Systemic vitamin intake impacting tissue proteomes
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(2020) 17:73
REVIEW
Open Access
Systemic vitamin intake impacting tissue proteomes Heesoo Jeong and Nathaniel M. Vacanti*
Abstract The kinetics and localization of the reactions of metabolism are coordinated by the enzymes that catalyze them. These enzymes are controlled via a myriad of mechanisms including inhibition/activation by metabolites, compartmentalization, thermodynamics, and nutrient sensing-based transcriptional or post-translational regulation; all of which are influenced as a network by the activities of metabolic enzymes and have downstream potential to exert direct or indirect control over protein abundances. Considering many of these enzymes are active only when one or more vitamin cofactors are present; the availability of vitamin cofactors likely yields a systems-influence over tissue proteomes. Furthermore, vitamins may influence protein abundances as nuclear receptor agonists, antioxidants, substrates for post-translational modifications, molecular signal transducers, and regulators of electrolyte homeostasis. Herein, studies of vitamin intake are explored for their contribution to unraveling vitamin influence over protein expression. As a body of work, these studies establish vitamin intake as a regulator of protein abundance; with the most powerful demonstrations reporting regulation of proteins directly related to the vitamin of interest. However, as a whole, the field has not kept pace with advances in proteomic platforms and analytical methodologies, and has not moved to validate mechanisms of regulation or potential for clinical application. Keywords: Proteomics, Big data, Vitamin, Metabolism, Precision nutrition, Molecular nutrition
Introduction Regulatory Mechanisms
Cellular metabolism is a system of chemical reactions in which cells harness the energy stored in the chemical bonds of substrate molecules to perform their biological functions, maintain homeostasis, or to synthesize building blocks for structural maintenance or cellular division. The kinetics of these reactions are dependent on the activity of the proteins which catalyze them; thus proteins are key modulators of metabolism. Metabolic activity also exerts network control over itself by a diverse array of mechanisms which finely tune protein expression responses via nutrient sensing machineries [1]. Products or intermediates of a metabolic pathway can inhibit or activate metabolic enzymes; e.g. malate inhibits the succinate dehydrogenase complex [2] and fructose* Correspondence: [email protected] Division of Nutritional Sciences, Cornell University, Ithaca, NY, USA
2,6-bisphosphate activates phosphofructokinase [3]. The oxidative status of a cell can drive the directionality of redox reactions and impact abundances of redox reactioncatalyzing proteins; e.g. the KEAP1/NRF2 network responds to oxidative stress by upregulating expression of antioxidant-functioning proteins [4]. Splice-variant or isozyme expression can impact relative pathway utilization at metabolic network nodes; e.g. splice variants and isozymes of pyru
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