Top-down Mass Spectrometry of Sarcomeric Protein Post-translational Modifications from Non-human Primate Skeletal Muscle

• DOI: 10.1007/s13361-019-02139-0
• Publication Date: 2019-03-04T17:21:59Z
• Authors: Yutong Jin; Gary M. Diffee; Ricki J. Colman; Rozalyn M. Anderson; Ying Ge
• Keywords: Deamidation; Myofilament

Sarcomeric proteins, including myofilament and Z-disk play critical roles in regulating muscle contractile properties. A variety of isoforms post-translational modifications (PTMs) sarcomeric proteins have been shown to be associated with modulation functions the occurrence diseases. Non-human primates (NHPs) are excellent research models for sarcopenia, a disease alterations due their marked similarities humans. However, NHP skeletal not well characterized. To gain deeper understanding muscle, we employed top-down mass spectrometry (MS) conduct comprehensive analysis on PTMs rhesus macaque muscle. We identified 23 protein 46 proteoforms 6 18 from fast troponin T. Particularly, first time, novel PDZ/LIM domain isoform, PDLIM7, was characterized newly sequence. Moreover, also multiple these deamidation, methylation, acetylation, tri-methylation, phosphorylation, S-glutathionylation. Most PTM sites were localized, Asn13 deamidation MLC-2S; His73 methylation αactin; N-terminal acetylation most proteins; tri-methylation MLC-1S, MLC-1F, MLC-2S, MLC-2F; Ser14 phosphorylation Ser15 Ser16 MLC-2F. In summary, characterization achieved by analyzing intact MS approach.