Inhibition of enzymes and oxidative damage of red blood cells induced by t-butylhydroperoxide-derived radicals

Zee, Jolanda Van der; Steveninck, J. Van; Koster, J.F.; Dubbelman, T. M. A. R.

doi:10.1016/0005-2736(89)90397-0

Cited by 69 publications

(47 citation statements)

References 22 publications

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“…t-BHP is a lipid-soluble radical former that can be incorporated into the membrane lipid bilayer of intact erythrocytes when added to a suspension of such cells and becomes an alkoxyl radical (BuO •) in the presence of hemoglobin iron [3]. This radical induces lipid peroxidation of the membrane.…”

Section: Discussionmentioning

confidence: 99%

“…It was already reported that exposure of erythrocytes to hydrogen peroxide, active oxygen radicals, or lipid peroxides brings about reduced activity of some membrane-bound enzymes [2,3]; opening of pores in the membrane, which permits passage of certain water-soluble, low-molecular weight substances [4]; enhanced phagocytosis by macrophages [5]; and finally hemolysis [6]. In some instances, even when lipid peroxidation by these oxidants was prevented by the addition of anti-oxidants, there still occurred some membrane damages, such as hemolysis and polymerization of certain membrane proteins [7] .…”

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confidence: 99%

“…Especially, attempts were made to clarify their possible inhibitory effects on the aminophospholipid translocase to alter the asymmetric distribution of the membrane phospholipids, thus affecting the bilayer structure. The oxidants used were a watersoluble radical former, 2,2'-azo-bis (2-amidinopropane) dihydrochloride (AAPH), which does not require any transition metal ion for the radical formation [14], and a lipid-soluble radical former, t-butylhydroperoxide (t-BHP), which is often used as a model compound of lipid peroxide [3]. MATERIALS AND METHODS…”

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confidence: 99%

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Oxidative Membrane Damage and the Resulting Alteration in the Membrane Lipid Bilayer Structure of Human Erythrocytes Caused by Radical-Forming Oxidants.

Sato

Tamura

Kawaguchi

et al. 1992

J. Clin. Biochem. Nutr.

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SummaryTreatment of washed human erythrocytes for a short time (up to 2 h) with 75 or loo mlvt 2,2'-azo-bis(2-amidinopropane) dihydrochloride (AAPH), a water-soluble, radical-forming oxidant, induced considerable oxidation of the membrane protein SH groups, without any detectable formation of lipid peroxide from the membrane lipid. These cells became susceptible to the action of pancreatic phospholipase A2, and the asymmetric distribution of their membrane aminophospholipids was partially lost, accompanied by a reduced activity of the aminophospholipid translocase of the membrane. In contrast, treatment of the erythrocytes with t-butylhydroperoxide (t-BHP), a lipid-soluble, radicalforming oxidant, caused rapid and intensive lipid peroxidation, but SH oxidation to a lesser extent than that achieved by AAPH. In these cells, the membrane phospholipid asymmetry was well maintained, although the aminophospholipid translocase activity was reduced. These results suggest that AAPH might oxidize both the aminophospholipid translocase of the membrane and the membrane skeletal proteins responsible for maintenance of the asymmetric phospholipid distribution, resulting in loss of the asymmetry, and that t-BHP causes formation of peroxides from the membrane phospholipids, which might affect aminophospholipid translocase only.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Oxidative Membrane Damage and the Resulting Alteration in the Membrane Lipid Bilayer Structure of Human Erythrocytes Caused by Radical-Forming Oxidants.

