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UBE2B is implicated in myofibrillar protein loss in catabolic C2C12 myotubes

BACKGROUND: Skeletal muscle protein loss is an adaptive response to various patho‐physiological situations, and the ubiquitin proteasome system (UPS) is responsible for the degradation of the bulk of muscle proteins. The role of E2 ubiquitin‐conjugating enzymes is still poorly understood in skeletal...

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Autores principales: Polge, Cécile, Leulmi, Roza, Jarzaguet, Marianne, Claustre, Agnes, Combaret, Lydie, Béchet, Daniel, Heng, Anne‐Elisabeth, Attaix, Didier, Taillandier, Daniel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4864198/
https://www.ncbi.nlm.nih.gov/pubmed/27239408
http://dx.doi.org/10.1002/jcsm.12060
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author Polge, Cécile
Leulmi, Roza
Jarzaguet, Marianne
Claustre, Agnes
Combaret, Lydie
Béchet, Daniel
Heng, Anne‐Elisabeth
Attaix, Didier
Taillandier, Daniel
author_facet Polge, Cécile
Leulmi, Roza
Jarzaguet, Marianne
Claustre, Agnes
Combaret, Lydie
Béchet, Daniel
Heng, Anne‐Elisabeth
Attaix, Didier
Taillandier, Daniel
author_sort Polge, Cécile
collection PubMed
description BACKGROUND: Skeletal muscle protein loss is an adaptive response to various patho‐physiological situations, and the ubiquitin proteasome system (UPS) is responsible for the degradation of the bulk of muscle proteins. The role of E2 ubiquitin‐conjugating enzymes is still poorly understood in skeletal muscle. METHODS: We screened for E2s expression levels in C2C12 myotubes submitted to the catabolic glucocorticoid dexamethasone (Dex). RESULTS: One micromolar Dex induced an accumulation of proteasome substrates (polyUb conjugates) and an overexpression of the muscle‐specific E3 ligase MuRF1 and of six E2 enzymes, UBE2A, UBE2B, UBE2D1, UBE2D2, UBE2G1, and UBE2J1. However, only MuRF1 and UBE2B were sensitive to mild catabolic conditions (0.16 μM Dex). UBE2B knockdown induced a sharp decrease of total (−18%) and K48 (−28%) Ub conjugates, that is, proteasome substrates, indicating an important role of UBE2B in the overall protein breakdown in catabolic myotubes. CONCLUSIONS: Interestingly, these results indicate an important role of UBE2B on muscle protein homeostasis during catabolic conditions.
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spelling pubmed-48641982016-05-27 UBE2B is implicated in myofibrillar protein loss in catabolic C2C12 myotubes Polge, Cécile Leulmi, Roza Jarzaguet, Marianne Claustre, Agnes Combaret, Lydie Béchet, Daniel Heng, Anne‐Elisabeth Attaix, Didier Taillandier, Daniel J Cachexia Sarcopenia Muscle Original Articles BACKGROUND: Skeletal muscle protein loss is an adaptive response to various patho‐physiological situations, and the ubiquitin proteasome system (UPS) is responsible for the degradation of the bulk of muscle proteins. The role of E2 ubiquitin‐conjugating enzymes is still poorly understood in skeletal muscle. METHODS: We screened for E2s expression levels in C2C12 myotubes submitted to the catabolic glucocorticoid dexamethasone (Dex). RESULTS: One micromolar Dex induced an accumulation of proteasome substrates (polyUb conjugates) and an overexpression of the muscle‐specific E3 ligase MuRF1 and of six E2 enzymes, UBE2A, UBE2B, UBE2D1, UBE2D2, UBE2G1, and UBE2J1. However, only MuRF1 and UBE2B were sensitive to mild catabolic conditions (0.16 μM Dex). UBE2B knockdown induced a sharp decrease of total (−18%) and K48 (−28%) Ub conjugates, that is, proteasome substrates, indicating an important role of UBE2B in the overall protein breakdown in catabolic myotubes. CONCLUSIONS: Interestingly, these results indicate an important role of UBE2B on muscle protein homeostasis during catabolic conditions. John Wiley and Sons Inc. 2015-11-19 2016-06 /pmc/articles/PMC4864198/ /pubmed/27239408 http://dx.doi.org/10.1002/jcsm.12060 Text en © 2015 The Authors. Journal of Cachexia, Sarcopenia and Muscle published by John Wiley & Sons Ltd on behalf of the Society of Sarcopenia, Cachexia and Wasting Disorders This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Original Articles
Polge, Cécile
Leulmi, Roza
Jarzaguet, Marianne
Claustre, Agnes
Combaret, Lydie
Béchet, Daniel
Heng, Anne‐Elisabeth
Attaix, Didier
Taillandier, Daniel
UBE2B is implicated in myofibrillar protein loss in catabolic C2C12 myotubes
title UBE2B is implicated in myofibrillar protein loss in catabolic C2C12 myotubes
title_full UBE2B is implicated in myofibrillar protein loss in catabolic C2C12 myotubes
title_fullStr UBE2B is implicated in myofibrillar protein loss in catabolic C2C12 myotubes
title_full_unstemmed UBE2B is implicated in myofibrillar protein loss in catabolic C2C12 myotubes
title_short UBE2B is implicated in myofibrillar protein loss in catabolic C2C12 myotubes
title_sort ube2b is implicated in myofibrillar protein loss in catabolic c2c12 myotubes
topic Original Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4864198/
https://www.ncbi.nlm.nih.gov/pubmed/27239408
http://dx.doi.org/10.1002/jcsm.12060
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