Functional Food for Sarcopenia: Investigating the Impact of Myostatin Epitope Fusion Protein in Elderly Mice using Probiotic Bacillus subtilis

References

• Aiello, D., K. Patel, and E. Lasagna. 2018. The myostatin gene: An overview of mechanisms of action and its relevance to livestock animals. Anim. Genet. 49 (6):505–519. doi:10.1111/age.12696.
   PubMed Web of Science ®Google Scholar
• Artaza, J. N., S. Bhasin, T. R. Magee, S. Reisz-Porszasz, R. Shen, N. P. Groome, M. Fareez Meerasahib, and N. F. Gonzalez-Cadavid. 2005. Myostatin inhibits myogenesis and promotes adipogenesis in C3H 10T(1/2) mesenchymal multipotent cells. Endocrinology 146 (8):3547–3557. doi:10.1210/en.2005-0362.
   PubMed Web of Science ®Google Scholar
• Beaudart, C., R. Rizzoli, O. Bruyère, J.-Y. Reginster, and E. Biver. 2014. Sarcopenia: Burden and challenges for public health. Arch. Belg. 72 (1):45. doi:10.1186/2049-3258-72-45.
   Google Scholar
• Cruz-Jentoft, A. J., G. Bahat, J. Bauer, Y. Boirie, O. Bruyère, T. Cederholm, C. Cooper, F. Landi, Y. Rolland, A. A. Sayer, et al. 2019. Sarcopenia: Revised European consensus on definition and diagnosis. Age Ageing 48(1):16–31. doi:10.1093/ageing/afy169.
   PubMed Web of Science ®Google Scholar
• Cruz-Jentoft, A. J., J. Pierre Baeyens, J. M. Bauer, Y. Boirie, T. Cederholm, F. Landi, F. C. Martin, J.-P. Michel, Y. Rolland, S. M. Schneider, et al. 2010. Sarcopenia: European consensus on definition and diagnosis: Report of the European working group on sarcopenia in older people. Age Ageing 39(4):412–423. doi:10.1093/ageing/afq034.
   PubMed Web of Science ®Google Scholar
• Feldman, B. J., R. S. Streeper, R. V. Farese, and K. R. Yamamoto. 2006. Myostatin modulates adipogenesis to generate adipocytes with favorable metabolic effects. Proc. Natl. Acad. Sci. USA 103 (42):15675–15680. doi:10.1073/pnas.0607501103.
   PubMed Web of Science ®Google Scholar
• Friehs, K. 2004. Plasmid copy number and plasmid stability. In New trends and developments in biochemical engineering, ed. T. Scheper, 47–82. Berlin, Heidelberg: Springer Advances in Biochemical Engineering. doi:10.1007/b12440.
   Google Scholar
• Granato, D., F. J. Barba, D. Bursać Kovačević, J. M. Lorenzo, A. G. Cruz, and P. Putnik. 2020. Functional foods: Product development, technological trends, efficacy testing, and safety. Ann. Rev. Food Sci. Technol. 11 (1):93–118. doi:10.1146/annurev-food-032519-051708.
   PubMedGoogle Scholar
• Guo, W., J. Flanagan, R. Jasuja, J. Kirkland, L. Jiang, and S. Bhasin. 2008. The effects of myostatin on adipogenic differentiation of human bone marrow-derived mesenchymal stem cells are mediated through cross-communication between Smad3 and Wnt/β-catenin signaling pathways. J. Biol. Chem. 283 (14):9136–9145. doi:10.1074/jbc.M708968200.
   PubMed Web of Science ®Google Scholar
• Hill, C., F. Guarner, G. Reid, G. R. Gibson, D. J. Merenstein, B. Pot, L. Morelli, R. B. Canani, H. J. Flint, S. Salminen, et al. 2014. The international scientific association for probiotics and prebiotics consensus statement on the scope and appropriate use of the term probiotic. Nat. Rev. Gastro. Hepat. 11(8):506–514. doi:10.1038/nrgastro.2014.66.
