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  Absolute Quantitative Profiling of the Key Metabolic Pathways in Slow and Fast Skeletal Muscle

Rakus, D., Gizak, A., Deshmukh, A., & Wisniewski, J. R. (2015). Absolute Quantitative Profiling of the Key Metabolic Pathways in Slow and Fast Skeletal Muscle. JOURNAL OF PROTEOME RESEARCH, 14(3), 1400-1411. doi:10.1021/pr5010357.

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 Creators:
Rakus, Dariusz1, Author
Gizak, Agnieszka1, Author
Deshmukh, Atul2, Author              
Wisniewski, Jacek R.2, Author              
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Free keywords: GLYCOLYTIC-ENZYMES; PROTEOMIC ANALYSIS; FIBER TYPES; IN-VIVO; FRUCTOSE 2,6-BISPHOSPHATE; PHOSPHOGLYCERATE MUTASE; GLYCOGEN-SYNTHASE; MASS-SPECTROMETRY; DEFICIENT MUSCLE; PROTEIN-KINASEglycolysis; fatty acid metabolism; carbohydrate metabolism; energy metabolism; label free quantitative proteomics; "total protein approach"; filter aided sample preparation; absolute protein quantitation;
 Abstract: Slow and fast skeletal muscles are composed of, respectively, mainly oxidative and glycolytic muscle fibers, which are the basic cellular motor units of the motility apparatus. They largely differ in excitability, contraction mechanism, and metabolism. Because of their pivotal role in body motion and homeostasis, the skeletal muscles have been extensively studied using biochemical and molecular biology approaches. Here we describe a simple analytical and computational approach to estimate titers of enzymes of basic metabolic pathways and proteins of the contractile machinery in the skeletal muscles. Proteomic analysis of mouse slow and fast muscles allowed estimation of the titers of enzymes involved in the carbohydrate, lipid, and energy metabolism. Notably, we observed that differences observed between the two muscle types occur simultaneously for all proteins involved in a specific process such as glycolysis, free fatty acid catabolism, Krebs cycle, or oxidative phosphorylation. These differences are in a good agreement with the well-established biochemical picture of the muscle types. We show a correlation between maximal activity and the enzyme titer, suggesting that change in enzyme concentration is a good proxy for its catalytic potential in vivo. As a consequence, proteomic profiling of enzyme titers can be used to monitor metabolic changes in cells. Additionally, quantitative data of structural proteins allowed studying muscle type specific cell architecture and its remodeling. The presented proteomic approach can be applied to study metabolism in any other tissue or cell line.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000350840900006
DOI: 10.1021/pr5010357
 Degree: -

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Title: JOURNAL OF PROTEOME RESEARCH
Source Genre: Journal
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Publ. Info: 1155 16TH ST, NW, WASHINGTON, DC 20036 USA : AMER CHEMICAL SOC
Pages: - Volume / Issue: 14 (3) Sequence Number: - Start / End Page: 1400 - 1411 Identifier: ISSN: 1535-3893