Impaired energy metabolism of senescent muscle satellite cells is associated with oxidative modifications of glycolytic enzymes

Martín A Baraibar, Janek Hyzewicz, Adelina Rogowska-Wrzesinska, Anne-Laure Bulteau, Carina Prip-Buus, Gillian Butler-Browne, Bertrand Friguet

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Resumé

Accumulation of oxidized proteins is a hallmark of cellular and organismal aging. Adult muscle stem cell (or satellite cell) replication and differentiation is compromised with age contributing to sarcopenia. However, the molecular events related to satellite cell dysfunction during aging are not completely understood. In the present study we have addressed the potential impact of oxidatively modified proteins on the altered metabolism of senescent human satellite cells. By using a modified proteomics analysis we have found that proteins involved in protein quality control and glycolytic enzymes are the main targets of oxidation (carbonylation) and modification with advanced glycation/lipid peroxidation end products during the replicative senescence of satellite cells. Inactivation of the proteasome appeared to be a likely contributor to the accumulation of such damaged proteins. Metabolic and functional analyses revealed an impaired glucose metabolism in senescent cells. A metabolic shift leading to increased mobilization of non-carbohydrate substrates such as branched chain amino acids or long chain fatty acids was observed. Increased levels of acyl-carnitines indicated an increased turnover of storage and membrane lipids for energy production. Taken together, these results support a link between oxidative protein modifications and the altered cellular metabolism associated with the senescent phenotype of human myoblasts.

OriginalsprogEngelsk
TidsskriftAging
Vol/bind8
Udgave nummer12
Sider (fra-til)3375-3389
ISSN1945-4589
DOI
StatusUdgivet - 4. dec. 2016

Fingeraftryk

Energy Metabolism
Enzymes
Proteins
Cell Aging
Sarcopenia
Branched Chain Amino Acids
Proteasome Endopeptidase Complex
Membrane Lipids
Lipid Peroxidation
Cell Differentiation
Fatty Acids

Citer dette

Baraibar, Martín A ; Hyzewicz, Janek ; Rogowska-Wrzesinska, Adelina ; Bulteau, Anne-Laure ; Prip-Buus, Carina ; Butler-Browne, Gillian ; Friguet, Bertrand. / Impaired energy metabolism of senescent muscle satellite cells is associated with oxidative modifications of glycolytic enzymes. I: Aging. 2016 ; Bind 8, Nr. 12. s. 3375-3389.
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title = "Impaired energy metabolism of senescent muscle satellite cells is associated with oxidative modifications of glycolytic enzymes",
abstract = "Accumulation of oxidized proteins is a hallmark of cellular and organismal aging. Adult muscle stem cell (or satellite cell) replication and differentiation is compromised with age contributing to sarcopenia. However, the molecular events related to satellite cell dysfunction during aging are not completely understood. In the present study we have addressed the potential impact of oxidatively modified proteins on the altered metabolism of senescent human satellite cells. By using a modified proteomics analysis we have found that proteins involved in protein quality control and glycolytic enzymes are the main targets of oxidation (carbonylation) and modification with advanced glycation/lipid peroxidation end products during the replicative senescence of satellite cells. Inactivation of the proteasome appeared to be a likely contributor to the accumulation of such damaged proteins. Metabolic and functional analyses revealed an impaired glucose metabolism in senescent cells. A metabolic shift leading to increased mobilization of non-carbohydrate substrates such as branched chain amino acids or long chain fatty acids was observed. Increased levels of acyl-carnitines indicated an increased turnover of storage and membrane lipids for energy production. Taken together, these results support a link between oxidative protein modifications and the altered cellular metabolism associated with the senescent phenotype of human myoblasts.",
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Impaired energy metabolism of senescent muscle satellite cells is associated with oxidative modifications of glycolytic enzymes. / Baraibar, Martín A; Hyzewicz, Janek; Rogowska-Wrzesinska, Adelina; Bulteau, Anne-Laure; Prip-Buus, Carina; Butler-Browne, Gillian; Friguet, Bertrand.

I: Aging, Bind 8, Nr. 12, 04.12.2016, s. 3375-3389.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Impaired energy metabolism of senescent muscle satellite cells is associated with oxidative modifications of glycolytic enzymes

AU - Baraibar, Martín A

AU - Hyzewicz, Janek

AU - Rogowska-Wrzesinska, Adelina

AU - Bulteau, Anne-Laure

AU - Prip-Buus, Carina

AU - Butler-Browne, Gillian

AU - Friguet, Bertrand

PY - 2016/12/4

Y1 - 2016/12/4

N2 - Accumulation of oxidized proteins is a hallmark of cellular and organismal aging. Adult muscle stem cell (or satellite cell) replication and differentiation is compromised with age contributing to sarcopenia. However, the molecular events related to satellite cell dysfunction during aging are not completely understood. In the present study we have addressed the potential impact of oxidatively modified proteins on the altered metabolism of senescent human satellite cells. By using a modified proteomics analysis we have found that proteins involved in protein quality control and glycolytic enzymes are the main targets of oxidation (carbonylation) and modification with advanced glycation/lipid peroxidation end products during the replicative senescence of satellite cells. Inactivation of the proteasome appeared to be a likely contributor to the accumulation of such damaged proteins. Metabolic and functional analyses revealed an impaired glucose metabolism in senescent cells. A metabolic shift leading to increased mobilization of non-carbohydrate substrates such as branched chain amino acids or long chain fatty acids was observed. Increased levels of acyl-carnitines indicated an increased turnover of storage and membrane lipids for energy production. Taken together, these results support a link between oxidative protein modifications and the altered cellular metabolism associated with the senescent phenotype of human myoblasts.

AB - Accumulation of oxidized proteins is a hallmark of cellular and organismal aging. Adult muscle stem cell (or satellite cell) replication and differentiation is compromised with age contributing to sarcopenia. However, the molecular events related to satellite cell dysfunction during aging are not completely understood. In the present study we have addressed the potential impact of oxidatively modified proteins on the altered metabolism of senescent human satellite cells. By using a modified proteomics analysis we have found that proteins involved in protein quality control and glycolytic enzymes are the main targets of oxidation (carbonylation) and modification with advanced glycation/lipid peroxidation end products during the replicative senescence of satellite cells. Inactivation of the proteasome appeared to be a likely contributor to the accumulation of such damaged proteins. Metabolic and functional analyses revealed an impaired glucose metabolism in senescent cells. A metabolic shift leading to increased mobilization of non-carbohydrate substrates such as branched chain amino acids or long chain fatty acids was observed. Increased levels of acyl-carnitines indicated an increased turnover of storage and membrane lipids for energy production. Taken together, these results support a link between oxidative protein modifications and the altered cellular metabolism associated with the senescent phenotype of human myoblasts.

U2 - 10.18632/aging.101126

DO - 10.18632/aging.101126

M3 - Journal article

VL - 8

SP - 3375

EP - 3389

JO - Aging

JF - Aging

SN - 1945-4589

IS - 12

ER -