   PubMed Web of Science ®Google Scholar
• Hjorth, M., S. Pourteymour, S. W. Görgens, T. M. Langleite, S. Lee, T. Holen, H. L. Gulseth, K. I. Birkeland, J. Jensen, C. A. Drevon, et al. 2016. Myostatin in relation to physical activity and dysglycaemia and its effect on energy metabolism in human skeletal muscle cells. Acta Physiol. 217(1):45–60. doi:10.1111/apha.12631.
   PubMed Web of Science ®Google Scholar
• Hoa, N. T., L. Baccigalupi, A. Huxham, A. Smertenko, P. Hung Van, S. Ammendola, E. Ricca, and S. M. Cutting. 2000. Characterization of bacillus species used for oral bacteriotherapy and bacterioprophylaxis of gastrointestinal disorders. Appl. Environ. Microb. 66 (12):5241–5247. doi:10.1128/AEM.66.12.5241-5247.2000.
   PubMed Web of Science ®Google Scholar
• Kaur, S., and M. Das. 2011. Functional foods: An overview. Food. Sci. Biotechnol. 20 (4):861. doi:10.1007/s10068-011-0121-7.
   Web of Science ®Google Scholar
• KernéKernéIs, S., A. Bogdanova, J.-P. Kraehenbuhl, and E. Pringault. 1997. Conversion by peyer’s patch lymphocytes of human enterocytes into M cells that transport bacteria. Science 277 (5328):949–952. doi:10.1126/science.277.5328.949.
   PubMed Web of Science ®Google Scholar
• Kim, H. S., L. Liang, R. G. Dean, D. B. Hausman, D. L. Hartzell, and C. A. Baile. 2001. Inhibition of preadipocyte differentiation by myostatin treatment in 3T3-L1 cultures. Biochem. Bioph. Res. Co. 281 (4):902–906. doi:10.1006/bbrc.2001.4435.
   PubMed Web of Science ®Google Scholar
• Kim, S.-H., K.-W. Seo, J. Kim, K.-Y. Lee, and Y.-S. Jang. 2010. The M cell-targeting ligand promotes antigen delivery and induces antigen-specific immune responses in mucosal vaccination. J. Immunol. 185 (10):5787–5795. doi:10.4049/jimmunol.0903184.
   PubMed Web of Science ®Google Scholar
• Kim, S.-H., and Y.-S. Jang. 2014. Antigen targeting to M cells for enhancing the efficacy of mucosal vaccines. Exp. Mol. Med. 46 (3):e85. doi:10.1038/emm.2013.165.
   PubMedGoogle Scholar
• Kobayashi, K. S., and P. J. van den Elsen. 2012. NLRC5: A key regulator of MHC class I-Dependent immune responses. Nat. Rev. Immunol. 12 (12):813–820. doi:10.1038/nri3339.
   PubMed Web of Science ®Google Scholar
• Lee, S.-J. 2004. Regulation of muscle mass by myostatin. Annu. Rev. Cell Dev. Biol. 20 (1):61–86. doi:10.1146/annurev.cellbio.20.012103.135836.
   PubMedGoogle Scholar
• Lin, J., H. Wu, P. T. Tarr, C.-Y. Zhang, Z. Wu, O. Boss, L. F. Michael, P. Puigserver, E. Isotani, E. N. Olson, et al. 2002. Transcriptional Co-activator PGC-1α drives the formation of slow-twitch muscle fibres. Nature 418 (6899):797–801. doi:10.1038/nature00904.
   PubMed Web of Science ®Google Scholar
• McPherron, A. C., and S.-J. Lee. 2002. Suppression of body fat accumulation in myostatin-deficient mice. J. Clin. Invest. 109 (5):595–601. doi:10.1172/JCI0213562.
   PubMed Web of Science ®Google Scholar
• McPherron, A. C., A. M. Lawler, and S.-J. Lee. 1997. Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member. Nature 387 (6628):83–90. doi:10.1038/387083a0.
   PubMed Web of Science ®Google Scholar
• Morissette, M. R., J. C. Stricker, M. A. Rosenberg, C. Buranasombati, E. B. Levitan, M. A. Mittleman, and A. Rosenzweig. 2009. Effects of myostatin deletion in aging mice. Aging Cell 8 (5):573–583. doi:10.1111/j.1474-9726.2009.00508.x.
