiapoptotic (178) effects of CO.”
BackgroundMethodInfluentialSrisook, K., Han, S.-S., Choi, H.-S., Li, M., UEDA, H. M. D., Kim, C., & Cha, Y. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.10.042 · Cited by 134 · see citing works
Scragg, J. L., Dallas, M. L., Wilkinson, J. A., Varadi, G., & Peers, C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803037200 · Cited by 133 · see citing works
Carbon Monoxide Activates Autophagy via Mitochondrial Reactive Oxygen Species Formation
Lee, S., Ryter, S. W., Xu, J., Nakahira, K., Kim, H. P., Choi, A. M. K., & Kim, Y. S. (2011) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2010-0352oc · Cited by 131 · see citing works
A Review on Hemeoxygenase-2: Focus on Cellular Protection and Oxygen Response
Muñoz‐Sánchez, J., & Chánez‐Cárdenas, M. E. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/604981 · Cited by 132 · see citing works
“Actually, it has been suggested that modulation of HO-1 expression and activity could have a potential therapeutic value [11–15].”
BackgroundTreatment with CO-RMs during cold storage improves renal function at reperfusion
Sandouka, A., Fuller, B. J., MANN, B. E., Green, C. J., Foresti, R., & Motterlini, R. (2006) · Kidney International · doi:10.1038/sj.ki.5000016 · Cited by 130 · see citing works
Self-citationMitochondria-Derived Reactive Oxygen Species Dilate Cerebral Arteries by Activating Ca 2+ Sparks
Xi, Q., Cheranov, S. Y., & Jaggar, J. H. (2005) · Circulation Research · doi:10.1161/01.res.0000177669.29525.78 · Cited by 127 · see citing works
Therapeutic Antioxidant Medical Gas
Nakao, A., Sugimoto, R., Billiar, T. R., & McCurry, K. R. (2009) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.08-193r · Cited by 123 · see citing works
“Recently, our group demonstrated that CO in the organ preservation solution used during transplantation can bind to and stabilize renal CYP and prevent CYP degradation and detrimental heme/iron release in renal grafts.”
BackgroundHasan, R. N., & Schafer, A. I. (2007) · Circulation Research · doi:10.1161/circresaha.107.155143 · Cited by 124 · see citing works
Backer, O. D., Elinck, E., Blanckaert, B., Leybaert, L., Motterlini, R., & Lefebvre, R. A. (2008) · Gut · doi:10.1136/gut.2008.155481 · Cited by 123 · see citing works
Self-citationProtection against cisplatin-induced nephrotoxicity by a carbon monoxide-releasing molecule
Tayem, Y. I., Johnson, T. R., Mann, B. E., Green, C. J., & Motterlini, R. (2005) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00363.2005 · Cited by 122 · see citing works
“Because apoptosis caused by CP is associated with an increased production of free radicals (33), we cannot exclude a priori that the antiapoptotic effects of CORM-3 may also involve the suppression of crucial pathways that trigger oxidative stress (31).”
BackgroundSelf-citationCarbon Monoxide: An Essential Signalling Molecule
Mann, B. E. (2010) · Topics in organometallic chemistry · doi:10.1007/978-3-642-13185-1_10 · Cited by 121 · see citing works
Desmard, M., Foresti, R., Morin, D., Dagouassat, M., Berdeaux, A., Denamur, É., Crook, S. H., Mann, B. E., Scapens, D., Montravers, P., et al. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3959 · Cited by 121 · see citing works
“On the other hand, small amounts of CO can either induce preconditioning through ROS signaling (20) or decrease ROS generation by NADPH oxidase (39), thus playing a role of arbiter in the process of cell survival and death (7, 5, 42).”
Self-citationCarbon monoxide: an emerging regulator of ion channels
Wilkinson, W. J., & Kemp, P. J. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.206706 · Cited by 121 · see citing works
“…leading to the cellular generation of cGMP (Brune & Ullrich, 1987); (ii) inhibition of reduced nicotinamide adenine dinucleotide (NADPH) oxidase (Taille et al. 2005); and (iii) inhibition of cytochrome c oxidase (for recent review see Pun et al. 2010), thus altering the redox state of the cell.”
BackgroundTargeting Heme Oxygenase-1 in Vascular Disease
Durante, W. (2010) · Current Drug Targets · doi:10.2174/1389450111009011504 · Cited by 115 · see citing works
“However, CO may also contribute to the antioxidant actions of HO-1 by stimulating the expression of antioxidant genes and inhibiting the activity of pro-oxidant enzymes [42,43].”
