Catalytic oxidant scavenging by selenium-containing compounds: Reduction of selenoxides and N-chloramines by thiols and redox enzymes

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

Catalytic oxidant scavenging by selenium-containing compounds : Reduction of selenoxides and N-chloramines by thiols and redox enzymes. / Carroll, Luke; Pattison, David I; Fu, Shanlin; Schiesser, Carl H; Davies, Michael J; Hawkins, Clare L.

I: Redox Biology, Bind 12, 2017, s. 872-882.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Carroll, L, Pattison, DI, Fu, S, Schiesser, CH, Davies, MJ & Hawkins, CL 2017, 'Catalytic oxidant scavenging by selenium-containing compounds: Reduction of selenoxides and N-chloramines by thiols and redox enzymes', Redox Biology, bind 12, s. 872-882. https://doi.org/10.1016/j.redox.2017.04.023

APA

Carroll, L., Pattison, D. I., Fu, S., Schiesser, C. H., Davies, M. J., & Hawkins, C. L. (2017). Catalytic oxidant scavenging by selenium-containing compounds: Reduction of selenoxides and N-chloramines by thiols and redox enzymes. Redox Biology, 12, 872-882. https://doi.org/10.1016/j.redox.2017.04.023

Vancouver

Carroll L, Pattison DI, Fu S, Schiesser CH, Davies MJ, Hawkins CL. Catalytic oxidant scavenging by selenium-containing compounds: Reduction of selenoxides and N-chloramines by thiols and redox enzymes. Redox Biology. 2017;12:872-882. https://doi.org/10.1016/j.redox.2017.04.023

Author

Carroll, Luke ; Pattison, David I ; Fu, Shanlin ; Schiesser, Carl H ; Davies, Michael J ; Hawkins, Clare L. / Catalytic oxidant scavenging by selenium-containing compounds : Reduction of selenoxides and N-chloramines by thiols and redox enzymes. I: Redox Biology. 2017 ; Bind 12. s. 872-882.

Bibtex

@article{812ffe021d8d4127a2f6d99542f1552c,
title = "Catalytic oxidant scavenging by selenium-containing compounds: Reduction of selenoxides and N-chloramines by thiols and redox enzymes",
abstract = "Myeloperoxidase produces strong oxidants during the immune response to destroy invading pathogens. However, these oxidants can also cause tissue damage, which contributes to the development of numerous inflammatory diseases. Selenium containing compounds, including selenomethionine (SeMet) and 1,4-anhydro-5-seleno-D-talitol (SeTal), react rapidly with different MPO-derived oxidants to form the respective selenoxides (SeMetO and SeTalO). This study investigates the susceptibility of these selenoxides to undergo reduction back to the parent compounds by intracellular reducing systems, including glutathione (GSH) and the glutathione reductase and thioredoxin reductase systems. GSH is shown to reduce SeMetO and SeTalO, with consequent formation of GSSG with apparent second order rate constants, k2, in the range 10(3)-10(4)M(-1)s(-1). Glutathione reductase reduces both SeMetO and SeTalO at the expense of NADPH via formation of GSSG, whereas thioredoxin reductase acts only on SeMetO. The presence of SeMet and SeTal also increased the rate at which NADPH was consumed by the glutathione reductase system in the presence of N-chloramines. In contrast, the presence of SeMet and SeTal reduced the rate of NADPH consumption by the thioredoxin reductase system after addition of N-chloramines, consistent with the rapid formation of selenoxides, but only slow reduction by thioredoxin reductase. These results support a potential role of seleno compounds to act as catalytic scavengers of MPO-derived oxidants, particularly in the presence of glutathione reductase and NADPH, assuming that sufficient plasma levels of the parent selenoether can be achieved in vivo following supplementation.",
author = "Luke Carroll and Pattison, {David I} and Shanlin Fu and Schiesser, {Carl H} and Davies, {Michael J} and Hawkins, {Clare L}",
note = "Copyright {\circledC} 2017. Published by Elsevier B.V.",
year = "2017",
doi = "10.1016/j.redox.2017.04.023",
language = "English",
volume = "12",
pages = "872--882",
journal = "Redox Biology",
issn = "2213-2317",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Catalytic oxidant scavenging by selenium-containing compounds

T2 - Reduction of selenoxides and N-chloramines by thiols and redox enzymes

AU - Carroll, Luke

AU - Pattison, David I

AU - Fu, Shanlin

AU - Schiesser, Carl H

AU - Davies, Michael J

AU - Hawkins, Clare L

N1 - Copyright © 2017. Published by Elsevier B.V.

