Psychiatry related information on MAOA

• Failure to use adequate reaction times for the concentration of pargyline added can lead to gross underestimation of the quantity of MAO-A present [1].

High impact information on MAOA

• Analysis of MAOA expression in bovine placentae from natural reproduction revealed imprinted XCI with preferential inactivation of the paternal X chromosome [2].
• The mode of action of the various steroids on MAO A activity in endothelial cells seemed to be that of affecting the number of MAO molecules, as binding of [3H]pargyline, an MAO inhibitor, changed in proportion to changes in enzyme activity [3].
• The specificity of steroid action on MAO A activity was also supported by the fact that steroid-induced changes in total cell division ([14C]thymidine incorporation) and total protein synthesis ([14C]leucine incorporation) were seen after changes in MAO A [3].
• The new synthesized compounds 1-12 proved to be more reversible, potent, and selective inhibitors of MAO-A than of MAO-B [4].
• Quantitative structure-activity relationship (QSAR) analysis of dissociation constants shows that the binding of para-substituted benzylamine analogues to MAO A is best correlated with the van der Waals volume of the substituent, with larger substituents binding most tightly [5].

Biological context of MAOA

• Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase A [5].
• Each compound in the series inhibits both MAO A and MAO B competitively, and IC50 values for each compound were determined [6].

Anatomical context of MAOA

• The corresponding kinetic values for this substrate in the retina and the choroid showed higher affinity for MAO A (Km 271 and 197 microM, respectively) than for MAO B (Km 861 and 404 microM, respectively) [7].
• A new series of thirty derivatives of 2-(5-methoxy-1-methylindolyl)alkylamines has been synthesized and the compounds assayed as inhibitors of MAO-A and MAO-B from bovine brain mitochondria [8].
• Monoamine oxidase A mediates iodotyrosine formation induced by monoamines in bovine thyroid particulate fraction [9].

Associations of MAOA with chemical compounds

• The reaction rates and binding affinities of 17 para-substituted benzylamine analogues with purified MAO A were determined by steady state and stopped flow kinetic experiments [5].
• Kinetic considerations show that the rate of reaction of MAO-A with low concentrations of free pargyline will be very much slower than that of MAO-B [1].
• MAO-A activity, measured with 5-HT as substrate, was considerably greater than those of MAO-B and SSAO, determined with 2-phenylethylamine and benzylamine, respectively, in all the eye tissues [10].
• Thus, the decomposition of the specific MAO-A-substrates noradrenaline and adrenaline as well as of N-methyltyramine itself is inhibited [11].

Other interactions of MAOA

• The primary structure of bovine monoamine oxidase type A. Comparison with peptide sequences of bovine monoamine oxidase type B and other flavoenzymes [12].

References