PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2770705-4 1989 A reciprocal relation was found to exist between inhibitory constants of 5-N-substituted amiloride analogues for monoamine oxidase A and the ratio of overflows of endogenous noradrenaline and 3,4-dihydroxyphenylethylene glycol from the isolated rat tail artery incubated in the presence of a 50 microM concentration of the analogue, when the tissue was exposed to 10 microM tyramine. Tyramine 374-382 monoamine oxidase A Rattus norvegicus 113-132 2819332-11 1989 The metabolism of Tyr by homogenates of the rat mesenteric vascular bed was carried out by SSAO (60%) and MAO-A (40%) with very little contribution from MAO-B. Tyramine 18-21 monoamine oxidase A Rattus norvegicus 106-111 2819332-12 1989 Homogenates from rats pretreated with MDL 72145 showed metabolism of Tyr by MAO-A only. Tyramine 69-72 monoamine oxidase A Rattus norvegicus 76-81 2587673-3 1989 The present results in rats and the clinical trials provide evidence that moclobemide is an orally active MAO-A inhibitor which, due to its remarkably low tyramine potentiating pressor effects and to its lack of anticholinergic activity, has a very attractive pharmacological profile. Tyramine 155-163 monoamine oxidase A Rattus norvegicus 106-111 2570842-2 1989 Hordenine was deaminated by rat liver MAO with a Michaelis constant of 479 microM and maximum velocity of 128 nmol (mg protein)-1 h-1 compared with 144 microM and 482 nmol (mg protein)-1 h-1 for tyramine. Tyramine 195-203 monoamine oxidase A Rattus norvegicus 38-41 3171572-1 1988 The histochemical distribution of monoamine oxidase A and B in rat brain was investigated using a coupled peroxidatic technique with benzylamine and tyramine as substrates and clorgyline and (-)-deprenyl as selective inhibitors. Tyramine 149-157 monoamine oxidase A Rattus norvegicus 34-59 2907098-3 1988 When MAO activity was inhibited by pargyline (10 mumol/l), p-tyramine and p-octopamine had mixed excitatory-inhibitory effects on the twitches, while noradrenaline had mostly excitatory effects along the whole range of concentrations assayed (0.158-15.8 mumol/l). Tyramine 59-69 monoamine oxidase A Rattus norvegicus 5-8 3822124-6 1986 The kinetics of the oxidase are similar to those of monoamine oxidase type A reported in other tissues including the adrenergic neuron, having apparent Km values of 400, 280, 170 and 227 microM for noradrenaline, dopamine, serotonin and tyramine. Tyramine 237-245 monoamine oxidase A Rattus norvegicus 52-76 2886556-3 1987 MAO was assessed by measuring the specific binding of [3H]pargyline, an irreversible MAO inhibitor, and the rates of oxidation of known MAO substrates: benzylamine, tyramine, tryptamine, and 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Tyramine 165-173 monoamine oxidase A Rattus norvegicus 0-3 3444478-14 1987 A larger fraction of vesicular 3H-noradrenaline is accessible to equireleasing concentrations of (+)-amphetamine (an inhibitor of MAO) than of tyramine (a substrate of MAO). Tyramine 143-151 monoamine oxidase A Rattus norvegicus 168-171 3785579-7 1986 Oxidation of norepinephrine, serotonin, octopamine, tyramine and dopamine by monoamine oxidase (MAO), an enzyme marker of the outer mitochondrial membrane, was inhibited in the presence of 0.01 to 0.1 mM of chlorphentermine. Tyramine 52-60 monoamine oxidase A Rattus norvegicus 77-94 2430159-6 1986 In vitro studies in rat brainstem mitochondrial preparations show a dose-dependent, reversible, inhibition of MAO using tyramine as the substrate for the enzyme reaction. Tyramine 120-128 monoamine oxidase A Rattus norvegicus 110-113 3785579-7 1986 Oxidation of norepinephrine, serotonin, octopamine, tyramine