Biliverdin reductase activity in cattle, sheep, rabbits and rats

George, Jeanne W.; Nulk, Kathryn; Weiss, Andrew; Brüss, Michael; Cornelius, Charles E.

doi:10.1016/0020-711x(89)90127-4

Cited by 15 publications

(9 citation statements)

References 18 publications

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“…Three mammalian isoforms of HO have been identified: HO-1, an inducible enzyme that is most highly concentrated in the tissues that are heavily involved in the catabolism of heme proteins (22); HO-2, a non-inducible isoform that is present at the highest concentrations in the brain and testes, and it is thought to be particularly involved in signaling pathways (23); and HO-3, an isoform with low catalytic activity and an uncertain physiological role (24). HO uses dioxygen and nicotinamide- adenine dinucleotide phosphate as cofactors, and the resulting products of the reaction are carbon monoxide, iron and biliverdin (21).…”

Section: Discussionmentioning

confidence: 99%

“…HO uses dioxygen and nicotinamide- adenine dinucleotide phosphate as cofactors, and the resulting products of the reaction are carbon monoxide, iron and biliverdin (21). Biliverdin is converted to bilirubin by a ubiquitous cytosolic enzyme biliverdin reductase (22). Both HO-2 and an inducible HO-1 have been identified in rat pancreatic islets (23-25), as well as in other tissues (26).…”

Section: Discussionmentioning

confidence: 99%

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A Protective Role for Heme Oxygenase-1 in INS-1 Cells and Rat Islets that are Exposed to High Glucose Conditions

et al. 2006

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Heme oxygenase-1 (HO-1) has been described as an inducible protein that is capable of cytoprotection via radical scavenging and the prevention of apoptosis. Chronic exposure to hyperglycemia can lead to cellular dysfunction that may become irreversible over time, and this process has been termed glucose toxicity. Yet little is known about the relation between glucose toxicity and HO-1 in the islets. The purposes of the present study were to determine whether prolonged exposure of pancreatic islets to a supraphysiologic glucose concentration disrupts the intracellular balance between reactive oxygen species (ROS) and HO-1, and so this causes defective insulin secretion; we also wanted to evaluate a protective role for HO-1 in pancreatic islets against high glucose levels. The intracellular peroxide levels of the pancreatic islets (INS-1 cell, rat islet) were increased in the high glucose media (30 mM glucose or 50 mM ribose). The HO-1 expression was induced in the INS-1 cells by the high glucose levels. Both the HO-1 expression and glucose stimulated insulin secretion (GSIS) was decreased simultaneously in the islets by treatment of the HO-1 antisense. The HO-1 was upregulated in the INS-1 cells by hemin, an inducer of HO-1. And, HO-1 upregulation induced by hemin reversed the GSIS in the islets at a high glucose condition. These results suggest HO-1 seems to mediate the protective response of pancreatic islets against the oxidative stress that is due to high glucose conditions.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

A Protective Role for Heme Oxygenase-1 in INS-1 Cells and Rat Islets that are Exposed to High Glucose Conditions

et al. 2006

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“…In rabbits, antioxidative effects of HO-1 on lipoproteins may be attributed to biliverdin, because relatively lower activity of biliverdin reductase has been reported previously. 34 Further experiments to determine which products of HO-1 are predominantly responsible for antiatherogenesis are also needed.…”

Section: Discussionmentioning

confidence: 99%

Heme Oxygenase-1 Inhibits Atherogenesis in Watanabe Heritable Hyperlipidemic Rabbits

et al. 2001

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Background-Heme oxygenase-1 (HO-1) is proposed to have a variety of adaptive responses against oxidative stress. To examine the function of HO-1 against atherogenesis in vivo, we observed the effects of HO-1 inhibition on atherosclerotic lesion formation in Watanabe heritable hyperlipidemic rabbits (WHHL). Methods and Results-During 4 weeks of a 1% cholesterol diet, intravenous injections of Sn-protoporphyrin IX to inhibit HO-1 (S group, nϭ10) and saline as a control (C group, nϭ10) were given to 3-month-old WHHL rabbits. The percentages of en face atherosclerotic lesion areas in total descending aorta by Sudan IV staining (EFA) and the ratio of intima to media in microscopic atherosclerotic lesions in the ascending aortas (I/M) were calculated. Two different quantitative methods revealed significantly greater atherosclerotic lesions in the S group than the C group (EFA, PϽ0.001; I/M, PϽ0.005). HO-1 expression in atherosclerotic lesions was confirmed by Northern blot and immunohistochemical analyses. The dominant cell types expressing HO-1 were macrophages and foam cells, in which oxidized phospholipids were also accumulated. HO inhibition increased plasma and tissue lipid peroxide levels without affecting plasma lipid composition. Conclusions-These results suggest the possibilities that HO-1 has antiatherogenic properties in vivo and that the antiatherogenic properties of HO-1 are conducted through the prevention of lipid peroxidation.

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“…In mammals, biliverdin reductase then converts biliverdin to bilirubin (Fig. 1), 5 that undergoes conjugation and further modification before eventual secretion in urine and feces. 6 There are considerable variations in the number of HO isoforms in different species.…”

Section: Enzymology Of Heme Oxygenasementioning

confidence: 99%

Heme oxygenase and iron: from bacteria to humans

Stocker

2009

Redox Report

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Iron and iron-containing prosthetic groups are involved in many fundamental processes that constitute life. One of the biologically most important iron-containing groups is heme, in which an iron atom is co-ordinated to a protoporphyrin ring. Heme proteins have a wide range of functions, participating in a vast repertoire of biochemical reactions. Due to its abundance, heme also serves as an important source of iron. Enzymatic degradation of heme usually involves its oxidative cleavage by heme oxygenase. Not surprisingly, heme oxygenase activity is present in organisms across different domains and kingdoms. This review summarises the current knowledge in the dynamic relationship between heme oxygenase and iron in metabolism and in the clinical context.

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Biliverdin reductase activity in cattle, sheep, rabbits and rats

Cited by 15 publications

References 18 publications

A Protective Role for Heme Oxygenase-1 in INS-1 Cells and Rat Islets that are Exposed to High Glucose Conditions

A Protective Role for Heme Oxygenase-1 in INS-1 Cells and Rat Islets that are Exposed to High Glucose Conditions

Heme Oxygenase-1 Inhibits Atherogenesis in Watanabe Heritable Hyperlipidemic Rabbits

Heme oxygenase and iron: from bacteria to humans

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