Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “MONOAMINE OXIDASE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,063 records · Page 59Linked to original sources
PubMed2004

Metabolism of monoamines in invertebrates: the relative importance of monoamine oxidase in different phyla.

A review of the occurrence of monoamine oxidase activity in invertebrates is presented. In contrast to vertebrates, invertebrates use a variety of enzymatic routes to metabolise monoamines. These routes include N-acetylation, gamma-glutamyl conjugation, sugar conjugation, sulphation, beta-alanyl conjugation as well as oxidative deamination. Some of these enzymatic routes appear to be strictly catabolic whereas others result in metabolites used for structural and pigmentation purposes. The development of the various catabolic routes for monoamines in different groups of invertebrates may be dependent on the physical requirements of the diverse excretory organs used by these animals.

Animals↗
PubMed1994

Can our knowledge of monoamine oxidase (MAO) help in the design of better MAO inhibitors?

This paper presents a rapid overview of the mechanism by which monoamine oxidase (MAO) catalyzes the deamination of its substrates, and highlights the stereoselective nature of the active site of the enzyme. With the help of a few selected examples it is also discussed which structural factors are thought to have a preponderant influence on the affinity and selectivity of molecules towards the active site of either form of MAO. From the currently available data on the enzyme and its inhibition, it clearly appears that new MAO inhibitors, of whatever type, could be easily designed by structural modulation of molecules already found to have MAO inhibitory properties. As to whether better MAO inhibitors could be envisaged, it is suggested that MAO inhibition might be advantageously combined with other pharmacological properties for the treatment of pathological conditions, such as stroke and epilepsy, to the occurrence of which MAO activity might contribute. The rationale of this approach is presented.

Animals↗
PubMed1980

Monoamine oxidase and catechol-O-methyltransferase activities in cultured fibroblasts and blood cells from children with autism and the Gilles de la Tourette syndrome.

Monoamine oxidase (MAO) and catechol-O-methyltransferase (COMT) activities were measured in cells from children with autism (n = 5) and the Gilles de la Tourette syndrome (n = 5). Monoamine oxidase activities in cultured skin fibroblasts (type A) and platelets (type B) from the same individual were not correlated. COMT activities in fibroblasts and red blood cells showed a negative but not significant correlation (r = -0.42). Fibroblast MAO and COMT activities from patients were similar to values from controls matched for age, race, and sex. Increasing clinical severity of illness in both disorders, however, correlated significantly with higher fibroblast MAE activity. Cultured fibroblasts provide a means of measuring enzyme activities independently of the individual's current physiological and psychological state.

Adolescent↗
PubMed2001

Inhibition of type A monoamine oxidase by coptisine in mouse brain.

The inhibitory effects of coptisine, a protoberberine isoquinoline alkaloid, on type A and type B monoamine oxidase (MAO-A and MAO-B) activities in mouse brain were investigated. Coptisine showed an inhibitory effect on MAO-A activity in a concentration-dependent manner using a substrate kynuramine, but coptisine did not inhibit MAO-B activity. Coptisine exhibited 54.3% inhibition of MAO-A activity at 2 microM. The values of Km and Vmax of MAO-A were 151.9 +/- 0.6 microM and 0.40 +/- 0.03 nmol/min/mg protein, respectively (n=5). Coptisine competitively inhibited MAO-A activity with kynuramine. The Ki value of coptisine was 3.3 microM. The inhibition of MAO-A by coptisine was found to be reversible by dialysis of the incubation mixture. These results suggest that coptisine is a potent reversible inhibitor of MAO-A, and that coptisine functions to regulate the catecholamine content.

Animals↗
PubMed1984

Interaction of N-(2-nitro-4-azidophenyl)-serotonin with two types of monoamine oxidase in rat brain.

The effects of N-(2-nitro-4-azidophenyl) serotonin (NAP-5-HT) on types A and B monoamine oxidase (MAO) in rat brain cortex were studied. In the dark this compound acted as a competitive inhibitor for both types A and B MAO (Ki values of 0.19 microM and 0.21 microM for types A and B MAO, respectively). Upon photolysis, NAP-5-HT became an irreversible inhibitor for only type B MAO. A 50% inhibition was obtained by irradiation of the enzyme in the presence of 35 nM NAP-5-HT. Furthermore the inhibition of type B MAO could be protected by including its substrate phenylethylamine during the irradiation. Under the same photolytic conditions photodependent inhibition of type A MAO by NAP-5-HT was not clearly observed. These results provide further evidence that there is a fundamental difference in the active site of the two types of MAO in brain. NAP-5-HT may be a useful photoaffinity probe for characterizing the active site of type B MAO.

Affinity Labels↗
PubMed1991

[Determination of the monoamine oxidase and the diamine oxidase activity of a single blood sample].

The known methods for simultaneous measurements of blood histamine and serotonin have prompted the authors to search for approaches to simultaneous measurements of monoamine oxidase and diamine oxidase, the enzymes contributing to serotonin and histamine inactivation. The authors suggest a method for simultaneous measurements of the blood serum monoamine oxidase and diamine oxidase activities that permits cut down the time of the blood and substrate incubation to 10 min, essentially shortens the procedure and simplifies it. The method is recommended for research and practice.

