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Spatial Proteomic Approach to Characterize Skeletal Muscle Myofibers

Overview
Journal J Proteome Res
Specialty Biochemistry
Date 2020 Nov 30
PMID 33251806
Citations 7
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Abstract

Skeletal muscle myofibers have differential protein expression resulting in functionally distinct slow- and fast-twitch types. While certain protein classes are well-characterized, the depth of all proteins involved in this process is unknown. We utilized the Human Protein Atlas (HPA) and the HPASubC tool to classify mosaic expression patterns of staining across 49,600 unique tissue microarray (TMA) images using a visual proteomic approach. We identified 2164 proteins with potential mosaic expression, of which 1605 were categorized as "likely" or "real." This list included both well-known fiber-type-specific and novel proteins. A comparison of the 1605 mosaic proteins with a mass spectrometry (MS)-derived proteomic dataset of single human muscle fibers led to the assignment of 111 proteins to fiber types. We additionally used a multiplexed immunohistochemistry approach, a multiplexed RNA-ISH approach, and STRING v11 to further assign or suggest fiber types of newly characterized mosaic proteins. This visual proteomic analysis of mature skeletal muscle myofibers greatly expands the known repertoire of twitch-type-specific proteins.

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References
1.
Drexler H, Ruhs A, Konzer A, Mendler L, Bruckskotten M, Looso M . On marathons and Sprints: an integrated quantitative proteomics and transcriptomics analysis of differences between slow and fast muscle fibers. Mol Cell Proteomics. 2012; 11(6):M111.010801. PMC: 3433927. DOI: 10.1074/mcp.M111.010801. View

2.
Iresjo B, Lundholm K . Myosin heavy chain 2A and α-actin expression in human and murine skeletal muscles at feeding; particularly amino acids. J Transl Med. 2012; 10:238. PMC: 3542095. DOI: 10.1186/1479-5876-10-238. View

3.
Cheah J, Nieuwenhuis T, Halushka M . An expanded proteome of cardiac t-tubules. Cardiovasc Pathol. 2019; 42:15-20. PMC: 6732025. DOI: 10.1016/j.carpath.2019.05.001. View

4.
Gendusa R, Scalia C, Buscone S, Cattoretti G . Elution of High-affinity (>10-9 KD) Antibodies from Tissue Sections: Clues to the Molecular Mechanism and Use in Sequential Immunostaining. J Histochem Cytochem. 2014; 62(7):519-31. PMC: 4174624. DOI: 10.1369/0022155414536732. View

5.
Philips A, Pinelli M, de Bie C, Mustonen A, Maatta T, Arts H . Identification of C12orf4 as a gene for autosomal recessive intellectual disability. Clin Genet. 2016; 91(1):100-105. DOI: 10.1111/cge.12821. View