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Desmin Reorganization by Stimuli Inducing Oxidative Stress and Electrophiles: Role of Its Single Cysteine Residue

The type III intermediate filament proteins vimentin and GFAP are modulated by oxidants and electrophiles, mainly through perturbation of their single cysteine residues. Desmin, the type III intermediate filament protein specific to muscle cells, is critical for muscle homeostasis, playing a key rol...

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Detalles Bibliográficos
Autores principales: Moneo-Corcuera, Diego, Viedma-Poyatos, Álvaro, Stamatakis, Konstantinos, Pérez-Sala, Dolores
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10525603/
https://www.ncbi.nlm.nih.gov/pubmed/37760006
http://dx.doi.org/10.3390/antiox12091703
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author Moneo-Corcuera, Diego
Viedma-Poyatos, Álvaro
Stamatakis, Konstantinos
Pérez-Sala, Dolores
author_facet Moneo-Corcuera, Diego
Viedma-Poyatos, Álvaro
Stamatakis, Konstantinos
Pérez-Sala, Dolores
author_sort Moneo-Corcuera, Diego
collection PubMed
description The type III intermediate filament proteins vimentin and GFAP are modulated by oxidants and electrophiles, mainly through perturbation of their single cysteine residues. Desmin, the type III intermediate filament protein specific to muscle cells, is critical for muscle homeostasis, playing a key role in sarcomere organization and mitochondrial function. Here, we have studied the impact of oxidants and cysteine-reactive agents on desmin behavior. Our results show that several reactive species and drugs induce covalent modifications of desmin in vitro, of which its single cysteine residue, C333, is an important target. Moreover, stimuli eliciting oxidative stress or lipoxidation, including H(2)O(2), 15-deoxy-prostaglandin J(2), and CoCl(2)-elicited chemical hypoxia, provoke desmin disorganization in H9c2 rat cardiomyoblasts transfected with wild-type desmin, which is partially attenuated in cells expressing a C333S mutant. Notably, in cells lacking other cytoplasmic intermediate filaments, network formation by desmin C333S appears less efficient than that of desmin wt, especially when these proteins are expressed as fluorescent fusion constructs. Nevertheless, in these cells, the desmin C333S organization is also protected from disruption by oxidants. Taken together, our results indicate that desmin is a target for oxidative and electrophilic stress, which elicit desmin remodeling conditioned by the presence of its single cysteine residue.
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spelling pubmed-105256032023-09-28 Desmin Reorganization by Stimuli Inducing Oxidative Stress and Electrophiles: Role of Its Single Cysteine Residue Moneo-Corcuera, Diego Viedma-Poyatos, Álvaro Stamatakis, Konstantinos Pérez-Sala, Dolores Antioxidants (Basel) Article The type III intermediate filament proteins vimentin and GFAP are modulated by oxidants and electrophiles, mainly through perturbation of their single cysteine residues. Desmin, the type III intermediate filament protein specific to muscle cells, is critical for muscle homeostasis, playing a key role in sarcomere organization and mitochondrial function. Here, we have studied the impact of oxidants and cysteine-reactive agents on desmin behavior. Our results show that several reactive species and drugs induce covalent modifications of desmin in vitro, of which its single cysteine residue, C333, is an important target. Moreover, stimuli eliciting oxidative stress or lipoxidation, including H(2)O(2), 15-deoxy-prostaglandin J(2), and CoCl(2)-elicited chemical hypoxia, provoke desmin disorganization in H9c2 rat cardiomyoblasts transfected with wild-type desmin, which is partially attenuated in cells expressing a C333S mutant. Notably, in cells lacking other cytoplasmic intermediate filaments, network formation by desmin C333S appears less efficient than that of desmin wt, especially when these proteins are expressed as fluorescent fusion constructs. Nevertheless, in these cells, the desmin C333S organization is also protected from disruption by oxidants. Taken together, our results indicate that desmin is a target for oxidative and electrophilic stress, which elicit desmin remodeling conditioned by the presence of its single cysteine residue. MDPI 2023-08-31 /pmc/articles/PMC10525603/ /pubmed/37760006 http://dx.doi.org/10.3390/antiox12091703 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Moneo-Corcuera, Diego
Viedma-Poyatos, Álvaro
Stamatakis, Konstantinos
Pérez-Sala, Dolores
Desmin Reorganization by Stimuli Inducing Oxidative Stress and Electrophiles: Role of Its Single Cysteine Residue
title Desmin Reorganization by Stimuli Inducing Oxidative Stress and Electrophiles: Role of Its Single Cysteine Residue
title_full Desmin Reorganization by Stimuli Inducing Oxidative Stress and Electrophiles: Role of Its Single Cysteine Residue
title_fullStr Desmin Reorganization by Stimuli Inducing Oxidative Stress and Electrophiles: Role of Its Single Cysteine Residue
title_full_unstemmed Desmin Reorganization by Stimuli Inducing Oxidative Stress and Electrophiles: Role of Its Single Cysteine Residue
title_short Desmin Reorganization by Stimuli Inducing Oxidative Stress and Electrophiles: Role of Its Single Cysteine Residue
title_sort desmin reorganization by stimuli inducing oxidative stress and electrophiles: role of its single cysteine residue
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10525603/
https://www.ncbi.nlm.nih.gov/pubmed/37760006
http://dx.doi.org/10.3390/antiox12091703
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