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. 2019 Jan 29;9:854. doi: 10.1038/s41598-018-36674-9

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Summary of changes in the blood metabolome during 58 hr of fasting. Prolonged human fasting causes a much more metabolically active state than previously recognized. It has long been known that prolonged fasting exhausts glycogen stores (glucose), consumes stored lipids as fuel substitutes, and stimulates gluconeogenesis. Fourteen confirmed markers such as butyrates, acylcarnitines, and BCAAs increased. In this study, 32 new fasting marker metabolites, were identified. They are catabolized as butyrates, organic acids, sugar metabolites relevant to gluconeogenesis, acylcarnitines, BCAAs, amino acids, purines/pyrimidines, antioxidants, and coenzymes. These novel markers reveal possible new metabolic aspects of fasting. Increased levels of organic acids may reflect increased mitochondrial activity, from which ROS are counteracted by antioxidant production; ergothioneine (EG), ophthalmic acid (OA), pentose-phosphate-pathway (PPP) and others. Purine and pyrimidine anabolism is increased for RNA and protein synthesis. Moreover, not only 3-HB (a histone deacetylase inhibitor), but also purines, pyrimidines, and 2-oxyglutarate (2-OG) function may participate in signal reprogramming.