Cysteine and methionine oxidation in thrombotic disorders.
Benzothiazine
Beta-2 glycoprotein I
Cysteine
Disulfide
Fibrinogen
Glutathionylation
Hemostasis
Methionine
Methionine sulfoxide
Methionine sulfoxide reductase
Nitrosation
Oxaziridine
Oxidation
Protein disulfide isomerase
Src kinase
Sulfenylation
Sulfhydration
Thrombosis
von Willebrand factor
Journal
Current opinion in chemical biology
ISSN: 1879-0402
Titre abrégé: Curr Opin Chem Biol
Pays: England
ID NLM: 9811312
Informations de publication
Date de publication:
10 2023
10 2023
Historique:
received:
27
04
2023
revised:
19
05
2023
accepted:
22
05
2023
pmc-release:
01
10
2024
medline:
22
9
2023
pubmed:
19
6
2023
entrez:
18
6
2023
Statut:
ppublish
Résumé
Thrombosis is the leading cause of death in many diseased conditions. Oxidative stress is characteristic of these conditions. Yet, the mechanisms through which oxidants become prothrombotic are unclear. Recent evidence suggests protein cysteine and methionine oxidation as prothrombotic regulators. These oxidative post-translational modifications occur on proteins that participate in the thrombotic process, including Src family kinases, protein disulfide isomerase, β2 glycoprotein I, von Willebrand factor, and fibrinogen. New chemical tools to identify oxidized cysteine and methionine proteins in thrombosis and hemostasis, including carbon nucleophiles for cysteine sulfenylation and oxaziridines for methionine, are critical to understanding why clots occur during oxidative stress. These mechanisms will identify alternative or novel therapeutic approaches to treat thrombotic disorders in diseased conditions.
Identifiants
pubmed: 37331217
pii: S1367-5931(23)00088-1
doi: 10.1016/j.cbpa.2023.102350
pmc: PMC10527720
mid: NIHMS1910280
pii:
doi:
Substances chimiques
Methionine
AE28F7PNPL
Cysteine
K848JZ4886
Proteins
0
Racemethionine
73JWT2K6T3
Types de publication
Journal Article
Review
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
102350Subventions
Organisme : NHLBI NIH HHS
ID : K99 HL164888
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM128840
Pays : United States
Informations de copyright
Copyright © 2023 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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