BackgroundProtective Functions of Heme Oxygenase-1 and Carbon Monoxide in the Respiratory System
Ryter, S. W., Kim, H. P., Nakahira, K., Zuckerbraun, B. S., Morse, D., & Choi, A. M. K. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1811 · Cited by 114 · see citing works
“…involve the downregulation of endothelial cell–derived mitogenic factors, and the down-regulation of the NADPH oxidase-dependent ERK1/2 pathway (66, 113). cells, which can produce a strong HO-1 response to proinflammatory stimuli, may represent a major source of endogenous CO production in the…”
InfluentialHyperinsulinemia adversely affects lung structure and function
Singh, S., Bodas, M., Bhatraju, N. K., PATTNAIK, B. R., Gheware, A., Parameswaran, P. K., Thompson, M., Freeman, M., Mabalirajan, U., Gosens, R., et al. (2016) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00091.2015 · Cited by 113 · see citing works
Carbon monoxide and mitochondria—modulation of cell metabolism, redox response and cell death
Almeida, A. S., Figueiredo-Pereira, C., & Vieira, H. L. A. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00033 · Cited by 111 · see citing works
“In airway smooth muscle cells, CORM2 limits cell proliferation via ROS generation due to a decrease on COX activity (Taillé et al., 2005).”
BackgroundLi, M., Jang, J.-H., Na, H., Cha, Y., & Surh, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701916200 · Cited by 109 · see citing works
Carbon Monoxide Modulates Apoptosis by Reinforcing Oxidative Metabolism in Astrocytes
Almeida, A. S., Queiroga, C. S. F., Sousa, M. F. Q., Alves, P. M., & Vieira, H. L. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.306738 · Cited by 104 · see citing works
Ruthenium Complexes in the Fight against Pathogenic Microorganisms. An Extensive Review
Munteanu, A.-C., & Uivaroși, V. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13060874 · Cited by 86 · see citing works
Carbon monoxide: present and future indications for a medical gas
Ryter, S. W., & Choi, A. M. K. (2013) · The Korean Journal of Internal Medicine · doi:10.3904/kjim.2013.28.2.123 · Cited by 99 · see citing works
“Additional signaling mechanisms potentially involved in CO-dependent regulation of cell proliferation, include the regulation of the lipid-raft associated signaling protein caveolin-1 [112], and modulation of NADPH oxidase [113].”
BackgroundThe Heme Oxygenase/Biliverdin Reductase Pathway in Drug Research and Development
Mancuso, C., & Barone, E. (2009) · Current Drug Metabolism · doi:10.2174/138920009789375405 · Cited by 98 · see citing works
“human smooth muscle cells [91,92].”
BackgroundAmara, N., Bachoual, R., Desmard, M., Gołda, S., Guichard, C., Lanone, S., Aubier, M., Ogier‐Denis, É., & Boczkowski, J. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00445.2006 · Cited by 98 · see citing works
“Intracellular ROS production was quantified by measuring 2 ,7 -dichlorodihydrofluorescein diacetate (H2DCFH-DA) oxidation as described previously (42).”
MethodSelf-citationCarbon Monoxide Targeting Mitochondria
Queiroga, C. S. F., Almeida, A. S., & Vieira, H. L. A. (2012) · Biochemistry Research International · doi:10.1155/2012/749845 · Cited by 93 · see citing works
“in airway smooth muscle cells [52], and (iv) induction of mitochondrial biogenesis in cardiomyocytes [31].”
BackgroundPre‐conditioning induced by carbon monoxide provides neuronal protection against apoptosis
Vieira, H. L. A., Queiroga, C. S. F., & Alves, P. M. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05610.x · Cited by 92 · see citing works
Franke, P. T., Johansen, R. L., Bertelsen, S., & Jørgensen, K. A. (2007) · Chemistry - An Asian Journal · doi:10.1002/asia.200700360 · Cited by 89 · see citing works
Emerging concepts on the anti-inflammatory actions of carbon monoxide-releasing molecules (CO-RMs)
Motterlini, R., Haas, B., & Foresti, R. (2012) · Medical Gas Research · doi:10.1186/2045-9912-2-28 · Cited by 86 · see citing works
“CO-RMs have shown a tendency to modulate pathways that produce ROS and the chemical nature of transition metal carbonyls might favour this reaction by allowing a selective transfer of CO from the CO-RMs to the target [78,79].”
