Pyruvate cellular uptake and enzymatic conversion probed by dissolution DNP‐NMR: the impact of overexpressed membrane transporters. (5th January 2017)

• Record Type: Journal Article
• Authors: Balzan, Riccardo; Fernandes, Laetitia; Pidial, Laetitia; Comment, Arnaud; Tavitian, Bertrand; Vasos, Paul R.
• Is Part Of: Magnetic resonance in chemistry. Volume 55:Number 6(2017:Jun.)
• Page Start: 579
• Page End: 583
• Publication Date: 2017-01-05
• Subjects: dissolution dynamic nuclear polarization (d‐DNP) -- nuclear magnetic resonance (NMR) -- lactate dehydrogenase (LDH) -- rodent cancer cells -- metabolism; Nuclear magnetic resonance spectroscopy -- Periodicals; Chemistry, Organic -- Periodicals; Magnetic resonance -- Periodicals; 538.36
• DOI: 10.1002/mrc.4553
• Languages: English
• ISSNs: 0749-1581

Abstract

Abstract : Pyruvate membrane crossing and its lactate dehydrogenase‐mediated conversion to lactate in cells featuring different levels of expression of membrane monocarboxylate transporters (MCT4) were probed by dissolution dynamic nuclear polarization‐enhanced NMR. Hyperpolarized 13 C‐1‐labeled pyruvate was transferred to suspensions of rodent tumor cell carcinoma, cell line 39. The pyruvate‐to‐lactate conversion rate monitored by dissolution dynamic nuclear polarization‐NMR in carcinoma cells featuring native MCT4 expression level was lower than the rate observed for cells in which the human MCT4 gene was overexpressed. The enzymatic activity of lactate dehydrogenase was also assessed in buffer solutions, following the real‐time pyruvate‐to‐lactate conversion speeds at different enzyme concentrations. Copyright © 2016 John Wiley & Sons, Ltd. Abstract : The lactate nuclear magnetic resonance signal stemming from dynamic nuclear polarization‐hyperpolarised pyruvate was observed to be higher in cells, containing overexpressed membrane monocarboxylate transporters (CCL39‐MCT+) than in wild‐type CCL39 cells.