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Mechanisms involved in the enhancement of mammalian target of rapamycin signalling and hypertrophy in skeletal muscle of myostatin-deficient mice

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Mechanisms involved in the enhancement of mammalian target of rapamycin signalling and hypertrophy in skeletal muscle of myostatin-deficient mice. / Lipina, Christopher; Kendall, Hannah; McPherron, Alexandra C.; Taylor, Peter M.; Hundal, Harinder S.

In: FEBS Letters, Vol. 584, No. 11, 03.06.2010, p. 2403-2408.

Research output: Contribution to journalArticle

Harvard

Lipina, C, Kendall, H, McPherron, AC, Taylor, PM & Hundal, HS 2010, 'Mechanisms involved in the enhancement of mammalian target of rapamycin signalling and hypertrophy in skeletal muscle of myostatin-deficient mice' FEBS Letters, vol 584, no. 11, pp. 2403-2408., 10.1016/j.febslet.2010.04.039

APA

Lipina, C., Kendall, H., McPherron, A. C., Taylor, P. M., & Hundal, H. S. (2010). Mechanisms involved in the enhancement of mammalian target of rapamycin signalling and hypertrophy in skeletal muscle of myostatin-deficient mice. FEBS Letters, 584(11), 2403-2408. 10.1016/j.febslet.2010.04.039

Vancouver

Lipina C, Kendall H, McPherron AC, Taylor PM, Hundal HS. Mechanisms involved in the enhancement of mammalian target of rapamycin signalling and hypertrophy in skeletal muscle of myostatin-deficient mice. FEBS Letters. 2010 Jun 3;584(11):2403-2408. Available from: 10.1016/j.febslet.2010.04.039

Author

Lipina, Christopher; Kendall, Hannah; McPherron, Alexandra C.; Taylor, Peter M.; Hundal, Harinder S. / Mechanisms involved in the enhancement of mammalian target of rapamycin signalling and hypertrophy in skeletal muscle of myostatin-deficient mice.

In: FEBS Letters, Vol. 584, No. 11, 03.06.2010, p. 2403-2408.

Research output: Contribution to journalArticle

Bibtex - Download

@article{11aca99053964cd7a05e3d506a9b4925,
title = "Mechanisms involved in the enhancement of mammalian target of rapamycin signalling and hypertrophy in skeletal muscle of myostatin-deficient mice",
keywords = "Growth differentiation factor-8, mTOR, p70S6K1, PKB/Akt, PROTEIN-KINASE-B, MYOBLAST DIFFERENTIATION, MYOTUBE HYPERTROPHY, INSULIN SENSITIVITY, WEIGHT-LOSS, IGF-I, EXPRESSION, AKT, PHOSPHORYLATION, RESISTANCE",
author = "Christopher Lipina and Hannah Kendall and McPherron, {Alexandra C.} and Taylor, {Peter M.} and Hundal, {Harinder S.}",
year = "2010",
doi = "10.1016/j.febslet.2010.04.039",
volume = "584",
number = "11",
pages = "2403--2408",
journal = "FEBS Letters",
issn = "0014-5793",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Mechanisms involved in the enhancement of mammalian target of rapamycin signalling and hypertrophy in skeletal muscle of myostatin-deficient mice

A1 - Lipina,Christopher

A1 - Kendall,Hannah

A1 - McPherron,Alexandra C.

A1 - Taylor,Peter M.

A1 - Hundal,Harinder S.

AU - Lipina,Christopher

AU - Kendall,Hannah

AU - McPherron,Alexandra C.

AU - Taylor,Peter M.

AU - Hundal,Harinder S.

PY - 2010/6/3

Y1 - 2010/6/3

N2 - <p>Myostatin deficiency leads to both an increased rate of protein synthesis and skeletal muscle hypertrophy. However, the mechanisms involved in mediating these effects are not yet fully understood. Here, we demonstrate that genetic loss of myostatin leads to enhanced muscle expression of both protein kinase B and mammalian target of rapamycin/S6K signalling components, consistent with their elevated activity. This is associated with a reduction in the expression of PGC1 alpha and COX IV, proteins which play important roles in maintaining mitochondrial function. Furthermore, we show that these changes in signalling and protein expression are largely independent of alterations in intramuscular amino acid content. Our findings, therefore, reveal potential new mechanisms and further contribute to our understanding of myostatin-regulated skeletal muscle growth and function. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.</p>

AB - <p>Myostatin deficiency leads to both an increased rate of protein synthesis and skeletal muscle hypertrophy. However, the mechanisms involved in mediating these effects are not yet fully understood. Here, we demonstrate that genetic loss of myostatin leads to enhanced muscle expression of both protein kinase B and mammalian target of rapamycin/S6K signalling components, consistent with their elevated activity. This is associated with a reduction in the expression of PGC1 alpha and COX IV, proteins which play important roles in maintaining mitochondrial function. Furthermore, we show that these changes in signalling and protein expression are largely independent of alterations in intramuscular amino acid content. Our findings, therefore, reveal potential new mechanisms and further contribute to our understanding of myostatin-regulated skeletal muscle growth and function. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.</p>

KW - Growth differentiation factor-8

KW - mTOR

KW - p70S6K1

KW - PKB/Akt

KW - PROTEIN-KINASE-B

KW - MYOBLAST DIFFERENTIATION

KW - MYOTUBE HYPERTROPHY

KW - INSULIN SENSITIVITY

KW - WEIGHT-LOSS

KW - IGF-I

KW - EXPRESSION

KW - AKT

KW - PHOSPHORYLATION

KW - RESISTANCE

U2 - 10.1016/j.febslet.2010.04.039

DO - 10.1016/j.febslet.2010.04.039

M1 - Article

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 11

VL - 584

SP - 2403

EP - 2408

ER -

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