Hydroxyl radical production in body fluids Roles of metal ions, ascorbate and superoxide

Winterbourn, C C

doi:10.1042/bj1980125

Cited by 242 publications

(81 citation statements)

References 28 publications

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“…20) The solution of the tested compound was prepared with DMF. The 5 ml assay mixture contained the following reagents: safranin (11.4 mM), ethylenediaminetetraacetic acid (EDTA)-Fe(II) (40 mM), H 2 O 2 (1.76 mM), the tested compound (2-15 mM) and a phosphate buffer (67 mM, pH 7.4).…”

Section: Hydroxyl Radical Scavenging Assaymentioning

confidence: 99%

Synthesis, Characterization, Antioxidant Activities, and DNA-Binding Studies of (E)-N′-[1-(Pyridin-2-yl)ethylidene]isonicotinohydrazide and Its Pr(III) and Nd(III) Complexes

Hao

Liu

et al. 2010

CHEMICAL & PHARMACEUTICAL BULLETIN

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It is well-known that Schiff bases play important role in bioinorganic chemistry and their metal complexes have been studied extensively for decades. These interesting ligand systems contain different donor sites in heterocyclic rings, e.g., NNO or NNS, which give rise to the architectural beauty of these coordination complexes.1) Among the ligand systems, hydrazide and hydrazone occupy important places because transition metal complexes of these ligands have been developed due to their chelating capability, structural flexibility, interesting electrical as well as magnetic properties, and various pharmacological activities, such as antibacterial, antitumoral, antiviral, antimalarial, and antituberculosis actions. 2,3)Investigation of molecular complexes of lanthanide ions has attracted significant attention, owing to their broad ranging fluorescent applications in biochemistry, material chemistry, medicine and so forth. [4][5][6] However, there have been only a few DNA-binding investigations of such complexes have been relatively few. Because the interaction between metal complexes and DNA is closely related to their potential biological and pharmaceutical activities, studies on the DNAbinding of metal complexes are very important in the development of new therapeutic reagents and DNA molecular probes. 7,8) Various coordination compounds of aroylhydrazones have been reported to act as enzyme inhibitors and are useful due to their pharmacological applications. 9,10)Here, we synthesized (E)-NЈ-[1-(2-pyridinyl)ethylidene]-isonicotinohydrazide (HL) and prepared its two of its lanthanide(III) complexes (Chart 1). The DNA-binding properties and antioxidant activities of the two lanthanide(III) complexes with HL are reported herein. ExperimentalMaterials Nitroblue tetrazolium (NBT), methionine (MET), vitamin B 2 (VitB 2 ), calf thymus DNA (CT-DNA) and ethidium bromide (EB) were obtained from Sigma Chemical Co. All experiments involving interaction of the complexes with CT-DNA were carried out in doubly distilled water buffer containing 5 mM Tris [Tris(hydroxymethyl)-aminomethane] and 50 mM NaCl, and adjusted to pH 7.2 with hydrochloric acid. The DNA concentrations of the solutions were determined from their UV absorption at 260 nm using the molar absorption coefficient e 260 ϭ6600 mol Ϫ1 cm Ϫ1. DNA Purity was checked by monitoring the ratio of the absorbance at 260 nm to that at 280 nm. The solution gave a ratio of A 260 /A 280 Ͼ1.80, indicating that DNA was sufficiently free from protein. 11)Physical Measurements The UV-vis absorption measurements were conducted by using a Varian Cary 100 spectrophotometer equipped with quartz cells. All fluorescence emission spectra were measured using a Hitachi F-4500 spectrofluorophotometer equipped with a xenon lamp source and a quartz cell of 5 cm path length. Viscosity experiments were carried out on an Ubbelodhe viscometer. The circular dichroic (CD) spectra were recorded on a Jasco J-810 spectropolarimeter. The 1 H-NMR spectra were recorded with a Bruker ACF300 FT-NMR instrum...

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Section: Hydroxyl Radical Scavenging Assaymentioning

confidence: 99%

Synthesis, Characterization, Antioxidant Activities, and DNA-Binding Studies of (E)-N′-[1-(Pyridin-2-yl)ethylidene]isonicotinohydrazide and Its Pr(III) and Nd(III) Complexes

Hao

Liu

et al. 2010

CHEMICAL & PHARMACEUTICAL BULLETIN

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“…AA recycles the metal catalyst in the in vitro Fenton reaction, thus favouring another cycle of hydroxyl radical formation from H 2 O 2 and ultimately leading to lipid, protein and DNA oxidation [1]. Although AA-mediated Fenton reactions may be controlled in the plasma and lymph of healthy individuals by efficient iron sequestration in transferrin [21,22], the redox-active NTBI found in the serum of individuals with iron overload may catalyse free radical formation in the presence of AA. AA supplements were reported to enhance cell and organ damage, and eventually cause cardiac failure, in patients with iron overload [23][24][25].…”

