Literature DB >> 20532643

A novel in vitro assay to assess phosphorylation of 3'-[(18)F]fluoro-3'-deoxythymidine.

Ning Guo1, Jingping Xie, H Charles Manning, Natasha G Deane, M Sib Ansari, Robert J Coffey, John Gore, Ronald R Price, Ronald M Baldwin, J Oliver McIntyre.   

Abstract

PURPOSE: 3'-[(18)F]fluoro-3'-deoxythymidine ([(18)F]FLT) is phosphorylated by thymidine kinase 1 (TK-1), a cell cycle regulated enzyme. Appropriate use of [(18)F]FLT tracer requires validation of the TK-1 activity. Here, we report development of a novel phosphoryl-transfer assay to assess phosphorylation of [(18)F]FLT both in tumor cell lysates and tumor cells. PROCEDURES: The intrinsic F-18 radioactivity was used to quantify both substrate and phosphorylated products using a rapid thin layer chromatography method. Phosphorylation kinetics of [(18)F]FLT in SW480 and DiFi tumor cell lysates and cellular uptake were measured.
RESULTS: The apparent Michaelis-Menten kinetic parameters for [(18)F]FLT are K(m) = 4.8 ± 0.3 μM and V(max) = 7.4 pmol min(-1) per 1 × 10(6) cells with ~2-fold higher TK-1 activity in DiFi versus SW480 lysates.
CONCLUSIONS: The apparent K (m) of [(18)F]FLT was comparable to the value reported with purified recombinant TK-1. The uptake of [(18)F]FLT by SW480 cells is inhibited by nitrobenzylthioinosine or dipyridamole indicating that uptake is mediated predominantly by the equilibrative nucleoside transporters in these tumor cells.

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Year:  2011        PMID: 20532643      PMCID: PMC4180216          DOI: 10.1007/s11307-010-0351-8

Source DB:  PubMed          Journal:  Mol Imaging Biol        ISSN: 1536-1632            Impact factor:   3.488


  38 in total

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