Heme and apoprotein modification of cytochrome P450 2B4 during its oxidative inactivation in monooxygenase reconstituted system

Karuzina, I I; Згода, В. Г.; Kuznetsova, Galina P.; Samenkova, N. F.; Archakov, Alexander I.

doi:10.1016/s0891-5849(98)00252-4

Cited by 47 publications

(27 citation statements)

References 55 publications

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“…We observed previously that H 2 O 2 -induced dilation of HCAs is reduced by a combination of charybdotoxin and apamin, 9 suggesting a role for K ϩ channels in this response; however, these inhibitors block not only BK Ca channels, but also intermediate-and smallconductance K Ca channels and voltage-dependent K v channels. 28 Although the present results with iberiotoxin indicate that H 2 O 2 -induced dilation does not require BK Ca channels, 30 by directly oxidizing and degrading the heme prosthetic group into monopyrrole and dipyrrole fragments that irreversibly bind to the protein. 31 Interestingly, P450BM-3 (a bacterial CYP) is highly unstable in the presence of H 2 O 2 .…”

Section: Eets and H 2 O 2 As Putative Edhfsmentioning

confidence: 61%

Hydrogen Peroxide Inhibits Cytochrome P450 Epoxygenases

Larsen

Gutterman

Sato

et al. 2008

Circulation Research

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Abstract-The cytochrome P450 epoxygenase (CYP)-derived metabolites of arachidonic acid the epoxyeicosatrienoic acids (EETs) and hydrogen peroxide (H 2 O 2 ) both function as endothelium-derived hyperpolarizing factors (EDHFs) in the human coronary microcirculation. However, the relative importance of and potential interactions between these 2 vasodilators remain unexplored. We identified a novel inhibitory interaction between CYPs and H 2 O 2 in human coronary arterioles, where EDHF-mediated vasodilatory mechanisms are prominent. Bradykinin induced vascular superoxide and H 2 O 2 production in an endothelium-dependent manner and elicited a concentration-dependent dilation that was reduced by catalase but not by 14,15-epoxyeicosa-5(Z)-enoic acid (EEZE), 6-(2-propargyloxyphenyl)hexanoic acid, sulfaphenazole, or iberiotoxin. However, in the presence of catalase, an inhibitory effect of these compounds was unmasked.In a tandem-bioassay preparation, application of bradykinin to endothelium-intact donor vessels elicited dilation of downstream endothelium-denuded detectors that was partially inhibited by donor-applied catalase but not by detector-applied EEZE; however, EEZE significantly inhibited dilation in the presence of catalase. EET production by human recombinant CYP 2C9 and 2J2, 2 major epoxygenase isozymes expressed in human coronary arterioles, was directly inhibited in a concentration-dependent fashion by H 2 O 2 in vitro, as observed by high-performance liquid chromatography (HPLC); however, EETs were not directly sensitive to oxidative modification. H 2 O 2 inhibited dilation to arachidonic acid but not to 11,12-EET. These findings suggest that an inhibitory interaction exists between 2 EDHFs in the human coronary microcirculation. CYP epoxygenases are directly inhibited by H 2 O 2 , and this interaction may modulate vascular EET bioavailability. (Circ Res. 2008;102:59-67.)Key Words: endothelium-derived hyperpolarizing factor Ⅲ hydrogen peroxide Ⅲ epoxyeicosatrienoic acid Ⅲ cytochrome P450 Ⅲ reactive oxygen species T he vascular endothelium releases numerous vasodilatory substances, including nitric oxide (NO), prostacyclin, and endothelium-derived hyperpolarizing factor (EDHF). EDHF is an important modulator of vasomotor tone, particularly in the microcirculation. 1,2 Despite more than a decade of investigation, the chemical identity of EDHF remains controversial, and multiple EDHFs have been proposed. Among these, substantial evidence now points to epoxyeicosatrienoic acids (EETs), [3][4][5] cytochrome P450 epoxygenase (CYP)-derived metabolites of arachidonic acid (AA), as EDHFs with another prominent candidate being the reactive oxygen species (ROS) hydrogen peroxide (H 2 O 2 ). 6,7 It has been reported that a significant inhibitory interaction occurs between NO and EET, in which NO inhibits CYPmediated production of EET from AA. 8 Such an interaction presumably exists to conserve vasodilator substances, while at the same time providing a compensatory mechanism of dilation when one is impaired. It is...

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Section: Eets and H 2 O 2 As Putative Edhfsmentioning

confidence: 61%

Hydrogen Peroxide Inhibits Cytochrome P450 Epoxygenases

Larsen

Gutterman

Sato

et al. 2008

Circulation Research

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“…Cytochrome P450 can be inactivated by free NADPH oxidation, NADPH-dependent monooxygenase reactions and lipid peroxidation. This self-inactivation also leads to the breakage of the bond between heme and apoenzyme and heme degradation (Karuzina et al, 1999).…”

Section: Heme-dependent and -Independent Endogenous Production Omentioning

confidence: 99%

Carbon Monoxide: Endogenous Production, Physiological Functions, and Pharmacological Applications

Wang²

2005

Pharmacol Rev

853

741

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“…CYP 51A1 and CYP 3A4 were kindly presented by Prof. S. A. Usanov (Institute of Bioorganic Chemistry, Minsk, Belarus). Cytochrome P450 2B4 (100 mM) was isolated from the microsomal fraction of rabbit liver induced by phenobarbital and purified as described in [22]. Concentration of P450 2B4 was determined by formation of a complex of the cytochrome P450's reduced form with carbon monooxide using the extinction coefficient e 450 = 91 mM À1 cm À1 [23].…”

Section: Chemicals and Proteinsmentioning

confidence: 99%

Direct Electrochemistry of Heme Proteins on Electrodes Modified with Didodecyldimethyl Ammonium Bromide and Carbon Black

et al. 2012

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A novel matrix based on commercially available carbon black (CB) N220 and didodecyldimethyl ammonium bromide (DDAB) was shown to be a reliable support for direct electron transfer reactions between screen printed electrode (SPE) and Fe(III)-heme proteins. Cytochrome c (cyt c), myoglobin (Mb), horseradish peroxidase (HRP) and cytochromes P450 (CYP 51A1, CYP 3A4, CYP 2B4) generated well-shaped cyclic voltammograms on SPE/CB/ DDAB electrodes (both in solution and in immobilized state). The attractive performance characteristics of CB modified electrodes are advantageous over single-walled carbon nanotubes (SW CNT) based ones. The achieved direct electrochemistry of heme proteins on CB/DDAB-modified electrodes provided successful elaboration of the immunosensor for cardiac Mb. The immunosensor showed applicability for diagnostics of myocardial infarction displaying significant difference in cardiac Mb content of human blood plasma samples taken from the corresponding patients.

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Heme and apoprotein modification of cytochrome P450 2B4 during its oxidative inactivation in monooxygenase reconstituted system

Cited by 47 publications

References 55 publications

Hydrogen Peroxide Inhibits Cytochrome P450 Epoxygenases

Hydrogen Peroxide Inhibits Cytochrome P450 Epoxygenases

Carbon Monoxide: Endogenous Production, Physiological Functions, and Pharmacological Applications

Direct Electrochemistry of Heme Proteins on Electrodes Modified with Didodecyldimethyl Ammonium Bromide and Carbon Black

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