Section: Introductionmentioning

confidence: 99%

Vitamin C modulation of H2O2-induced damage and iron homeostasis in human cells

Duarte

Jones

2007

Free Radical Biology and Medicine

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Vitamin C (ascorbic acid, AA) is an important antioxidant in human plasma. It is clear, however, that AA has other important, non-antioxidant roles in cells. Of particular interest is its involvement in iron metabolism, since AA enhances dietary iron absorption, increases the activity of Fe 2+ -dependent cellular enzymes, promotes Fenton reactions in vitro and was reported to have deleterious effects in individuals with iron overload. Nevertheless, the ability of AA to modulate iron metabolism and enhance iron-dependent damage in cells, tissues and organisms has not been fully elucidated. Here we investigated the effect of AA on iron-mediated oxidative stress in normal human fibroblasts. Incubation with physiologically relevant concentrations of AA was not harmful but sensitised cells towards H 2 O 2 -induced, iron-dependent DNA strand breakage and cell death. We also report that AA increased the levels of intracellular catalytic iron and concomitantly modulated the expression of two wellestablished iron-regulated genes, ferritin and transferrin receptor. In summary, we present evidence of a novel, non-antioxidant role of AA in human cells, where it increases iron availability and enhances ROS-mediated, iron-dependent damage. We suggest that AA may exacerbate the deleterious effects of metals in vivo and promote normal tissue injury in situations associated with elevated ROS production.

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“…Nearly all the iron present in the body is located in haem-containing proteins and in ironbinding proteins such as transferrin, ferritin, lactoferrin, or in enzymes. In in vitro test systems, protein-bound iron is often unable to catalyze OH formation (2,3,4). Iron-binding proteins are even able to inhibit oxygen-free radical destruction by binding of iron (5,6).…”

Section: Introductionmentioning

confidence: 99%

Iron mobilization from ferritin by superoxide derived from stimulated polymorphonuclear leukocytes. Possible mechanism in inflammation diseases.

Biemond¹,

Eijk²,

Swaak³

et al. 1984

J. Clin. Invest.

386

116

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Abstract. During inflammation, the superoxide anion (O°) and hydrogen peroxide (H202) are produced by stimulated polymorphonuclear leukocytes and macrophages. The toxic effects of these reactive oxygen intermediates increase when traces of iron are present, because iron catalyzes the formation of the hydroxyl radical (OH'). Partially saturated iron-binding proteins, such as transferrin and ferritin, are unable to catalyze OH formation in vitro. Mobilization of iron from these proteins is necessary for iron stimulation of OH" formation. This paper reports that stimulated polymorphonuclear leukocytes mobilize iron from human and horse ferritin, but not from human transferrin. Iron release from ferritin depends on O2 because it can be prevented by the addition of superoxide dismutase. Catalase and dimethylsulfoxide have no inhibitory effect on iron mobilization. The efficiency of the iron release increases at low levels of O2 production. Only O2 produced by granulocytes is sufficient for iron mobilization, because solid potassium superoxide is also able to release iron from ferritin. We propose that this reaction may potentiate the formation of the OH radical in inflammatory states.

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Hydroxyl radical production in body fluids Roles of metal ions, ascorbate and superoxide

Cited by 242 publications

References 28 publications

Synthesis, Characterization, Antioxidant Activities, and DNA-Binding Studies of (<i>E</i>)-<i>N</i>′-[1-(Pyridin-2-yl)ethylidene]isonicotinohydrazide and Its Pr(III) and Nd(III) Complexes

Synthesis, Characterization, Antioxidant Activities, and DNA-Binding Studies of (<i>E</i>)-<i>N</i>′-[1-(Pyridin-2-yl)ethylidene]isonicotinohydrazide and Its Pr(III) and Nd(III) Complexes

Vitamin C modulation of H2O2-induced damage and iron homeostasis in human cells

Iron mobilization from ferritin by superoxide derived from stimulated polymorphonuclear leukocytes. Possible mechanism in inflammation diseases.

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Hydroxyl radical production in body fluids Roles of metal ions, ascorbate and superoxide

Cited by 242 publications

References 28 publications

Synthesis, Characterization, Antioxidant Activities, and DNA-Binding Studies of (<i>E</i>)-<i>N</i>&prime;-[1-(Pyridin-2-yl)ethylidene]isonicotinohydrazide and Its Pr(III) and Nd(III) Complexes

Synthesis, Characterization, Antioxidant Activities, and DNA-Binding Studies of (<i>E</i>)-<i>N</i>&prime;-[1-(Pyridin-2-yl)ethylidene]isonicotinohydrazide and Its Pr(III) and Nd(III) Complexes

Vitamin C modulation of H2O2-induced damage and iron homeostasis in human cells

Iron mobilization from ferritin by superoxide derived from stimulated polymorphonuclear leukocytes. Possible mechanism in inflammation diseases.

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Synthesis, Characterization, Antioxidant Activities, and DNA-Binding Studies of (<i>E</i>)-<i>N</i>′-[1-(Pyridin-2-yl)ethylidene]isonicotinohydrazide and Its Pr(III) and Nd(III) Complexes

Synthesis, Characterization, Antioxidant Activities, and DNA-Binding Studies of (<i>E</i>)-<i>N</i>′-[1-(Pyridin-2-yl)ethylidene]isonicotinohydrazide and Its Pr(III) and Nd(III) Complexes