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Magn Reson Med. 2009 Nov;62(5):1300-4. doi: 10.1002/mrm.22049.

Hyperpolarized (13)C magnetic resonance detection of carboxypeptidase G2 activity.

Author information

1
CRUK and EPSRC Cancer Imaging Centre, Institute of Cancer Research, Royal Marsden NHS Foundation Trust, Sutton, Surrey, UK.

Abstract

Carboxypeptidase G2 (CPG2) is a bacterial enzyme that is currently employed in a range of targeted cancer chemotherapy strategies such as gene-directed enzyme prodrug therapy (GDEPT). Employing dynamic nuclear polarization (DNP) and natural abundance (13)C magnetic resonance spectroscopy (MRS), we observed the CPG2-mediated conversion of a novel hyperpolarized reporter probe 3,5-difluorobenzoyl-L-glutamic acid (3,5-DFBGlu) to 3,5-difluorobenzoic acid (3,5-DFBA) and L-glutamic acid (L-Glu) in vitro. Isotopic labeling of the relevant nuclei with (13)C in 3,5-DFBGlu or related substrates will yield a further factor of 100 increase in the signal-to-noise. We discuss the feasibility of translating these experiments to generate metabolic images of CPG2 activity in vivo.

PMID:
19780183
DOI:
10.1002/mrm.22049
[Indexed for MEDLINE]
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