13C magnetic resonance spectroscopy measurements with hyperpolarized [1-13C] pyruvate can be used to detect the expression of transgenic pyruvate decarboxylase activity in vivo.

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Title: 13C magnetic resonance spectroscopy measurements with hyperpolarized [1-13C] pyruvate can be used to detect the expression of transgenic pyruvate decarboxylase activity in vivo.
Authors: Dzien, Piotr1,2, Tee, Sui‐Seng1,2, Kettunen, Mikko I.1,2, Lyons, Scott K.1,2, Larkin, Timothy J.1, Timm, Kerstin N.1, Hu, De‐En1,2, Wright, Alan2, Rodrigues, Tiago B.1,2, Serrao, Eva M.1,2, Marco‐Rius, Irene1, Mannion, Elizabeth2, D'Santos, Paula2, Kennedy, Brett W. C.1, Brindle, Kevin M.1,2
Source: Magnetic Resonance in Medicine. Aug2016, Vol. 76 Issue 2, p391-401. 11p.
Abstract: Purpose Dissolution dynamic nuclear polarization can increase the sensitivity of the 13C magnetic resonance spectroscopy experiment by at least four orders of magnitude and offers a novel approach to the development of MRI gene reporters based on enzymes that metabolize 13C-labeled tracers. We describe here a gene reporter based on the enzyme pyruvate decarboxylase (EC 4.1.1.1), which catalyzes the decarboxylation of pyruvate to produce acetaldehyde and carbon dioxide. Methods Pyruvate decarboxylase from Zymomonas mobilis ( zmPDC) and a mutant that lacked enzyme activity were expressed using an inducible promoter in human embryonic kidney (HEK293T) cells. Enzyme activity was measured in the cells and in xenografts derived from the cells using 13C MRS measurements of the conversion of hyperpolarized [1-13C] pyruvate to H13 [ABSTRACT FROM AUTHOR]
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Database: Engineering Source
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Abstract:Purpose Dissolution dynamic nuclear polarization can increase the sensitivity of the 13C magnetic resonance spectroscopy experiment by at least four orders of magnitude and offers a novel approach to the development of MRI gene reporters based on enzymes that metabolize 13C-labeled tracers. We describe here a gene reporter based on the enzyme pyruvate decarboxylase (EC 4.1.1.1), which catalyzes the decarboxylation of pyruvate to produce acetaldehyde and carbon dioxide. Methods Pyruvate decarboxylase from Zymomonas mobilis ( zmPDC) and a mutant that lacked enzyme activity were expressed using an inducible promoter in human embryonic kidney (HEK293T) cells. Enzyme activity was measured in the cells and in xenografts derived from the cells using 13C MRS measurements of the conversion of hyperpolarized [1-13C] pyruvate to H13 [ABSTRACT FROM AUTHOR]
ISSN:07403194
DOI:10.1002/mrm.25879