BackgroundOxidative stress targets in pulmonary emphysema: focus on the Nrf2 pathway
Boutten, A., Goven, D., Boczkowski, J., & Bonay, M. (2010) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728221003629750 · Cited by 87 · see citing works
“Thiol compounds N-acetylcysteine " GSH production, # H2O2 exhaled, # NF-kB activation, # Exacerbations [117-120,139] Carbocysteine # Exacerbations, # Inflammatory cells recruitment [121,139] N-acystelyn " GSH production, # H2O2 and O2- released from human blood derived neutrophils [139] Erdosteine # Exacerbations [139…”
BackgroundInfluentialSelf-citationNguyen, D., & Boyer, C. A. (2015) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.5b00230 · Cited by 86 · see citing works
The Microbiology of Ruthenium Complexes
Southam, H. M., Butler, J. A., Chapman, J. A., & Poole, R. K. (2017) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2017.03.001 · Cited by 84 · see citing works
Protective role of heme oxygenase-1 against inflammation in atherosclerosis
Durante, W. (2011) · Frontiers in bioscience · doi:10.2741/3860 · Cited by 83 · see citing works
“Finally, CO may further enhance the antioxidant actions of HO-1 by inducing the expression of antioxidant genes while blocking the activity of pro-oxidant enzymes (56,57).”
BackgroundBioactive Properties of Iron-Containing Carbon Monoxide-Releasing Molecules
Sawle, P., Hammad, J., Fairlamb, I. J. S., Moulton, B. E., O'Brien, C. T., Lynam, J. M., Duhme‐Klair, A., Foresti, R., & Motterlini, R. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.101758 · Cited by 83 · see citing works
“In addition, CO-RMs may be used as an expedient to identify and elucidate new mechanisms mediated by CO (Chatterjee, 2004; Sandouka et al., 2005; Taille et al., 2005), and an increasing number of reports substantiate the feasibility of this new approach (Jozkowicz et al.”
BackgroundSelf-citationEnhancement of tolerance of Indian mustard (Brassica juncea) to mercury by carbon monoxide
Meng, D. K., Chen, J., & Yang, Z. M. (2010) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2010.12.062 · Cited by 81 · see citing works
Peterson, S. J., & Frishman, W. H. (2009) · Cardiology in Review · doi:10.1097/crd.0b013e31819d813a · Cited by 79 · see citing works
“In particular, CO suppresses the expression of the cdk2 activators, cyclin A and D1, while stimulating the expression of the cdk2 inhibitor, p21.(89,142,143) The antiproliferative action of CO appears to be mediated by the sGC/cGMP pathway because inhibitors of GC and protein kinase C restored SMC growth.”
BackgroundTakagi, T., Naito, Y., Uchiyama, K., Suzuki, T., Hirata, I., Mizushima, K., Tsuboi, H., Hayashi, N., Handa, O., Ishikawa, T., et al. (2010) · Digestive Diseases and Sciences · doi:10.1007/s10620-010-1484-y · Cited by 78 · see citing works
“CORMderived CO has been shown to exert vasorelaxant [21], anti-proliferative [22], cytoprotective [23], tissue-remodeling [24], and anti-inflammatory effects [25].”
BackgroundKim, H. S., Loughran, P., Rao, J., Billiar, T. R., & Zuckerbraun, B. S. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00105.2007 · Cited by 76 · see citing works
“Both endogenous and exogenous CO have previously been shown to increase cellular ROS generation (5, 42).”
BackgroundVera, T., Kelsen, S., Yanes, L. L., Reckelhoff, J. F., & Stec, D. E. (2006) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00601.2006 · Cited by 75 · see citing works
“While CO is not traditionally thought of as a antioxidant, it can bind to the heme group on NADPH oxidase, as well as mitochondrial respiratory chain enzymes, to decrease superoxide production (32).”
BackgroundCerebroprotective Functions of HO-2
Parfenova, H., & Leffler, C. W. (2008) · Current Pharmaceutical Design · doi:10.2174/138161208783597380 · Cited by 75 · see citing works
Carbon monoxide: A vital signalling molecule and potent toxin in the myocardium
Peers, C., & Steele, D. S. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.05.013 · Cited by 74 · see citing works
“Since CO has been shown to inhibit this oxidase in macrophages and airway smooth muscle cells [49,57], it will be of interest to examine whether CO may be cardioprotective via inhibition of cardiac isoforms of NADPH oxidase.”
