Molecular basis for differential glycine transporters sensitivity to sanguinarine.

Frantisek Jursky, Martina Baliova, Andrea Mihalikova

Laboratory of Neurobiology, Institute of Molecular Biology, Slovak Academy of Sciences, Dubravska cesta 21, 842 51 Bratislava, Slovakia. Frantisek.Jursky@savba.sk

Toxicology letters 2012 Aug 3

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We previously demonstrated that glycine transporters GlyT1 and GlyT2 are differentially affected by toxic benzophenanthridine alkaloids. Using a combination of homology modeling, knowledge of the sensitivity of sanguinarine to sulfhydryl reagents and site directed mutagenesis we show here that the increased sensitivity of human GlyT1c to sanguinarine is abolished by the mutation of only cysteine 475. Inhibition requires the membrane permeable alkaloid alkanolamine, which is consistent with the intracellular location of the targeted cysteine. Copyright © 2012 Elsevier Ireland Ltd. All rights reserved.

Citation

Frantisek Jursky, Martina Baliova, Andrea Mihalikova. Molecular basis for differential glycine transporters sensitivity to sanguinarine. Toxicology letters. 2012 Aug 3;212(3):262-7