Noninvasive detection of carboxypeptidase G2 activity in vivo
Noninvasive detection of carboxypeptidase G2 activity in vivo
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DOI:
10.1002/nbm.1597
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发表时间:
2011-05-01
影响因子:
2.9
通讯作者:
Payne, Geoffrey S.
中科院分区:
文献类型:
--
作者:
Jamin, Yann;Smyth, Lynette;Payne, Geoffrey S.
The pseudomonad protein, carboxypeptidase G2 (CPG2), is a prodrug-activating enzyme utilized in the targeted chemotherapy strategies of antibody-and gene-directed enzyme prodrug therapy (ADEPT and GDEPT). We have developed a noninvasive imaging approach to monitor CPG2 activity in vivo that will facilitate the preclinical and clinical development of CPG2-based ADEPT and GDEPT strategies. Cleavage of the novel reporter probe, 3,5-difluorobenzoyl-L-glutamic acid (3,5-DFBGlu), by CPG2, in human colon adenocarcinoma WiDr xenografts engineered to stably express CPG2, was monitored using F-19 MRSI. The high signal-to-noise ratio afforded by the two MR-equivalent F-19 nuclei of 3,5-DFBGlu, and the 1.4 ppm F-19 chemical shift difference on CPG2-mediated cleavage, enabled the dynamics and quantification of the apparent pharmacokinetics of 3,5-DFBGlu and its CPG2-mediated cleavage in the tumor to be evaluated. In addition, the apparent rate of increase of 3,5-difluorobenzoic acid concentration could also provide a biomarker of CPG2 activity levels in tumors of patients undergoing CPG2-based therapies, as well as a biomarker of treatment response. The addition of in vivo reporter probes, such as 3,5-DFBGlu, to the armamentarium of prodrugs cleaved by CPG2 affords new applications for CPG2 as a gene reporter of transgene expression. Copyright (C) 2010 John Wiley & Sons, Ltd.