2019
DOI: 10.3390/antiox8100475
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Role of Heme Oxygenase as a Modulator of Heme-Mediated Pathways

Abstract: The heme oxygenase (HO) system is essential for heme and iron homeostasis and necessary for adaptation to cell stress. HO degrades heme to biliverdin (BV), carbon monoxide (CO) and ferrous iron. Although mostly beneficial, the HO reaction can also produce deleterious effects, predominantly attributed to excessive product formation. Underrated so far is, however, that HO may exert effects additionally via modulation of the cellular heme levels. Heme, besides being an often-quoted generator of oxidative stress, … Show more

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Cited by 75 publications
(55 citation statements)
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References 238 publications
(282 reference statements)
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“…Biliverdin is rapidly reduced by biliverdin reductase to produce bilirubin, which can effectively remove peroxyl radicals, thereby inhibiting LPO, attenuating heme-induced oxidative stress, cell activation, and death [ 55 ]. Likewise, the released carbon monoxide activates nuclear factor E2-related factor 2 (Nrf2) signaling, promoting the endogenous antioxidant availability and increasing HO-1 levels [ 58 ]. On the other hand, ROS stimulate ferritin synthesis and iron sequestration, being essential for proper iron homeostasis [ 55 ].…”
Section: Meat Consumption As a Source Of Oxidative Stressmentioning
confidence: 99%
“…Biliverdin is rapidly reduced by biliverdin reductase to produce bilirubin, which can effectively remove peroxyl radicals, thereby inhibiting LPO, attenuating heme-induced oxidative stress, cell activation, and death [ 55 ]. Likewise, the released carbon monoxide activates nuclear factor E2-related factor 2 (Nrf2) signaling, promoting the endogenous antioxidant availability and increasing HO-1 levels [ 58 ]. On the other hand, ROS stimulate ferritin synthesis and iron sequestration, being essential for proper iron homeostasis [ 55 ].…”
Section: Meat Consumption As a Source Of Oxidative Stressmentioning
confidence: 99%
“…Human heme catabolism is accomplished by the inducible heme oxigenase (HO-1) and, likely to a lesser extent, by the constitutional HO-2 (Duvigneau et al 2019). HO-1 metabolizes the heme group of a variety of hemeproteins including myoglobin, neuroglobin, cytochrome c, cytochrome p450, nitric oxide synthases, and guanylate cyclase.…”
Section: Heme Oxygenase 1 (Ho-1) Carbon Monoxide (Co) and Heme Metabmentioning
confidence: 99%
“…HO-1 expression, but not HO-2, is increased in cultured VSM and endothelial cells in response to various stress stimuli ( Christodoulides et al, 1995 ). Similar to SirT1, HO-1 overexpression serves a protective role by virtue of anti-oxidant ( Ferrandiz and Devesa, 2008 ; Bonacasa et al, 2013 ), anti-inflammatory ( Lee et al, 2004 ), anti-apoptotic ( Ferrandiz and Devesa, 2008 ), and anti-proliferative ( Deng et al, 2004 ; Lee et al, 2004 ) effects in endothelial, smooth muscle cells and macrophages in the vascular wall ( Kim et al, 2011 ), by increasing CO and/or biliverdin production or by reducing the pro-oxidant heme levels ( Abraham and Kappas, 2005 ; Duvigneau et al, 2019 ). Like SirT1, HO-1 confers protection in several vascular injury models, such us ischemic heart disease, atherosclerosis, hypertension, diabetes, or vascular proliferative diseases ( Abraham and Kappas, 2005 ; Loboda et al, 2008 ; Kim et al, 2011 ).…”
Section: Sirt1 and Ho-1 In Aortic Aneurysmmentioning
confidence: 99%