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Chemical Compound Review

Lopac-R-107     N-(2-aminoethyl)-5-(3- fluorophenyl)-1,3...

Synonyms: SureCN6866198, ANW-71398, CCG-205189, Lopac0_001113, AC1L1JKU, ...
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High impact information on Lopac-R-107

  • Here we describe how reversible and selective inhibitors of MAO-A and MAO-B [Ro 41-1049 and Ro 19-6327 (lazabemide), respectively] can be used, as tritiated radioligands, to map the distribution and abundance of the enzymes in microscopic regions of the rat CNS and peripheral organs, and human brain by quantitative enzyme radioautography [1].
  • These mutants also showed a distinct shift in sensitivity for the MAO A- and B-selective inhibitors Ro 41-1049 and Ro 16-6491 [2].
  • The existence of a Ro 41-1049 adduct reversibly bound to the enzyme active site might explain the inhibition mechanism of this compound [3].
  • The structurally diverse MAO inhibitors Ro 16-6491 (selective for MAO-B) and Ro 41-1049 (selective for MAO-A), as well as the other psychotropic drugs (desipramine, cocaine, reserpine and haloperidol) displaced the binding of [3H]-idazoxan to NAIBS monophasically and with very low potencies.(ABSTRACT TRUNCATED AT 250 WORDS)[4]
  • Our results showed that cell incubation with tyramine (50 micromol/l) led to a time-dependent H2O2 generation which was fully inhibited by MAO A (clorgyline and RO 41-1049) and MAO B (selegiline and RO 19-6327) inhibitors [5].

Biological context of Lopac-R-107


Anatomical context of Lopac-R-107

  • In these studies a clear inhibition of DOPAC formation was observed with Ro 41-1049 (250 nM), while 250 nM lazabemide was found not to increase the accumulation of newly-formed DA in those tubular epithelial cells loaded with 50 microM L-DOPA [6].

Associations of Lopac-R-107 with other chemical compounds


Gene context of Lopac-R-107

  • The binding of 18F-fluoroclorgyline in the rat brain correlated with the distribution of MAO-A and was inhibited by preadministration of MAO-A inhibitors, clorgyline, and Ro 41-1049, whereas (R)-deprenyl, a MAO-B blocker, had no inhibitory effect [10].


  1. Quantitative enzyme radioautography with 3H-Ro 41-1049 and 3H-Ro 19-6327 in vitro: localization and abundance of MAO-A and MAO-B in rat CNS, peripheral organs, and human brain. Saura, J., Kettler, R., Da Prada, M., Richards, J.G. J. Neurosci. (1992) [Pubmed]
  2. Substrate and inhibitor specificities for human monoamine oxidase A and B are influenced by a single amino acid. Geha, R.M., Rebrin, I., Chen, K., Shih, J.C. J. Biol. Chem. (2001) [Pubmed]
  3. Characterization of the binding of [3H]Ro 41-1049 to the active site of human monoamine oxidase-A. Cesura, A.M., Bös, M., Galva, M.D., Imhof, R., Da Prada, M. Mol. Pharmacol. (1990) [Pubmed]
  4. Chronic treatment with the monoamine oxidase inhibitors clorgyline and pargyline down-regulates non-adrenoceptor [3H]-idazoxan binding sites in the rat brain. Olmos, G., Gabilondo, A.M., Miralles, A., Escriba, P.V., García-Sevilla, J.A. Br. J. Pharmacol. (1993) [Pubmed]
  5. Reactive oxygen species production by monoamine oxidases in intact cells. Pizzinat, N., Copin, N., Vindis, C., Parini, A., Cambon, C. Naunyn Schmiedebergs Arch. Pharmacol. (1999) [Pubmed]
  6. The activity of MAO A and B in rat renal cells and tubules. Guimarães, J.T., Soares-da-Silva, P. Life Sci. (1998) [Pubmed]
  7. Monoamine oxidase A inhibition by fluoxetine: an in vitro and in vivo study. Mukherjee, J., Yang, Z.Y. Synapse (1999) [Pubmed]
  8. Effect of monoamine oxidase A and B and of catechol-O-methyltransferase inhibition on L-DOPA-induced circling behavior. Heeringa, M.J., d'Agostini, F., DeBoer, P., DaPrada, M., Damsma, G. Journal of neural transmission (Vienna, Austria : 1996) (1997) [Pubmed]
  9. Unusual pattern of beta-phenylethylamine deamination in the rat heart. Tiago Guimarães, J., Soares-da-Silva, P. Neurobiology (Budapest, Hungary) (2000) [Pubmed]
  10. Development of N-[3-(2',4'-dichlorophenoxy)-2-18F-fluoropropyl]-N-methylpropargylamine (18F-fluoroclorgyline) as a potential PET radiotracer for monoamine oxidase-A. Mukherjee, J., Yang, Z.Y. Nucl. Med. Biol. (1999) [Pubmed]
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