Results 31 to 40 of about 120,483,411 (287)
A Dual Role of Heme Oxygenase-1 in Tuberculosis [PDF]
Frontiers in Immunology, 2022 Iron metabolism is vital for the survival of both humans and microorganisms. Heme oxygenase-1 (HO-1) is an essential stress-response enzyme highly expressed in the lungs, and catabolizes heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV)/bilirubin (BR), especially in pathological conditions which cause oxidative stress and inflammation ...
Sen Yang +4 more
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BMC Complementary and Alternative Medicine, 2011 Background Both resveratrol and vitamin C (ascorbic acid) are frequently used in complementary and alternative medicine. However, little is known about the underlying mechanisms for potential health benefits of resveratrol and its interactions with ...
Hori Osamu +9 more
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Haematologica, 2015 Sickle cell disease is a risk factor for invasive bacterial infections, and splenic dysfunction is believed to be the main underlying cause. We have previously shown that the liberation of heme in acute hemolysis can induce heme oxygenase-1 during ...
Ceri Evans +6 more
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Heme-oxygenases during erythropoiesis in K562 and human bone marrow cells. [PDF]
PLoS ONE, 2011 In mammalian cells, heme can be degraded by heme-oxygenases (HO). Heme-oxygenase 1 (HO-1) is known to be the heme inducible isoform, whereas heme-oxygenase 2 (HO-2) is the constitutive enzyme.
Liliane R Alves +10 more
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Carbon monoxide: from toxin to endogenous modulator of cardiovascular functions
Brazilian Journal of Medical and Biological Research, 1999 Carbon monoxide (CO) is a pollutant commonly recognized for its toxicological attributes, including CNS and cardiovascular effects. But CO is also formed endogenously in mammalian tissues. Endogenously formed CO normally arises from heme degradation in a
R.A. Johnson, F. Kozma, E. Colombari
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Heme oxygenase-1 deletion affects stress erythropoiesis. [PDF]
PLoS ONE, 2011 BACKGROUND:Homeostatic erythropoiesis leads to the formation of mature red blood cells under non-stress conditions, and the production of new erythrocytes occurs as the need arises.
Yu-An Cao +5 more
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Circulation, 2006 Schmid and coworkers1 were the first to report on the presence of heme oxygenase (HO) in liver microsomes capable of degrading heme to bilirubin, and this activity was subsequently dissociated from cytochrome P-450.2,3 HO catalyzes the first and rate-limiting step in the oxidative degradation of heme (Fe-protoporphyrin-IX) to carbon monoxide (CO ...
Roland, Stocker, Mark A, Perrella
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Heme Oxygenase-1 in Tumors: Is It a False Friend? [PDF]
Antioxidants & Redox Signaling, 2007 Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron. It participates in maintaining cellular homeostasis and plays an important protective role in the tissues by reducing oxidative injury, attenuating the inflammatory response, inhibiting cell apoptosis, and ...
Józkowicz, Alicja +2 more
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Human AKI and Heme Oxygenase-1 [PDF]
Journal of the American Society of Nephrology, 2012 Findings derived from animal models of AKI gain clinical credence and appeal when translational studies corroborate their occurrence in human AKI. In the current issue of JASN , Zager et al.
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Ferritin heavy chain mediates the protective effect of heme oxygenase-1 against oxidative stress
, 2017 The phenomenon that heme oxygenase-1 (HO-1) protects cell from injury yet its enzymatic product, iron, may facilitate generation of free radical has been long puzzling. Here we establish a functional connection between ferritin heavy chain (FHC) and HO-1.
Cheng, Hui-Teng;Yen, Chung-Jen;Chang, Chen-Chih;Huang, Kuo-Tong;Chen, Kuo-Hsuan;Zhang, Rui-Yang;Lee, Ping-Yi;Miaw, Shi-Chuen;Huang, Jenq-Wen;Chiang, Chih-Kang;Wu, Kwan-Dun;Hung, Kuan-Yu +1 more
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