Amine Oxidase (Copper-Containing)↗
PubMed1997

Monoamine oxidase inhibition causes a long-term prolongation of the dopamine-induced responses in rat midbrain dopaminergic cells.

The way monoamine oxidase (MAO) modulates the depression of the firing rate and the hyperpolarization of the membrane caused by dopamine (DA) on rat midbrain dopaminergic cells was investigated by means of intracellular recordings in vitro. The cellular responses to DA, attributable to the activation of somatodendritic D2/3 autoreceptors, were prolonged and did not completely wash out after pharmacological blockade of both types (A and B) of MAO. On the contrary, depression of the firing rate and membrane hyperpolarization induced by quinpirole (a direct D2 receptor agonist) were not affected by MAO inhibition. Furthermore, although the inhibition of DA reuptake by cocaine and nomifensine caused a short-term prolongation of DA responses, the combined inhibition of MAO A and B enzymes caused a long-term prolongation of DA effects. Moreover, the effects of DA were not largely prolonged during the simultaneous inhibition of MAO and the DA reuptake system. Interestingly, the actions of amphetamine were not clearly augmented by MAO inhibition. From the present data it is concluded that the termination of DA action in the brain is controlled mainly by MAO enzymes. This long-term prolongation of the dopaminergic responses suggests a substitutive therapeutic approach that uses MAO inhibitors and DA precursors in DA-deficient disorders in which continuous stimulation of the dopaminergic receptors is preferable.

Amphetamine↗
PubMed1988

4-(O-benzylphenoxy)-N-methylbutylamine (bifemelane) and other 4-(O-benzylphenoxy)-N-methylalkylamines as new inhibitors of type A and B monoamine oxidase.

4-(O-Benzylphenoxy)-N-methylbutylamine (Bifemelane, BP-N-methylbutylamine), a new psychotropic drug, was found to inhibit monoamine oxidase (MAO) in human brain synaptosomes. It inhibited type A MAO (MAO-A) competitively and type B (MAO-B) noncompetitively. BP-N-methylbutylamine had a much higher affinity to MAO-A than an amine substrate, kynuramine, and it was a more potent inhibitor of MAO-A than of MAO-B. The Ki values of MAO-A and -B were determined to be 4.20 and 46.0 microM, respectively, while the Km values of MAO-A and -B with kynuramine were 44.1 and 90.0 microM, respectively. The inhibition of MAO-A and -B by BP-N-methylbutylamine was found to be reversible by dialysis of the incubation mixture. MAO-A in human placental and liver mitochondria and in a rat clonal pheochromocytoma cell line, PC12h, was inhibited competitively by BP-N-methylbutylamine, while MAO-B in human liver mitochondria was inhibited noncompetitively, as in human brain synaptosomes. BP-N-methylbutylamine was not oxidized by MAO-A and -B. The effects of other BP-N-methylalkylamines, such as BP-N-methylethylamine, -propylamine, and -pentanylamine, on MAO activity were examined. BP-N-methylbutylamine was the most potent inhibitor of MAO-A, and BP-N-methylethylamine and -propylamine inhibited MAO-B competitively, whereas BP-N-methylbutylamine and -pentanylamine inhibited it noncompetitively. Inhibition of these BP-N-methylalkylamines on MAO-A and -B is discussed in relation to their chemical structure.

Adrenal Gland Neoplasms↗
PubMed1997

Striatal 6-[18F]fluorodopa accumulation after combined inhibition of peripheral catechol-O-methyltransferase and monoamine oxidase type B: differing response in relation to presynaptic dopaminergic dysfunction.

The aim was to investigate the effects of inhibition of monoamine oxidase type B (MAO-B) with selegiline alone and the combined inhibition of peripheral catechol-O-methyltransferase (COMT) with entacapone and MAO-B with selegiline on striatal 6-[18F]fluorodopa (FDOPA) accumulation, and whether the effect of entacapone + selegiline on FDOPA uptake differed depending on the severity of the presynaptic dopaminergic dysfunction. Thus, eight healthy controls, eight de novo patients with Parkinson's disease (PD), and 18 levodopa-treated PD patients were investigated with positron emission tomography (PET). Half of the subjects in each population belonged to the selegiline group and half to the entacapone + selegiline group. Both groups were studied twice with PET using FDOPA. After the first (baseline) FDOPA PET investigation, both groups were on 2 weeks of selegiline treatment, 10 mg daily. Thereafter, the second FDOPA PET was performed for all subjects with a premedication administered 60 min before the PET imaging; one group received 10 mg of selegiline, and the other group received a single 400 mg dose of entacapone coadministered with 10 mg of selegiline. Selegiline treatment alone had no significant influence on striatal FDOPA metabolism. The FDOPA accumulation, expressed as striatal-to-occipital ratios and modified decarboxylation coefficients (k3R0), increased significantly after entacapone + selegiline administration in all subject populations. The FDOPA uptake rate constant (Ki) remained virtually unchanged in controls and in de novo patients but decreased significantly in levodopa-treated PD patients after entacapone + selegiline intake. Entacapone + selegiline administration did not influence significantly the unidirectional blood-to-brain clearance for FDOPA (K1D) or the relative dopadecarboxylase activity (k3D). The changes in the studied parameters after entacapone + selegiline administration probably reflect the effects of entacapone, since entacapone alone has caused similar changes in previous PET studies. Response in FDOPA accumulation to entacapone + selegiline was higher in controls and de novo patients compared with levodopa-treated PD patients. The milder response in levodopa-treated patients might reflect the reduced ability of the degenerated dopaminergic neurons to utilize the prolonged FDOPA availability, produced by entacapone.

