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Japanese Journal of Pharmacology
Vol 41 (No. 2) June 1986, 191-197
by Y. Arai; Y. Toyoshima; H. Kinemuchi

The alpha-methylated substrate-analogue monoamines, dl-alpha-methyltryptamine, dl-alpha-methylbenzylamine and two optical isomers of alpha-methylbenzylamine, were shown to be inhibitors of rat lung semicarbazide-sensitive amine oxidase (SSAO), with dl-alpha-methyltryptamine being the most potent and d-alpha-methylbenzylamine, the least. The three compounds, dl-alpha-methyltryptamine and the two isomers of alpha-methylbenzylamine also inhibited rat brain monoamine oxidase (MAO)-A and -B with a greater selectivity towards MAO-A. Preincubation of rat lung and brain homogenates with either of these compounds revealed that the inhibition of MAO and SSAO is reversible. The modes of inhibition of MAO-A and -B were competitive with the substrates tested. However, inhibition of SSAO by dl-alpha-methyltryptamine was found to be a mixed type (with a Ki value of 47 microM) and those by the racemic form and two isomers of alpha-methylbenzylamine were non-competitive (with Ki values of 90 microM for the racemic compound, 1070 microM for the d-isomer and 72 microM for the l-isomer). The present results indicate that SSAO can recognize optical isomers and that some alpha-methylated monoamines tested in the present study inhibit SSAO with properties different from those as MAO inhibitors.