and dopamine by monoamine oxidase (MAO), an enzyme marker of the outer mitochondrial membrane, was inhibited in the presence of 0.01 to 0.1 mM of chlorphentermine. Tyramine 52-60 monoamine oxidase A Rattus norvegicus 96-99 6741571-3 1984 The increase in MAO activity in the presence of human plasma can be explained by the observed decrease in the apparent Km for the amine (tyramine, PEA). Tyramine 137-145 monoamine oxidase A Rattus norvegicus 16-19 3083168-5 1986 This increase in the tyramine isomers is consistent with the ability of chlordimeform and its metabolite, demethylchlordimeform, to inhibit monoamine oxidase (MAO). Tyramine 21-29 monoamine oxidase A Rattus norvegicus 140-157 3083168-5 1986 This increase in the tyramine isomers is consistent with the ability of chlordimeform and its metabolite, demethylchlordimeform, to inhibit monoamine oxidase (MAO). Tyramine 21-29 monoamine oxidase A Rattus norvegicus 159-162 3023548-5 1986 MAO A and B were inhibited approximately equipotently and the material competitively inhibited tyramine oxidation by rat liver. Tyramine 95-103 monoamine oxidase A Rattus norvegicus 0-11 3839173-8 1985 Pargyline and tranylcypromine shifted the dose-response curves for tyramine and beta-phenylethylamine, but not serotonin, to the left, indicating inhibition of type B MAO. Tyramine 67-75 monoamine oxidase A Rattus norvegicus 167-170 3835805-1 1985 In experiments on male Wistar albino rats was studied the effect of Co, Cd, Ni, Zn, Hg and Pb on the activity of rat liver and brain monoamine oxidase (MAO) using tyramine, serotonin and beta-phenylethylamine as substrates. Tyramine 163-171 monoamine oxidase A Rattus norvegicus 152-155 3835805-2 1985 It was established that ZnSO4 significantly increased the activity of liver MAO with all substrates studied, Co(NO3)2 increased it when tyramine and serotonin were used while NiSO4 increased MAO activity when serotonin was used as a substrate. Tyramine 136-144 monoamine oxidase A Rattus norvegicus 76-79 6748816-3 1984 produces a slight but appreciable inhibition of MAO activity with tyramine or serotonin but not with benzylamine as substrate in both rat brain and liver mitochondria. Tyramine 66-74 monoamine oxidase A Rattus norvegicus 48-51 6748816-4 1984 Lignocaine (2-20 mM) inhibits (in vitro) both brain and liver mitochondrial MAO activity, using tyramine, serotonin and benzylamine as substrates, in a concentration-dependent manner. Tyramine 96-104 monoamine oxidase A Rattus norvegicus 76-79 6748816-5 1984 Furthermore, lignocaine produces a marked in vitro inhibition of serotonin and tyramine oxidation in MAO-A and not in MAO-B preparation of rat brain. Tyramine 79-87 monoamine oxidase A Rattus norvegicus 101-106 6748816-7 1984 Lineweaver-Burk plots show that lignocaine (2-10 mM) produces a significant increase in Km and decrease in Vmax of MAO for tyramine and serotonin in both brain and liver. Tyramine 123-131 monoamine oxidase A Rattus norvegicus 115-118 2872316-5 1986 The changes in Km and Vmax values at pH 7 and pH 9 indicated that the affinities of MAO-A towards 5-HT and tyramine slightly increased at pH 9 and those of MAO-B towards tyramine and benzylamine also increased at pH 9, while uncharged amines at pH 9 amounted to about a hundred times of those at pH 7. Tyramine 107-115 monoamine oxidase A Rattus norvegicus 84-89 2872316-5 1986 The changes in Km and Vmax values at pH 7 and pH 9 indicated that the affinities of MAO-A towards 5-HT and tyramine slightly increased at pH 9 and those of MAO-B towards tyramine and benzylamine also increased at pH 9, while uncharged amines at pH 9 amounted to about a hundred times of those at pH 7. Tyramine 170-178 monoamine oxidase A Rattus