   PubMed Web of Science ®Google Scholar
• Neutra, M. R., and P. A. Kozlowski. 2006. Mucosal vaccines: The promise and the challenge. Nat. Rev. Immunol. 6 (2):148–158. doi:10.1038/nri1777.
   PubMed Web of Science ®Google Scholar
• Raschke, S., and J. Eckel. 2013. Adipo-myokines: Two sides of the same coin–mediators of inflammation and mediators of exercise. Mediators Inflamm. 2013:320724. doi:10.1155/2013/320724.
   PubMed Web of Science ®Google Scholar
• Rebbapragada, A., H. Benchabane, J. L. Wrana, A. J. Celeste, and L. Attisano. 2003. Myostatin signals through a transforming growth factor beta-like signaling pathway to block adipogenesis. Mol. Cell. Biol. 23 (20):7230–7242. doi:10.1128/MCB.23.20.7230-7242.2003.
   PubMed Web of Science ®Google Scholar
• Ricca, E., L. Baccigalupi, G. Cangiano, M. De Felice, and R. Isticato. 2014. Mucosal vaccine delivery by non-recombinant spores of Bacillus Subtilis. Microb. Cell Fact. 13 (August):115. doi:10.1186/PREACCEPT-4933865371330529.
   PubMedGoogle Scholar
• Souza, R. D. D., M. Tavares Batista, W. Barros Luiz, R. Ciro Marques Cavalcante, J. Henrique Amorim, R. Sales Pereira Bizerra, E. Gimenes Martins, L. C. D. S. Ferreira, and M. M. Rodrigues. 2014. Bacillus Subtilis spores as vaccine adjuvants: Further insights into the mechanisms of action. PLOS ONE 9 (1):e87454. doi:10.1371/journal.pone.0087454.
   PubMed Web of Science ®Google Scholar
• Toes, R. E., A. K. Nussbaum, S. Degermann, M. Schirle, N. P. Emmerich, M. Kraft, C. Laplace, A. Zwinderman, T. P. Dick, J. Müller, et al. 2001. Discrete cleavage motifs of constitutive and immunoproteasomes revealed by quantitative analysis of cleavage products. J. Exp. Med. 194(1):1–12. doi:10.1084/jem.194.1.1.
   PubMed Web of Science ®Google Scholar
• Vos, W. M. D. 1999. Safe and sustainable systems for food-grade fermentations by genetically modified lactic acid bacteria. Int. Dairy J. 9 (1):3–10. doi:10.1016/S0958-6946(99)00038-2.
   Web of Science ®Google Scholar
• Wang, J.-P., C.-M. Yeh, and Y.-C. Tsai. 2006. Improved subtilisin YaB production in Bacillus Subtilis using engineered synthetic expression control sequences. J. Agric. Food Chem. 54 (25):9405–9410. doi:10.1021/jf061982f.
   PubMed Web of Science ®Google Scholar
• Yan, F., and D. B. Polk. 2011. Probiotics and immune health. Curr. Opin. Gastroenterol. 27 (6):496–501. doi:10.1097/MOG.0b013e32834baa4d.
   PubMed Web of Science ®Google Scholar
• Yeh, C. M., C. K. Yeh, X. Y. Hsu, Q. M. Luo, and M. Y. Lin. 2008. Extracellular expression of a functional recombinant ganoderma lucidium immunomodulatory protein by Bacillus Subtilis and Lactococcus Lactis. Appl. Environ. Microbiol. 74 (4):1039–1049. doi:10.1128/AEM.01547-07.
   PubMed Web of Science ®Google Scholar
• Zhao, B., R. J. Wall, and J. Yang. 2005. Transgenic expression of myostatin propeptide prevents diet-induced obesity and insulin resistance. Biochem. Biophys. Res. Comm. 337 (1):248–255. doi:10.1016/j.bbrc.2005.09.044.
   PubMed Web of Science ®Google Scholar
• Zimmers, T. A., M. V. Davies, L. G. Koniaris, P. Haynes, A. F. Esquela, K. N. Tomkinson, A. C. McPherron, N. M. Wolfman, and S.-J. Lee. 2002. Induction of cachexia in mice by systemically administered myostatin. Science 296 (5572):1486–1488. doi:10.1126/science.1069525.
   PubMed Web of Science ®Google Scholar