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  Proteomics Analysis of Skeletal Muscle from Leptin-Deficient ob/ob Mice Reveals Adaptive Remodeling of Metabolic Characteristics and Fiber Type Composition

Schonke, M., Bjornholm, M., Chibalin, A. V., Zierath, J. R., & Deshmukh, A. S. (2018). Proteomics Analysis of Skeletal Muscle from Leptin-Deficient ob/ob Mice Reveals Adaptive Remodeling of Metabolic Characteristics and Fiber Type Composition. Proteomics, 18(5-6): 1700375. doi:10.1002/pmic.201700375.

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 Creators:
Schonke, Milena1, Author
Bjornholm, Marie1, Author
Chibalin, Alexander V.1, Author
Zierath, Juleen R.1, Author
Deshmukh, Atul S.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: fatty acid oxidation insulin resistance metabolism mitochondria obesity
 Abstract: Skeletal muscle insulin resistance, an early metabolic defect in the pathogenesis of type 2 diabetes (T2D), may be a cause or consequence of altered protein expression profiles. Proteomics technology offers enormous promise to investigate molecular mechanisms underlying pathologies, however, the analysis of skeletal muscle is challenging. Using state‐of‐the‐art multienzyme digestion and filter‐aided sample preparation (MED‐FASP) and a mass spectrometry (MS)‐based workflow, we performed a global proteomics analysis of skeletal muscle from leptin‐deficient, obese, insulin resistant (ob/ob) and lean mice in mere two fractions in a short time (8 h per sample). We identified more than 6000 proteins with 118 proteins differentially regulated in obesity. This included protein kinases, phosphatases, and secreted and fiber type associated proteins. Enzymes involved in lipid metabolism in skeletal muscle from ob/ob mice were increased, providing evidence against reduced fatty acid oxidation in lipid‐induced insulin resistance. Mitochondrial and peroxisomal proteins, as well as components of pyruvate and lactate metabolism, were increased. Finally, the skeletal muscle proteome from ob/ob mice displayed a shift toward the “slow fiber type.” This detailed characterization of an obese rodent model of T2D demonstrates an efficient workflow for skeletal muscle proteomics, which may easily be adapted to other complex tissues.

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 Dates: 2018-03
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000428343700008
DOI: 10.1002/pmic.201700375
 Degree: -

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Title: Proteomics
  Alternative Title : Special Issue: Reviews 2018 ‐ Part I
Source Genre: Journal
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Publ. Info: Weinheim : WILEY-VCH
Pages: - Volume / Issue: 18 (5-6) Sequence Number: 1700375 Start / End Page: - Identifier: ISSN: 1615-9853
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000294310