Low proteasomal activity in fast skeletal muscle fibers is not associated with increased age-related oxidative damage.


Journal

Experimental gerontology
ISSN: 1873-6815
Titre abrégé: Exp Gerontol
Pays: England
ID NLM: 0047061

Informations de publication

Date de publication:
03 2019
Historique:
received: 24 05 2018
revised: 09 10 2018
accepted: 23 10 2018
pubmed: 28 10 2018
medline: 26 5 2020
entrez: 28 10 2018
Statut: ppublish

Résumé

The skeletal muscle is a crucial tissue for maintaining whole body homeostasis. Aging seems to have a disruptive effect on skeletal muscle homeostasis including proteostasis. However, how aging specifically impacts slow and fast twitch fiber types remains elusive. Muscle proteostasis is largely maintained by the proteasomal system. Here we characterized the proteasomal system in two different fiber types, using a non-sarcopenic aging model. By analyzing the proteasomal activity and amount, as well as the polyubiquitinated proteins and the level of protein oxidation in Musculus soleus (Sol) and Musculus extensor digitorum longus (EDL), we found that the slow twitch Sol muscle shows an overall higher respiratory and proteasomal activity in young and old animals. However, especially during aging the fast twitch EDL muscle reduces protein oxidation by an increase of antioxidant capacity. Thus, under adaptive non-sarcopenic conditions, the two fibers types seem to have different strategies to avoid age-related changes.

Identifiants

pubmed: 30367978
pii: S0531-5565(18)30335-8
doi: 10.1016/j.exger.2018.10.018
pii:
doi:

Substances chimiques

Antioxidants 0
Muscle Proteins 0
Polyubiquitin 120904-94-1
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

45-52

Informations de copyright

Copyright © 2018. Published by Elsevier Inc.

Auteurs

Raquel Fernando (R)

Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbrücke, 14558 Nuthetal, Germany.

Cathleen Drescher (C)

Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbrücke, 14558 Nuthetal, Germany; German Center for Cardiovascular Research (DZHK), 10117 Berlin, Germany.

Stefanie Deubel (S)

Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbrücke, 14558 Nuthetal, Germany.

Tobias Jung (T)

Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbrücke, 14558 Nuthetal, Germany.

Mario Ost (M)

Department of Physiology of Energy Metabolism, German Institute of Human Nutrition Potsdam-Rehbrücke, 14558 Nuthetal, Germany.

Susanne Klaus (S)

University of Potsdam, Institute of Nutritional Science, 14558 Nuthetal, Germany; Department of Physiology of Energy Metabolism, German Institute of Human Nutrition Potsdam-Rehbrücke, 14558 Nuthetal, Germany.

Tilman Grune (T)

Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbrücke, 14558 Nuthetal, Germany; German Center for Diabetes Research (DZD), 85764 München-Neuherberg, Germany; German Center for Cardiovascular Research (DZHK), 10117 Berlin, Germany; University of Potsdam, Institute of Nutritional Science, 14558 Nuthetal, Germany.

José Pedro Castro (JP)

Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbrücke, 14558 Nuthetal, Germany; German Center for Diabetes Research (DZD), 85764 München-Neuherberg, Germany; Faculty of Medicine, Department for Biomedicine, University of Porto, 4200-319, Portugal; Institute for Innovation and Health Research (I3S), Aging and Stress Group, R. Alfredo Allen, 4200-135 Porto, Portugal. Electronic address: jose.castro@dife.de.

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Classifications MeSH