Abstract

Here we present original data related to the research paper entitled “Proteome analysis in dystrophic mdx mouse muscle reveals a drastic alteration of Key Metabolic and Contractile Proteins after chronic exercise and the potential modulation by anti-oxidant compounds” (Gamberi et al., 2018) [1]. The dystrophin-deficient mdx mouse is the most common animal model for Duchenne muscular dystrophy. The mdx mice phenotype of the disorder is milder than in human sufferers and it can be worsened by chronic treadmill exercise. Apocynin and taurine are two antioxidant compounds proved to be beneficial on some pathology related parameters (Schröder and Schoser, 2009) [2]. This article reports the detailed proteomic data on protein abundance alterations, in tibialis anterior muscle of mdx mice, induced by chronic exercise protocol. A selected group of mdx mice was also treated with apocynin and taurine during this protocol. Detailed MS data, comparison between mdx vs wild type, exercised mdx vs wild type, and complete analysis of spot variation are provided. Furthermore, in wild type mice subjected to the same exercise protocol, the abundance of key proteins, resulted modified in exercised mdx, were analyzed by western blot.

Highlights

  • 34 Triosephosphate isomerase P17751[21-32] K.DFNMPLTISR.I [37-69] K.AAQSQLSQGDLVVAIDGVNT DTMTHLEAQNK.I [70-83] K.SASYNLSLTLQK.S [21-32] K.DFNMPLTISR.I [273-294] R.ILAQMTGTEFMQDPDEE ALR.R [42-57] R.DVMLEELSLLTNR.G [69-90] K.FIYENHPDVFSDSSMDHFQK

  • We present original data related to the research paper entitled “Proteome analysis in dystrophic mdx mouse muscle reveals a drastic alteration of Key Metabolic and Contractile Proteins after chronic exercise and the potential modulation by anti-oxidant compounds” (Gamberi et al, 2018) [1]

  • Male mdx mice divided in: -sedentary mdx mice -exercised mdx mice - mdx exercised mice treated with taurine -mdx exercised mice treated with apocynin -C57/BL wild-type mice exercised and control

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Summary

34 Triosephosphate isomerase P17751

[21-32] K.DFNMPLTISR.I [37-69] K.AAQSQLSQGDLVVAIDGVNT DTMTHLEAQNK.I [70-83] K.SASYNLSLTLQK.S [21-32] K.DFNMPLTISR.I [273-294] R.ILAQMTGTEFMQDPDEE ALR.R [42-57] R.DVMLEELSLLTNR.G [69-90] K.FIYENHPDVFSDSSMDHFQK. F [61-76] K.IPEGEKVDFDDIQK.K [159-175] K.ALSSMGANYSSYLAK.A [61-76] K.IPEGEKVDFDDIQK.K [159-175] K.ALSSMGANYSSYLAK.A [31-42] K.EAFTVIDQNR.D [41-52] R.DGIIDKEDLR.D [63-73] K.NEELDAMMK.E [92-106] K.GADPEDVITGAFK.V [31-42] K.EAFTVIDQNR.D [41-52] R.DGIIDKEDLR.D [92-106] K.GADPEDVITGAFK.V [97-116] R.VAPEEHPTLLTEAPLNPK.A [240-257] K.SYELPDGQVITIGNER.F [25-46] R.LIVDEAINEDNSVVSLSQPK.M [295-313] K.NAPAIIFIDELDAIAPK.R [28-43] K.GILAADESTGSIAK.R [111-135] K.GVVPLAGTNGETTTQGLDG LSER.C [173-201] R.YASICQQNGIVPIVEPEILPD GDHDLK.R [56-65] K.FFVGGNWK.M

70 Adenylate kinase isoenzyme 1
51 TFNSYMKEWE ELFVNNNYLA TVRQKGINGQ LRSSRFRSIC WKLFLCVLPQ
Comparison with wt strain
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