Loss of methionine sulfoxide reductases increases resistance to oxidative stress.


Journal

Free radical biology & medicine
ISSN: 1873-4596
Titre abrégé: Free Radic Biol Med
Pays: United States
ID NLM: 8709159

Informations de publication

Date de publication:
12 2019
Historique:
received: 15 08 2019
revised: 07 10 2019
accepted: 08 10 2019
pubmed: 14 10 2019
medline: 4 9 2020
entrez: 14 10 2019
Statut: ppublish

Résumé

Oxidation of methionine residues to methionine sulfoxide scavenges reactive species, thus protecting against oxidative stress. Reduction of the sulfoxide back to methionine by methionine sulfoxide reductases creates a cycle with catalytic efficiency. Protection by the methionine sulfoxide reductases is well documented in cultured cells, from microorganisms to mammals. However, knocking out one or two of the 4 mammalian reductases had little effect in mice that were not stressed. We hypothesized that the minimal effect is due to redundancy provided by the 4 reductases. We tested the hypothesis by creating a transgenic mouse line lacking all 4 reductases and predicted that this mouse would be exceptionally sensitive to oxidative stress. The mutant mice were phenotypically normal at birth, exhibited normal post-natal growth, and were fertile. Surprisingly, rather than being more sensitive to oxidative stress, they were more resistant to both cardiac ischemia-reperfusion injury and to parenteral paraquat, a redox-cycling agent. Resistance was not a result of hormetic induction of the antioxidant transcription factor Nrf2 nor activation of Akt. The mechanism of protection may be novel.

Identifiants

pubmed: 31606431
pii: S0891-5849(19)31342-5
doi: 10.1016/j.freeradbiomed.2019.10.006
pmc: PMC6891793
mid: NIHMS1543005
pii:
doi:

Substances chimiques

NF-E2-Related Factor 2 0
Nfe2l2 protein, mouse 0
Methionine AE28F7PNPL
Methionine Sulfoxide Reductases EC 1.8.4.-
Paraquat PLG39H7695
methionine sulfoxide XN1XVI4B2C

Types de publication

Journal Article Research Support, N.I.H., Intramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

374-384

Subventions

Organisme : Intramural NIH HHS
ID : Z01 HL000225-31
Pays : United States
Organisme : Intramural NIH HHS
ID : ZIA HL000225
Pays : United States
Organisme : Intramural NIH HHS
ID : ZIA HL002066
Pays : United States
Organisme : Intramural NIH HHS
ID : ZIA HL002066-10
Pays : United States

Informations de copyright

Published by Elsevier Inc.

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Auteurs

Lo Lai (L)

Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD, 20892, United States.

Junhui Sun (J)

Laboratory of Cardiac Physiology, National Heart, Lung, and Blood Institute, Bethesda, MD, 20892, United States.

Sreya Tarafdar (S)

Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD, 20892, United States.

Chengyu Liu (C)

Transgenic Core Facility, National Heart, Lung, and Blood Institute, Bethesda, MD, 20892, United States.

Elizabeth Murphy (E)

Laboratory of Cardiac Physiology, National Heart, Lung, and Blood Institute, Bethesda, MD, 20892, United States.

Geumsoo Kim (G)

Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD, 20892, United States.

Rodney L Levine (RL)

Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD, 20892, United States. Electronic address: rlevine@nih.gov.

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Classifications MeSH