Sato

Tamura

Kawaguchi

et al. 1992

J. Clin. Biochem. Nutr.

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“…[6][7][8] Although most cells are susceptible to oxidative injury, RBCs are particularly at risk due to their high iron content and regular exposure to high concentrations of oxygen, as well as environmental chemicals and drugs. tert-Butyl hydroperoxide (BHP) is a commonly used compound to investigate the effects of peroxides and radicals on biological systems.…”

mentioning

confidence: 99%

“…tert-Butyl hydroperoxide (BHP) is a commonly used compound to investigate the effects of peroxides and radicals on biological systems. [6][7][8][9] Many lines of evidence have emerged to support a fundamental role of redox modification of certain proteins in normal cellular biochemical and physiological processes. A number of purified proteins are sensitive to oxidation by thiol disulfide interchange reactions.…”

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confidence: 99%

Pyruvate Kinase Is Protected by Glutathione-Dependent Redox Balance in Human Red Blood Cells Exposed to Reactive Oxygen Species

Ogasawara

Funakoshi

Ishii

2008

Biological & Pharmaceutical Bulletin

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To determine the antioxidant role of glutathione (GSH) in human red blood cells (RBCs), we investigated the effect of disrupting GSH homeostasis on the oxidative modification of thiol-dependent enzymes by exposure to tert-butyl hydroperoxide (BHP). When hemolysate was incubated with BHP, significant decreases in enzyme activity were observed. However, the inactivation did not occur in intact RBC suspensions that were exposed to BHP. In this study, we used two independent treatments aimed at decreasing the level of reduced form of GSH, pre-incubation with a glutathione reductase inhibitor or glucose-free medium to examine the influences of preventing GSH-dependent antioxidant and reactivation activity on thiol-dependent enzyme. Pyruvate kinase (PK) activity clearly decreased along with depletion of GSH compared to other glycolytic enzyme activities by BHP exposure in RBCs. The addition of GSH, but not glucose, before BHP exposure completely prevented the inactivation of PK in hemolysate; however, partial reactivation of inactivated PK was observed by post-addition of both GSH and glutaredoxin at an early stage during BHP exposure. Moreover, hydroxyl radicals but not hydrogen peroxide inactivated PK. These results suggest that PK is highly susceptible to radicals and that GSH is essential to protect PK activity by not only directly scavenging radicals but also by systematically reactivating oxidized enzyme in human RBCs.

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Bactericidal Activities of Radical Species Generated by Catalytic Reaction of Iron(III) Octacarboxyphthalocyanine

Ichinohe

Miyajima

Noguchi

et al. 1998

J. Porphyrins Phthalocyanines

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Strong bactericidal activities against various bacteria were observed in the reaction system of iron(III) octacarboxyphthalocyanine ( Fe III - oapc ) and tert-butyl hydroperoxide (tert-BuOOH). The kinetics of the decomposition of tert-BuOOH catalysed by Fe III -oapc were studied in buffered solutions between pH 5 to 12 using gas chromatography analysis. The rate of catalytic decomposition of tert-BuOOH followed second-order kinetics in tert-BuOOH concentrations. The second-order rate constant (k2) had a maximum value at pH 11. Oxygen evolution was observed at high tert-BuOOH concentration, while oxygen consumption was observed at low tert-BuOOH concentration. The former indicates plural radical chain reactions of the tert-butoxyl radical and the latter suggests decomposition of the tert-butoxyl radical to acetone and methyl radical. By the electron spin resonance spin trapping method using 5,5-dimethyl-1-pyrroline-N-oxide and α-phenyl-N-tert-butylnitrone it was found that the radical species generated in the reaction system is tert-butoxyl radical, which plays crucial roles in bactericidal activities.

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Inhibition of enzymes and oxidative damage of red blood cells induced by t-butylhydroperoxide-derived radicals

Cited by 69 publications

References 22 publications

Oxidative Membrane Damage and the Resulting Alteration in the Membrane Lipid Bilayer Structure of Human Erythrocytes Caused by Radical-Forming Oxidants.

Oxidative Membrane Damage and the Resulting Alteration in the Membrane Lipid Bilayer Structure of Human Erythrocytes Caused by Radical-Forming Oxidants.

Pyruvate Kinase Is Protected by Glutathione-Dependent Redox Balance in Human Red Blood Cells Exposed to Reactive Oxygen Species

Bactericidal Activities of Radical Species Generated by Catalytic Reaction of Iron(III) Octacarboxyphthalocyanine

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