ArticleJournal of the American Society for Mass Spectrometry2019
Top-down Mass Spectrometry of Sarcomeric Protein Post-translational Modifications from Non-human Primate Skeletal Muscle.
Article in Journal of the American Society for Mass Spectrometry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 34 citations in OpenAlex.
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- Post-translational modifications of vertebrate striated muscle myosin heavy chains.Cytoskeleton (Hoboken, N.J.) · 2024Review
- Top-down proteomics of myosin light chain isoforms define chamber-specific expression in the human heart.Journal of molecular and cellular cardiology · 2023Article
- Myofilament-associated proteins with intrinsic disorder (MAPIDs) and their resolution by computational modeling.Quarterly reviews of biophysics · 2023Review
- Emerging chemistry and biology in protein glutathionylation.Current opinion in chemical biology · 2022Review
- Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches.Antioxidants (Basel, Switzerland) · 2022Review
- Fourier-transform ion cyclotron resonance mass spectrometry for characterizing proteoforms.Mass spectrometry reviews · 2022Review
- Size Exclusion Chromatography Strategies and MASH Explorer for Large Proteoform Characterization.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Post-translational Modification in Muscular Dystrophies.Advances in experimental medicine and biology · 2022Article
- Protein profile of fiber types in human skeletal muscle: a single-fiber proteomics study.Skeletal muscle · 2021Article
- Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases.Redox biology · 2021Review
- Inter-proteomic posttranslational modifications of the SARS-CoV-2 and the host proteins ‒ A new frontier.Experimental biology and medicine (Maywood, N.J.) · 2021Review
- Research on the Human Proteome Reaches a Major Milestone: >90% of Predicted Human Proteins Now Credibly Detected, According to the HUPO Human Proteome Project.Journal of proteome research · 2020Article
- Calorie Restriction and Aging in Humans.Annual review of nutrition · 2020Article
- Exoproteomics for Better UnderstandingToxins · 2020Review
- MASH Explorer: A Universal Software Environment for Top-Down Proteomics.Journal of proteome research · 2020Article
- Enhancing Top-Down Proteomics Data Analysis by Combining Deconvolution Results through a Machine Learning Strategy.Journal of the American Society for Mass Spectrometry · 2020Article
- Fiber type diversity in skeletal muscle explored by mass spectrometry-based single fiber proteomics.Histology and histopathology · 2020Review
- Ion Activation Methods for Peptides and Proteins.Analytical chemistry · 2020Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Sarcomeric proteins, including myofilament and Z-disk proteins, play critical roles in regulating muscle contractile properties. A variety of isoforms and post-translational modifications (PTMs) of sarcomeric proteins have been shown to be associated with modulation of muscle functions and the occurrence of muscle diseases. Non-human primates (NHPs) are excellent research models for sarcopenia, a disease associated with alterations in sarcomeric proteins, due to their marked similarities to humans. However, the sarcomeric proteins in NHP skeletal muscle have not been well characterized. To gain a deeper understanding of sarcomeric proteins in NHP skeletal muscle, we employed top-down mass spectrometry (MS) to conduct a comprehensive analysis on isoforms and PTMs of sarcomeric proteins in rhesus macaque skeletal muscle. We identified 23 protein isoforms with 46 proteoforms of sarcomeric proteins, including 6 isoforms with 18 proteoforms from fast skeletal troponin T. Particularly, for the first time, a novel PDZ/LIM domain protein isoform, PDLIM7, was characterized with a newly identified protein sequence. Moreover, we also identified multiple PTMs on these proteins, including deamidation, methylation, acetylation, tri-methylation, phosphorylation, and S-glutathionylation. Most PTM sites were localized, including Asn13 deamidation on MLC-2S; His73 methylation on αactin; N-terminal acetylation on most identified proteins; N-terminal tri-methylation on MLC-1S, MLC-1F, MLC-2S, and MLC-2F; Ser14 phosphorylation on MLC-2S; and Ser15 and Ser16 phosphorylation on MLC-2F. In summary, a comprehensive characterization of sarcomeric proteins including multiple isoforms and PTMs in NHP skeletal muscle was achieved by analyzing intact proteins in the top-down MS approach.
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