PY - 2017

Y1 - 2017

N2 - Myeloperoxidase produces strong oxidants during the immune response to destroy invading pathogens. However, these oxidants can also cause tissue damage, which contributes to the development of numerous inflammatory diseases. Selenium containing compounds, including selenomethionine (SeMet) and 1,4-anhydro-5-seleno-D-talitol (SeTal), react rapidly with different MPO-derived oxidants to form the respective selenoxides (SeMetO and SeTalO). This study investigates the susceptibility of these selenoxides to undergo reduction back to the parent compounds by intracellular reducing systems, including glutathione (GSH) and the glutathione reductase and thioredoxin reductase systems. GSH is shown to reduce SeMetO and SeTalO, with consequent formation of GSSG with apparent second order rate constants, k2, in the range 10(3)-10(4)M(-1)s(-1). Glutathione reductase reduces both SeMetO and SeTalO at the expense of NADPH via formation of GSSG, whereas thioredoxin reductase acts only on SeMetO. The presence of SeMet and SeTal also increased the rate at which NADPH was consumed by the glutathione reductase system in the presence of N-chloramines. In contrast, the presence of SeMet and SeTal reduced the rate of NADPH consumption by the thioredoxin reductase system after addition of N-chloramines, consistent with the rapid formation of selenoxides, but only slow reduction by thioredoxin reductase. These results support a potential role of seleno compounds to act as catalytic scavengers of MPO-derived oxidants, particularly in the presence of glutathione reductase and NADPH, assuming that sufficient plasma levels of the parent selenoether can be achieved in vivo following supplementation.

AB - Myeloperoxidase produces strong oxidants during the immune response to destroy invading pathogens. However, these oxidants can also cause tissue damage, which contributes to the development of numerous inflammatory diseases. Selenium containing compounds, including selenomethionine (SeMet) and 1,4-anhydro-5-seleno-D-talitol (SeTal), react rapidly with different MPO-derived oxidants to form the respective selenoxides (SeMetO and SeTalO). This study investigates the susceptibility of these selenoxides to undergo reduction back to the parent compounds by intracellular reducing systems, including glutathione (GSH) and the glutathione reductase and thioredoxin reductase systems. GSH is shown to reduce SeMetO and SeTalO, with consequent formation of GSSG with apparent second order rate constants, k2, in the range 10(3)-10(4)M(-1)s(-1). Glutathione reductase reduces both SeMetO and SeTalO at the expense of NADPH via formation of GSSG, whereas thioredoxin reductase acts only on SeMetO. The presence of SeMet and SeTal also increased the rate at which NADPH was consumed by the glutathione reductase system in the presence of N-chloramines. In contrast, the presence of SeMet and SeTal reduced the rate of NADPH consumption by the thioredoxin reductase system after addition of N-chloramines, consistent with the rapid formation of selenoxides, but only slow reduction by thioredoxin reductase. These results support a potential role of seleno compounds to act as catalytic scavengers of MPO-derived oxidants, particularly in the presence of glutathione reductase and NADPH, assuming that sufficient plasma levels of the parent selenoether can be achieved in vivo following supplementation.

U2 - 10.1016/j.redox.2017.04.023

DO - 10.1016/j.redox.2017.04.023

M3 - Journal article

C2 - 28458184

VL - 12

SP - 872

EP - 882

JO - Redox Biology

JF - Redox Biology

SN - 2213-2317

ER -

ID: 177115074