Insulin/IGF1 signalling mediates the effects of β


Journal

Journal of cachexia, sarcopenia and muscle
ISSN: 2190-6009
Titre abrégé: J Cachexia Sarcopenia Muscle
Pays: Germany
ID NLM: 101552883

Informations de publication

Date de publication:
04 2019
Historique:
received: 15 05 2018
accepted: 18 12 2018
pubmed: 2 4 2019
medline: 4 6 2020
entrez: 2 4 2019
Statut: ppublish

Résumé

Stimulation of β Fed wild type (WT), 2-day fasted WT, muscle-specific insulin (INS) receptor (IR) knockout (M-IR In fed and fasted mice, one injection of FOR inhibited autophagosome formation (LC3-II content, 65%, P ≤ 0.05) that was paralleled by an increase in serum INS levels (4-fold to 25-fold, P ≤ 0.05) and the phosphorylation of Akt (4.4-fold to 6.5-fold, P ≤ 0.05) and ERK1/2 (50% to two-fold, P ≤ 0.05). This led to the suppression (40-70%, P ≤ 0.05) of the master regulators of atrophy, FoxOs, and the mRNA levels of their target genes. FOR enhanced (41%, P ≤ 0.05) protein synthesis only in fed condition and stimulated (4.4-fold to 35-fold, P ≤ 0.05) the prosynthetic Akt/mTOR/p70S6K pathway in both fed and fasted states. FOR effects on Akt signalling during fasting were blunted in both M-IR NS/IGF1 signalling is necessary for the anti-proteolytic and hypertrophic effects of in vivo β

Sections du résumé

BACKGROUND
Stimulation of β
METHODS
Fed wild type (WT), 2-day fasted WT, muscle-specific insulin (INS) receptor (IR) knockout (M-IR
RESULTS
In fed and fasted mice, one injection of FOR inhibited autophagosome formation (LC3-II content, 65%, P ≤ 0.05) that was paralleled by an increase in serum INS levels (4-fold to 25-fold, P ≤ 0.05) and the phosphorylation of Akt (4.4-fold to 6.5-fold, P ≤ 0.05) and ERK1/2 (50% to two-fold, P ≤ 0.05). This led to the suppression (40-70%, P ≤ 0.05) of the master regulators of atrophy, FoxOs, and the mRNA levels of their target genes. FOR enhanced (41%, P ≤ 0.05) protein synthesis only in fed condition and stimulated (4.4-fold to 35-fold, P ≤ 0.05) the prosynthetic Akt/mTOR/p70S6K pathway in both fed and fasted states. FOR effects on Akt signalling during fasting were blunted in both M-IR
CONCLUSIONS
NS/IGF1 signalling is necessary for the anti-proteolytic and hypertrophic effects of in vivo β

Identifiants

pubmed: 30932373
doi: 10.1002/jcsm.12395
pmc: PMC6463755
doi:

Substances chimiques

Adrenergic beta-2 Receptor Agonists 0
Insulin 0
Muscle Proteins 0
Insulin-Like Growth Factor I 67763-96-6
Proto-Oncogene Proteins c-akt EC 2.7.11.1

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

455-475

Subventions

Organisme : NIDDK NIH HHS
ID : K08 DK100543
Pays : United States
Organisme : NIDDK NIH HHS
ID : P30 DK036836
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK055545
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK033201
Pays : United States

Informations de copyright

© 2019 The Authors. Journal of Cachexia, Sarcopenia and Muscle published by John Wiley & Sons Ltd on behalf of the Society on Sarcopenia, Cachexia and Wasting Disorders.

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Auteurs

Dawit A Gonçalves (DA)

Department of Physiology, Ribeirão Preto Medical School/University of São Paulo, Ribeirão Preto, SP, Brazil.
Department of Biochemistry/Immunology, Ribeirão Preto Medical School/University of São Paulo, Ribeirão Preto, SP, Brazil.
Department of Biomedical Sciences, University of Padova, Padova, Italy.

Wilian A Silveira (WA)

Department of Physiology, Ribeirão Preto Medical School/University of São Paulo, Ribeirão Preto, SP, Brazil.

Leandro H Manfredi (LH)

Department of Physiology, Ribeirão Preto Medical School/University of São Paulo, Ribeirão Preto, SP, Brazil.

Flávia A Graça (FA)

Department of Physiology, Ribeirão Preto Medical School/University of São Paulo, Ribeirão Preto, SP, Brazil.

Andrea Armani (A)

Department of Biomedical Sciences, University of Padova, Padova, Italy.
Venetian Institute of Molecular Medicine, Padova, Italy.

Enrico Bertaggia (E)

Department of Biomedical Sciences, University of Padova, Padova, Italy.
Venetian Institute of Molecular Medicine, Padova, Italy.

Brian T O Neill (BT)

Section on Integrative Physiology and Metabolism, Joslin Diabetes Center, Harvard Medical School, Boston, MA, USA.

Natalia Lautherbach (N)

Department of Physiology, Ribeirão Preto Medical School/University of São Paulo, Ribeirão Preto, SP, Brazil.

Juliano Machado (J)

Department of Physiology, Ribeirão Preto Medical School/University of São Paulo, Ribeirão Preto, SP, Brazil.

Leonardo Nogara (L)

Department of Biomedical Sciences, University of Padova, Padova, Italy.
Venetian Institute of Molecular Medicine, Padova, Italy.

Marcelo G Pereira (MG)

Department of Biomedical Sciences, University of Padova, Padova, Italy.

Diletta Arcidiacono (D)

Digestive Endoscopy Unit, Veneto Institute of Oncology IOV-IRCCS, Padova, Italy.

Stefano Realdon (S)

Digestive Endoscopy Unit, Veneto Institute of Oncology IOV-IRCCS, Padova, Italy.

C Ronald Kahn (CR)

Section on Integrative Physiology and Metabolism, Joslin Diabetes Center, Harvard Medical School, Boston, MA, USA.

Marco Sandri (M)

Department of Biomedical Sciences, University of Padova, Padova, Italy.
Venetian Institute of Molecular Medicine, Padova, Italy.
Myology Center, University of Padova, Padova, Italy.

Isis C Kettelhut (IC)

Department of Physiology, Ribeirão Preto Medical School/University of São Paulo, Ribeirão Preto, SP, Brazil.
Department of Biochemistry/Immunology, Ribeirão Preto Medical School/University of São Paulo, Ribeirão Preto, SP, Brazil.

Luiz Carlos C Navegantes (LCC)

Department of Physiology, Ribeirão Preto Medical School/University of São Paulo, Ribeirão Preto, SP, Brazil.

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Classifications MeSH