norvegicus 84-89 3953019-1 1986 Activity of monoamine oxidases (MAO) of the types A and B (substrates: 5-hydroxytryptamine, 2-phenylethylamine, tyramine) has been studied in mitochondrial fractions from brain, heart, liver and kidney of 24-week-old rats of the normotonic strain Wistar Kyoto (WKY) and spontaneously hypertonic rats (SHR). Tyramine 112-120 monoamine oxidase A Rattus norvegicus 12-30 3953019-1 1986 Activity of monoamine oxidases (MAO) of the types A and B (substrates: 5-hydroxytryptamine, 2-phenylethylamine, tyramine) has been studied in mitochondrial fractions from brain, heart, liver and kidney of 24-week-old rats of the normotonic strain Wistar Kyoto (WKY) and spontaneously hypertonic rats (SHR). Tyramine 112-120 monoamine oxidase A Rattus norvegicus 32-35 3953019-4 1986 However, in experiments with tyramine as a substrate of MAO the enzymatic activity in SHR brain mitochondria was increased 1.5-fold (P less than 0.05) as compared with the WKY rats. Tyramine 29-37 monoamine oxidase A Rattus norvegicus 56-59 3953019-5 1986 In kidney mitochondria of SHR the activity of MAO (substrates: 5-hydroxytryptamine, 2-phenylethylamine, tyramine) did not exhibit any alterations as compared with the control WKY rats. Tyramine 104-112 monoamine oxidase A Rattus norvegicus 46-49 3840523-8 1985 Such combinations had a greatly reduced propensity to augment the cardiovascular effects of intraduodenally administered tyramine, when compared with FMMT given alone or with clorgyline, a selective inhibitor of MAO type A. Tyramine 121-129 monoamine oxidase A Rattus norvegicus 212-215 4073474-2 1985 Results indicated an underestimation of MAO activity when liquid ion exchange chromatography (LIEC) was used instead of an ion exchange chromatographic method (IEC) to separate the different products of the deaminated tyramine, phenylethylamine, or serotonin. Tyramine 218-226 monoamine oxidase A Rattus norvegicus 40-43 6830619-0 1983 Intestinal metabolism of tyramine by both forms of monoamine oxidase in the rat. Tyramine 25-33 monoamine oxidase A Rattus norvegicus 51-68 6645113-7 1983 Km values for tyramine of heart MAO in WKY and SHR were approx. Tyramine 14-22 monoamine oxidase A Rattus norvegicus 32-35 6414536-5 1983 In intact mitochondria the intensity of inhibition by clorgyline of tyramine deamination in the presence of benzyl alcohol (competitive reversible MAO inhibitor) was increased, but the additive effect was not achieved. Tyramine 68-76 monoamine oxidase A Rattus norvegicus 147-150 6830619-1 1983 The two forms of monoamine oxidase (MAO) in rat intestine and brain homogenates were found to have different Km and Vmax values towards tyramine. Tyramine 136-144 monoamine oxidase A Rattus norvegicus 17-34 6830619-1 1983 The two forms of monoamine oxidase (MAO) in rat intestine and brain homogenates were found to have different Km and Vmax values towards tyramine. Tyramine 136-144 monoamine oxidase A Rattus norvegicus 36-39 6830619-3 1983 As a consequence, the ratio of activities (MAO-A: MAO-B) towards tyramine are dependent upon the substrate concentration. Tyramine 65-73 monoamine oxidase A Rattus norvegicus 43-48 6830619-4 1983 The MAO-A-selective inhibitors, toloxatone and cimoxatone, were found to be competitive inhibitors of the oxidation of tyramine by the A-form of this enzyme in the rat intestine, with Ki values of 3.4 microM and 3.7 nM respectively. Tyramine 119-127 monoamine oxidase A Rattus norvegicus 4-9 6830619-5 1983 The significance of these results in relation to the "cheese effect", a pressor response to tyramine after monoamine oxidase inhibition, are discussed. Tyramine 92-100 monoamine oxidase A Rattus norvegicus 107-124 6686709-0 1983 