Deep proteomics of mouse skeletal muscle enables quantitation of protein isoforms, metabolic pathways and transcription factors

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Deep proteomics of mouse skeletal muscle enables quantitation of protein isoforms, metabolic pathways and transcription factors. / Deshmukh, Atul S; Murgia, Marta; Nagaraja, Nagarjuna; Treebak, Jonas Thue; Cox, Jurgen; Mann, Matthias.

In: Molecular and Cellular Proteomics, Vol. 14, No. 4, 04.2015, p. 841-853.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Deshmukh, AS, Murgia, M, Nagaraja, N, Treebak, JT, Cox, J & Mann, M 2015, 'Deep proteomics of mouse skeletal muscle enables quantitation of protein isoforms, metabolic pathways and transcription factors', Molecular and Cellular Proteomics, vol. 14, no. 4, pp. 841-853. https://doi.org/10.1074/mcp.M114.044222

APA

Deshmukh, A. S., Murgia, M., Nagaraja, N., Treebak, J. T., Cox, J., & Mann, M. (2015). Deep proteomics of mouse skeletal muscle enables quantitation of protein isoforms, metabolic pathways and transcription factors. Molecular and Cellular Proteomics, 14(4), 841-853. https://doi.org/10.1074/mcp.M114.044222

Vancouver

Deshmukh AS, Murgia M, Nagaraja N, Treebak JT, Cox J, Mann M. Deep proteomics of mouse skeletal muscle enables quantitation of protein isoforms, metabolic pathways and transcription factors. Molecular and Cellular Proteomics. 2015 Apr;14(4):841-853. https://doi.org/10.1074/mcp.M114.044222

Author

Deshmukh, Atul S ; Murgia, Marta ; Nagaraja, Nagarjuna ; Treebak, Jonas Thue ; Cox, Jurgen ; Mann, Matthias. / Deep proteomics of mouse skeletal muscle enables quantitation of protein isoforms, metabolic pathways and transcription factors. In: Molecular and Cellular Proteomics. 2015 ; Vol. 14, No. 4. pp. 841-853.

Bibtex

@article{1eacfe97511443669d3b9ebfebad8472,
title = "Deep proteomics of mouse skeletal muscle enables quantitation of protein isoforms, metabolic pathways and transcription factors",
abstract = "Skeletal muscle constitutes 40% of individual body mass and plays vital roles in locomotion and whole-body metabolism. Proteomics of skeletal muscle is challenging due to highly abundant contractile proteins that interfere with detection of regulatory proteins. Using a state-of-the art mass spectrometric (MS) workflow and a strategy to map identifications from the C2C12 cell line model to tissues, we identified a total of 10,218 proteins, including skeletal muscle specific transcription factors like myod1 and myogenin and circadian clock proteins. We obtain absolute abundances for proteins expressed in a muscle cell line and skeletal muscle, which should serve as a valuable resource. Quantitation of protein isoforms of glucose uptake signaling pathways and in glucose and lipid metabolic pathways provides a detailed metabolic map of the cell line compare to tissue. This revealed unexpectedly complex regulation of AMP-activated protein kinase and insulin signaling in muscle tissue at the level of enzyme isoforms.",
author = "Deshmukh, {Atul S} and Marta Murgia and Nagarjuna Nagaraja and Treebak, {Jonas Thue} and Jurgen Cox and Matthias Mann",
note = "Copyright {\textcopyright} 2015, The American Society for Biochemistry and Molecular Biology.",
year = "2015",
month = apr,
doi = "10.1074/mcp.M114.044222",
language = "English",
volume = "14",
pages = "841--853",
journal = "Molecular and Cellular Proteomics",
issn = "1535-9476",
publisher = "American Society for Biochemistry and Molecular Biology",
number = "4",

}

RIS

TY - JOUR

T1 - Deep proteomics of mouse skeletal muscle enables quantitation of protein isoforms, metabolic pathways and transcription factors

AU - Deshmukh, Atul S

AU - Murgia, Marta

AU - Nagaraja, Nagarjuna

AU - Treebak, Jonas Thue

AU - Cox, Jurgen

AU - Mann, Matthias

N1 - Copyright © 2015, The American Society for Biochemistry and Molecular Biology.

PY - 2015/4

Y1 - 2015/4

N2 - Skeletal muscle constitutes 40% of individual body mass and plays vital roles in locomotion and whole-body metabolism. Proteomics of skeletal muscle is challenging due to highly abundant contractile proteins that interfere with detection of regulatory proteins. Using a state-of-the art mass spectrometric (MS) workflow and a strategy to map identifications from the C2C12 cell line model to tissues, we identified a total of 10,218 proteins, including skeletal muscle specific transcription factors like myod1 and myogenin and circadian clock proteins. We obtain absolute abundances for proteins expressed in a muscle cell line and skeletal muscle, which should serve as a valuable resource. Quantitation of protein isoforms of glucose uptake signaling pathways and in glucose and lipid metabolic pathways provides a detailed metabolic map of the cell line compare to tissue. This revealed unexpectedly complex regulation of AMP-activated protein kinase and insulin signaling in muscle tissue at the level of enzyme isoforms.

AB - Skeletal muscle constitutes 40% of individual body mass and plays vital roles in locomotion and whole-body metabolism. Proteomics of skeletal muscle is challenging due to highly abundant contractile proteins that interfere with detection of regulatory proteins. Using a state-of-the art mass spectrometric (MS) workflow and a strategy to map identifications from the C2C12 cell line model to tissues, we identified a total of 10,218 proteins, including skeletal muscle specific transcription factors like myod1 and myogenin and circadian clock proteins. We obtain absolute abundances for proteins expressed in a muscle cell line and skeletal muscle, which should serve as a valuable resource. Quantitation of protein isoforms of glucose uptake signaling pathways and in glucose and lipid metabolic pathways provides a detailed metabolic map of the cell line compare to tissue. This revealed unexpectedly complex regulation of AMP-activated protein kinase and insulin signaling in muscle tissue at the level of enzyme isoforms.

U2 - 10.1074/mcp.M114.044222

DO - 10.1074/mcp.M114.044222

M3 - Journal article

C2 - 25616865

VL - 14

SP - 841

EP - 853

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

SN - 1535-9476

IS - 4

ER -

ID: 130636173