Lang, Franziska, Khaghani, Solmaz, Tuerk, Clara, Wiederstein, Janica Lea, Hoelper, Soraya, Piller, Tanja, Nogara, Leonardo ORCID: 0000-0002-7009-8707, Blaauw, Bert, Guenther, Stefan, Mueller, Stefan, Braun, Thomas ORCID: 0000-0002-6165-4804 and Krueger, Marcus ORCID: 0000-0003-2008-4582 (2018). Single Muscle Fiber Proteomics Reveals Distinct Protein Changes in Slow and Fast Fibers during Muscle Atrophy. J. Proteome Res., 17 (10). S. 3333 - 3348. WASHINGTON: AMER CHEMICAL SOC. ISSN 1535-3907

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Abstract

Skeletal muscles are composed of heterogeneous collections of fibers with different metabolic profiles. With varied neuronal innervation and fiber-type compositions, each muscle fulfils specific functions and responds differently to stimuli and perturbations. We assessed individual fibers by mass spectrometry to dissect protein changes after loss of neuronal innervation due to section of the sciatic nerve in mice. This proteomics approach enabled us to quantify similar to 600 proteins per individual soleus and EDL (extensor digitorum longus) muscle fiber. Expression of myosin heavy chain (MyHC) in individual fibers enabled clustering of specific fiber types; comparison of fibers from control and denervated muscles with the same MyHC expression revealed restricted regulation of a total of 240 proteins in type-I, -II, or -IIb fibers 7 days after denervation. The levels of several mitochondrial and proteasomal proteins were significantly altered, indicating rapid adaption of metabolic processes after denervation. Furthermore, we observed fiber-type-specific regulation of proteins involved in calcium ion binding and transport, such as troponins, parvalbumin, and ATP2A2, indicating marked remodeling of muscle contractility after denervation. This study provides novel insight into how different muscle fiber types remodel their proteomes during muscular atrophy.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Lang, FranziskaUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Khaghani, SolmazUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Tuerk, ClaraUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Wiederstein, Janica LeaUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Hoelper, SorayaUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Piller, TanjaUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Nogara, LeonardoUNSPECIFIEDorcid.org/0000-0002-7009-8707UNSPECIFIED
Blaauw, BertUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Guenther, StefanUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Mueller, StefanUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Braun, ThomasUNSPECIFIEDorcid.org/0000-0002-6165-4804UNSPECIFIED
Krueger, MarcusUNSPECIFIEDorcid.org/0000-0003-2008-4582UNSPECIFIED
URN: urn:nbn:de:hbz:38-171237
DOI: 10.1021/acs.jproteome.8b00093
Journal or Publication Title: J. Proteome Res.
Volume: 17
Number: 10
Page Range: S. 3333 - 3348
Date: 2018
Publisher: AMER CHEMICAL SOC
Place of Publication: WASHINGTON
ISSN: 1535-3907
Language: English
Faculty: Faculty of Mathematics and Natural Sciences
Divisions: Faculty of Mathematics and Natural Sciences > Department of Biology > Institute for Genetics
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
MYOSIN HEAVY-CHAIN; AMINO-ACID-TRANSPORT; HUMAN SKELETAL-MUSCLE; ALPHA-B-CRYSTALLIN; SOLEUS MUSCLES; SARCOPLASMIC-RETICULUM; COMPUTATIONAL PLATFORM; DENERVATION ATROPHY; METABOLIC PATHWAYS; MASS-SPECTROMETRYMultiple languages
Biochemical Research MethodsMultiple languages
Refereed: Yes
URI: http://kups.ub.uni-koeln.de/id/eprint/17123

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