Levels of p-tyramine in rat brain after chronic administration of MAO-inhibiting antidepressants. Tyramine 10-20 monoamine oxidase A Rattus norvegicus 66-69 7080482-1 1982 Monoamine oxidase (MAO) activity (substrate: tyramine) has been studied in rat intestinal wall mitochondrial fractions identified by monitoring succinate dehydrogenase and cytochrome oxidase activities. Tyramine 45-53 monoamine oxidase A Rattus norvegicus 0-17 6127132-6 1982 5 Potentiation of tyramine responses by clorgyline and LY51641 occurred at 91% and 64% inhibition of MAO type A respectively, although full potentiation of the tyramine response was elicited only when substantial inhibition of both enzyme types occurred. Tyramine 18-26 monoamine oxidase A Rattus norvegicus 101-104 7080482-1 1982 Monoamine oxidase (MAO) activity (substrate: tyramine) has been studied in rat intestinal wall mitochondrial fractions identified by monitoring succinate dehydrogenase and cytochrome oxidase activities. Tyramine 45-53 monoamine oxidase A Rattus norvegicus 19-22 41907-1 1979 The specific actiivty of rat heart MAO, towards both tyramine and benzylamine as substrates, was found to increase with the age of the animal, and also after administration of (-)-thyroxine to young male rats. Tyramine 53-61 monoamine oxidase A Rattus norvegicus 35-38 6455104-1 1981 The MAO activity (tyramine substrate) was measured in 17 different brain regions, the spinal cord, and 13 different organs of four patients with Huntington"s disease and three patients with Parkinson"s disease. Tyramine 18-26 monoamine oxidase A Rattus norvegicus 4-7 6786369-0 1980 [Mechanism of inhibition by chlorgyline and deprenyl of tyramine deamination by mitochondrial monoamine oxidase of rat liver]. Tyramine 56-64 monoamine oxidase A Rattus norvegicus 94-111 6786369-1 1980 The inhibition by chlorgyline and deprenyl of deamination of tyramine, i. e. substrate of two forms of monoamine oxidase (MAO) A and B, by fragments of rat liver mitochondrial membrane and the effects of competitive reversible inhibitors of the MAO activity, e. g. 4-ethylpyridine, benzyl alcohol, O-benzyl-hydroxylamine and 2-oxyquinoline, on this process were studied. Tyramine 61-69 monoamine oxidase A Rattus norvegicus 103-134 6786369-1 1980 The inhibition by chlorgyline and deprenyl of deamination of tyramine, i. e. substrate of two forms of monoamine oxidase (MAO) A and B, by fragments of rat liver mitochondrial membrane and the effects of competitive reversible inhibitors of the MAO activity, e. g. 4-ethylpyridine, benzyl alcohol, O-benzyl-hydroxylamine and 2-oxyquinoline, on this process were studied. Tyramine 61-69 monoamine oxidase A Rattus norvegicus 122-125 6786369-3 1980 The stimulating effect is due to the independent action of two inhibitors on the two different sites of the MAO active center: chlorgyline--on the isoalloxazine ring of FAD, that of 4-ethylpyridine, benzyl alcohol, O-benzylhydroxylamine, 2-oxyquinoline, respectively, on the hydrophobic region involved in tyramine binding. Tyramine 306-314 monoamine oxidase A Rattus norvegicus 108-111 6786369-6 1980 The data obtained revealed the differences in the type and mechanism of action of chlorgyline and deprenyl on tyramine deamination and showed that these inhibitors act on different sites of the MAO active center, responsible for tyramine oxidation. Tyramine 110-118 monoamine oxidase A Rattus norvegicus 194-197 6786369-6 1980 The data obtained revealed the differences in the type and mechanism of action of chlorgyline and deprenyl on tyramine deamination and showed that these inhibitors act on different sites of the MAO active center, responsible for tyramine oxidation. Tyramine 229-237 