BackgroundBauer, N., Yuan, Z., Yang, X., & Wang, B. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115642 · Cited by 71 · see citing works
Diverse mechanisms underlying the regulation of ion channels by carbon monoxide
Peers, C., Boyle, J. P., Scragg, J. L., Dallas, M. L., Al‐Owais, M. M., Hettiarachichi, N. T., Elíes, J., Johnson, E., Gamper, N. L., & Steele, D. S. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12760 · Cited by 69 · see citing works
“…oxidase (Nox) family of proteins, which are a widely distributed source of ROS required in numerous signalling pathways, can also be inhibited by CO, with significant consequences: for example, inhibition of Nox2 contributes to inhibition of airway smooth muscle proliferation (Taille et al., 2005).”
BackgroundBeneficial effects of carbon monoxide-releasing molecules on post-ischemic myocardial recovery
Váradi, J., Lekli, I., Juhász, B., Bácskay, I., Szabo, G., Gesztelyi, R., Szendrei, L., Varga, E., Bak, I., Foresti, R., et al. (2007) · Life Sciences · doi:10.1016/j.lfs.2007.01.047 · Cited by 67 · see citing works
Self-citationCarbon Monoxide Rapidly Impairs Alveolar Fluid Clearance by Inhibiting Epithelial Sodium Channels
Althaus, M., Fronius, M., Buchäckert, Y., Vadász, I., Clauss, W. G., Seeger, W., Motterlini, R., & Morty, R. E. (2009) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2008-0458oc · Cited by 66 · see citing works
Self-citationProtective effects of a carbon monoxide-releasing molecule (CORM-3) during hepatic cold preservation
Pizarro, M. D., Rodriguez, J. V., Mamprin, M. E., Fuller, B. J., MANN, B. E., Motterlini, R., & Guibert, E. E. (2009) · Cryobiology · doi:10.1016/j.cryobiol.2009.01.002 · Cited by 65 · see citing works
Self-citationKohmoto, J., Nakao, A., Sugimoto, R., Wang, Y., Zhan, J., UEDA, H. M. D., & McCurry, K. R. (2008) · Journal of Thoracic and Cardiovascular Surgery · doi:10.1016/j.jtcvs.2008.06.026 · Cited by 64 · see citing works
Carbon monoxide and the eye: Implications for glaucoma therapy
Bucolo, C., & Drago, F. (2011) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.01.013 · Cited by 63 · see citing works
“CO can exhibit cell-specific anti-inflammatory (Sato et al., 2001; Motterlini et al., 2003), anti-proliferative (Taille et al., 2005), and anti- on of the heme pathway. apoptotic (Zhang et al., 2005) effects by physiological mechanisms that are still largely undetermined.”
Faizan, M., Muhammad, N., Niazi, K. U. K., Hu, Y., Wang, Y., Wu, Y., Sun, H., Liu, R., Dong, W., Zhang, W., et al. (2019) · Materials · doi:10.3390/ma12101643 · Cited by 62 · see citing works
“It has a modulated utility for heme-dependent proteins like mitochondrial cytochromes and NADPH [28,41].”
BackgroundAfonso, V., Santos, G. M., Collin, P., Khatib, A., Mitrovic, D. R., Lomri, N., Leitman, D. C., & Lomri, A. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.05.014 · Cited by 62 · see citing works
Yao, P., Hao, L., Nüssler, N. C., Lehmann, A., Song, F., Zhao, J., Neuhaus, P., Liu, L., & Nussler, A. K. (2009) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00555.2007 · Cited by 61 · see citing works
“Ruthenium-containing CO-releasing compound (tricarbonyldichlororuthenium dimmer, CORM-2) has been confirmed to possess similar effects as a gas as CO administration, which provides a useful tool to study the mechanism of CO action (33).”
BackgroundCheng, S.-E., Luo, S., Jou, M., Lin, C., Kou, Y. R., Lee, I., Hsieh, H., & Yang, C. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.01.006 · Cited by 60 · see citing works
Lipid Autacoids in Inflammation and Injury Responses: A Matter of Privilege
Gronert, K. (2008) · Molecular Interventions · doi:10.1124/mi.8.1.7 · Cited by 59 · see citing works
Rousset, F., Nguyen, M. V. C., Grange, L., Morel, F., & Lardy, B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066478 · Cited by 59 · see citing works
“During Nox2 maturation, heme is incorporated into a 65 kDa precursor allowing its dimerization with the stabilizing subunit p22phox [25].”
BackgroundInfluentialHeme Oxygenase-2 (HO-2) as a therapeutic target: Activators and inhibitors
Intagliata, S., Salerno, L., Ciaffaglione, V., Leonardi, C., Fallica, A. N., Carota, G., Amata, E., Marrazzo, A., Pittalà, V., & Romeo, G. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111703 · Cited by 59 · see citing works
- 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 › 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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