Decreased proteasomal cleavage at nitrotyrosine sites in proteins and peptides.

Cytochrome c Nitrotyrosine Peroxynitrite Proteasome activity Protein oxidation

Journal

Redox biology
ISSN: 2213-2317
Titre abrégé: Redox Biol
Pays: Netherlands
ID NLM: 101605639

Informations de publication

Date de publication:
10 2021
Historique:
received: 15 07 2021
revised: 05 08 2021
accepted: 15 08 2021
pubmed: 30 8 2021
medline: 26 10 2021
entrez: 29 8 2021
Statut: ppublish

Résumé

Removal of moderately oxidized proteins is mainly carried out by the proteasome, while highly modified proteins are no longer degradable. However, in the case of proteins modified by nitration of tyrosine residues to 3-nitrotyrosine (NO

Identifiants

pubmed: 34455147
pii: S2213-2317(21)00265-2
doi: 10.1016/j.redox.2021.102106
pmc: PMC8403764
pii:
doi:

Substances chimiques

Peptides 0
Proteins 0
3-nitrotyrosine 3604-79-3
Tyrosine 42HK56048U
Proteasome Endopeptidase Complex EC 3.4.25.1

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

102106

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier B.V. All rights reserved.

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Auteurs

Christiane Ott (C)

Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbruecke (DIfE), Nuthetal, Germany; German Center for Cardiovascular Research (DZHK), Berlin, Germany.

Florencia Tomasina (F)

Departamento de Bioquímica, Facultad de Medicina, Universidad de la República, Montevideo, Uruguay; Centro de Investigaciones Biomédicas (CEINBIO), Universidad de la República, Montevideo, Uruguay.

Nicolás Campolo (N)

Departamento de Bioquímica, Facultad de Medicina, Universidad de la República, Montevideo, Uruguay; Centro de Investigaciones Biomédicas (CEINBIO), Universidad de la República, Montevideo, Uruguay.

Silvina Bartesaghi (S)

Departamento de Bioquímica, Facultad de Medicina, Universidad de la República, Montevideo, Uruguay; Centro de Investigaciones Biomédicas (CEINBIO), Universidad de la República, Montevideo, Uruguay.

Mauricio Mastrogiovanni (M)

Departamento de Bioquímica, Facultad de Medicina, Universidad de la República, Montevideo, Uruguay; Centro de Investigaciones Biomédicas (CEINBIO), Universidad de la República, Montevideo, Uruguay.

Alejandro Leyva (A)

Analytical Biochemistry and Proteomics Unit, Instituto de Investigaciones Biológicas Clemente Estable & Institut Pasteur de Montevideo, Montevideo, Uruguay.

Carlos Batthyány (C)

Centro de Investigaciones Biomédicas (CEINBIO), Universidad de la República, Montevideo, Uruguay; Analytical Biochemistry and Proteomics Unit, Instituto de Investigaciones Biológicas Clemente Estable & Institut Pasteur de Montevideo, Montevideo, Uruguay.

Walter Meinl (W)

Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbruecke (DIfE), Nuthetal, Germany.

Tilman Grune (T)

Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbruecke (DIfE), Nuthetal, Germany; University of Potsdam, Institute of Nutritional Science, Nuthetal, Germany; German Center for Diabetes Research (DZD), München-Neuherberg, Germany; German Center for Cardiovascular Research (DZHK), Berlin, Germany; Department of Physiological Chemistry, Faculty of Chemistry, University of Vienna, Vienna, Austria. Electronic address: Tilman.Grune@dife.de.

Rafael Radi (R)

Departamento de Bioquímica, Facultad de Medicina, Universidad de la República, Montevideo, Uruguay; Centro de Investigaciones Biomédicas (CEINBIO), Universidad de la República, Montevideo, Uruguay. Electronic address: rradi@fmed.edu.uy.

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