monoamine oxidase A Rattus norvegicus 194-197 6797482-3 1981 After solubilization of MAO by methylethylketone 7% of mitochondrial activity passes into solution and the rate of deamination of serotonin, tyramine and beta-phenylethylamine by soluble MAO preparation is selectively decreased. Tyramine 141-149 monoamine oxidase A Rattus norvegicus 24-27 6797482-3 1981 After solubilization of MAO by methylethylketone 7% of mitochondrial activity passes into solution and the rate of deamination of serotonin, tyramine and beta-phenylethylamine by soluble MAO preparation is selectively decreased. Tyramine 141-149 monoamine oxidase A Rattus norvegicus 187-190 41907-4 1979 Clorgyline and deprenyl, used as inhibitors of rat heart MAO, indicated that tyramine is metabolized solely by MAO-A, whereas benzylamine is a substrate for both MAO-A and -B, and also a clorgyline- and deprenyl-resistant enzymic activity. Tyramine 77-85 monoamine oxidase A Rattus norvegicus 57-60 41907-4 1979 Clorgyline and deprenyl, used as inhibitors of rat heart MAO, indicated that tyramine is metabolized solely by MAO-A, whereas benzylamine is a substrate for both MAO-A and -B, and also a clorgyline- and deprenyl-resistant enzymic activity. Tyramine 77-85 monoamine oxidase A Rattus norvegicus 111-116 429200-1 1979 Monoamine oxidase (MAO) activity has been demonstrated histochemically in rat hypothalamic ependyma using the sulphate-tetrazolium and coupled peroxidatic techniques with tryptamine, tyramine, 5-hydroxytryptamine and benzylamine as substrates. Tyramine 183-191 monoamine oxidase A Rattus norvegicus 0-17 446597-0 1979 Effects of thyroidectomy on monoamine oxidase activities toward tyramine and serotonin in the circumventricular nuclei of the rat. Tyramine 64-72 monoamine oxidase A Rattus norvegicus 28-45 446597-1 1979 Following thyroidectomy, monoamine oxidase (MAO) activities toward tyramine decreased significantly by 20% in the nucleus periventricularis and the nucleus arcuatus among the 3 hypothalamic nuclei of the rat, while MAO activity toward serotonin decreased significantly by 10% only in the nucleus periventricularis. Tyramine 67-75 monoamine oxidase A Rattus norvegicus 25-42 446597-1 1979 Following thyroidectomy, monoamine oxidase (MAO) activities toward tyramine decreased significantly by 20% in the nucleus periventricularis and the nucleus arcuatus among the 3 hypothalamic nuclei of the rat, while MAO activity toward serotonin decreased significantly by 10% only in the nucleus periventricularis. Tyramine 67-75 monoamine oxidase A Rattus norvegicus 44-47 109783-4 1979 The inhibition of tyramine deamination by clorgyline and deprenyl yielded biphasic plots indicative of the presence of MAO-A and MAO-B enzyme forms in the vervet brain. Tyramine 18-26 monoamine oxidase A Rattus norvegicus 119-124 429200-1 1979 Monoamine oxidase (MAO) activity has been demonstrated histochemically in rat hypothalamic ependyma using the sulphate-tetrazolium and coupled peroxidatic techniques with tryptamine, tyramine, 5-hydroxytryptamine and benzylamine as substrates. Tyramine 183-191 monoamine oxidase A Rattus norvegicus 19-22 21126-2 1977 MAO activity in rat brain mitochondria with tyramine as substrate at 100% oxygen concentration was three times as much as that at 20%. Tyramine 44-52 monoamine oxidase A Rattus norvegicus 0-3 21126-5 1977 At 100% oxygen concentration, pargyline showed the most potent inhibition of MAO activity in liver mitochondria with tyramine as substrate, but inhibitions caused by pheniprazine and harmaline were not remarkable. Tyramine 117-125 monoamine oxidase A Rattus norvegicus 77-80 19894083-0 2010 limited potentiation of blood pressure in response to oral tyramine