Adult↗
PubMed1979

Selectivity of clorgyline and pargyline as inhibitors of monoamine oxidases A and B in vivo in man.

During 4 weeks of treatment with clorgyline, a selective MAO-A inhibitor, platelet monoamine oxidase (MAO) activity was unchanged. During a similar 4-week crossover treatment period with pargyline, a selective MAO-B inhibitor, platelet MAO activity was essentially completely inhibited in the same individuals. The differential effects of the two drugs on platelet MAO, which consists exclusively of the MAO-B form, suggests that the in vitro selectivity of clorgyline, and possibly of pargyline, on MAO-A and MAO-B may be maintained in vivo during long-term administration in man. Reductions in blood pressure, heart rate, and plasma amine oxidase activity were generally similar in magnitude during treatment with both drugs, however, suggesting that either these effects are nonspecific consequences of both MAO-A and MAO-B inhibition, or that pargyline also inhibited MAO-A activity.

Blood Platelets↗
PubMed1975

Effect of acylation with eleostearic acids on the monoamine oxidase inhibitory potency of some hydrazine antidepressants in mice.

The effect of incorporation of an eleostearoyl group into molecules of aralkylhydrazines on their monoamine oxidase inhibitory potency was investigated in vitro and in vivo. The results showed that on a molar basis the hydrazides possessed an in vitro potency lower than and an in vivo potency and acute toxicity comparable to those of the corresponding aralkylhydrazines. The sequence of the relative potency of aralkylhydrazines and their hydrazides was similar. The overall pharmacological profile indicated that these aralkylhydrazines retained their monoamine oxidase inhibitory properties when the free hydrazine nitrogen was acylated with an eleostearoyl group.

Acylation↗
PubMedDate not supplied

[Selective inhibition of monoamine oxidase in bovine brain by befol and moclobemide].

Effects of befol and moklobemide on thyramine-, serotonin- and 2-phenyl ethylamine deaminase activities of mitochondrial monoamine oxidase from bovine truncus cerebri were studied. These drugs are reversible noncompetitive inhibitors of the enzyme not requiring preincubation. They inhibited most effectively the serotonin deaminase activity as compared with phenyl ethylamine deaminase activity, however they should not be concerned with typical inhibitors of monoamine oxidases of the A type as inhibition of thyramine deaminase activity was not found.

Animals↗
PubMed2004

The FAD binding sites of human monoamine oxidases A and B.

The structural details of the interactions of the covalent 8alpha-S-cysteinyl-FAD with the protein moiety in monoamine oxidase B (MAO B) based on the MAO B crystal structure are described. The dinucleotide is bound to the protein in an extended conformation with the majority of the bonds to the protein identified as hydrogen bonds with amino acid side chains, amide bonds, and water molecules. Since those amino acids interacting with the FAD are conserved in monoamine oxidase A (MAO A), it is proposed that the FAD binding site in MAO A is quite similar to that in MAO B. The redox-active isoalloxazine ring is buried in the protein without direct access to bulk solvent. An electrostatic interaction is observed between the anionic pyrophosphate moiety and Arg42. The normally flat oxidized flavin ring is in a bent, puckered conformation in the MAO B binding site which is suggested to contribute to its reactivity in catalysis. This structural information is then used to explain previous studies on flavin analog incorporation into either MAO B or into MAO A.

Animals↗
PubMed1984

On the substrate specificities of the two forms of monoamine oxidase.

By use of the selective irreversible inhibitors clorgyline and selegiline [(-)-deprenyl], it is possible to determine the Km and Vmax values of the two forms of monoamine oxidase towards a variety of substrates. The validity of this procedure is demonstrated for the deamination of dopamine by rat liver monoamine oxidase -A and -B, and the specificities of the two forms are analysed in terms of their kinetic parameters towards different substrates.

Animals↗
PubMed1965

CIRCADIAN RHYTHM IN PINEAL SEROTONIN: EFFECT OF MONOAMINE OXIDASE INHIBITION AND RESERPINE.

The pineal gland of the rat shows a circadian rhythm in its serotonin content, the amount of serotonin decreasing at night. This decrease can be prevented by inhibiting the action of monoamine oxidase. Reserpine abolishes the circadian rhythm in pineal serotonin in the same manner as does interruption of the sympathetic nervous connections of the central nervous system and the pineal gland. These observations suggest that circadian changes in release and binding of serotonin may occur in the pineal gland, and that a central mechanism in which monoamines participate may control the circadian pineal-serotonin rhythm.

Amines↗