by the anti-Parkinson brain selective multifunctional monoamine oxidase-AB inhibitor, M30. Tyramine 59-67 monoamine oxidase A Rattus norvegicus 122-139 1080179-1 1975 The monoamine oxidase (MAO) activity in the ovariectomized rat uterus was significantly increased above control levels in animals given testosterone: 33% (P smaller than 0.01) with tryptamine or 34% (P smaller than 0.05) with tyramine as substrate. Tyramine 226-234 monoamine oxidase A Rattus norvegicus 4-21 1080179-1 1975 The monoamine oxidase (MAO) activity in the ovariectomized rat uterus was significantly increased above control levels in animals given testosterone: 33% (P smaller than 0.01) with tryptamine or 34% (P smaller than 0.05) with tyramine as substrate. Tyramine 226-234 monoamine oxidase A Rattus norvegicus 23-26 1080179-3 1975 Progesterone injection increased MAO activity toward tyramine by 20% but towards tryptamine by only 8%. Tyramine 53-61 monoamine oxidase A Rattus norvegicus 33-36 12389-3 1976 Enzymic properties of partially purified monoamine oxidase (MAO) from human placenta were studied with tyramine, serotonin and benzylamine as substrates. Tyramine 103-111 monoamine oxidase A Rattus norvegicus 60-63 938797-6 1976 3 MAO activity towards kynuramine, tyramine and dopamine increased after birth in all brain regions and also in the liver, to reach maximal values between days 40 and 80. Tyramine 35-43 monoamine oxidase A Rattus norvegicus 2-5 938797-19 1976 7 In the domestic pig there was a significant rise in the values in hippocampal MAO activity towards dopamine and tyramine from the foetus (55 day gestation) to the 1 week old piglet. Tyramine 114-122 monoamine oxidase A Rattus norvegicus 80-83 1262860-3 1976 When the activity of MAO was plotted as % of the highest specific activity towards tyramine, kynuramine oxidation remained fairly constant in fractions 10 to 30 but tyramine and dopamine showed separate peaks of activity in fractions 21 and 32 respectively. Tyramine 83-91 monoamine oxidase A Rattus norvegicus 21-24 1262860-3 1976 When the activity of MAO was plotted as % of the highest specific activity towards tyramine, kynuramine oxidation remained fairly constant in fractions 10 to 30 but tyramine and dopamine showed separate peaks of activity in fractions 21 and 32 respectively. Tyramine 165-173 monoamine oxidase A Rattus norvegicus 21-24 26574516-3 2016 The "cheese effect"-paroxysmal hypertension evoked by tyramine-containing foodstuffs-limits clinical use of irreversible MAO-A inhibitors. Tyramine 54-62 monoamine oxidase A Rattus norvegicus 121-126 19894083-1 2010 One of the limitations of non-selective monoamine oxidase (MAO) inhibitors as anti-depressant or anti-Parkinson drugs is their ability to potentiate the cardiovascular effect of oral tyramine, resulting from inhibition of systemic MAO-A and release of noradrenaline. Tyramine 183-191 monoamine oxidase A Rattus norvegicus 40-57 19894083-1 2010 One of the limitations of non-selective monoamine oxidase (MAO) inhibitors as anti-depressant or anti-Parkinson drugs is their ability to potentiate the cardiovascular effect of oral tyramine, resulting from inhibition of systemic MAO-A and release of noradrenaline. Tyramine 183-191 monoamine oxidase A Rattus norvegicus 59-62 19894083-1 2010 One of the limitations of non-selective monoamine oxidase (MAO) inhibitors as anti-depressant or anti-Parkinson drugs is their ability to potentiate the cardiovascular effect of oral tyramine, resulting from inhibition of systemic MAO-A and release of noradrenaline. Tyramine 183-191 monoamine oxidase A Rattus norvegicus 231-236 8313392-1 1993 Severe side effects such as hepatotoxicity and potentiation of the sympathomimetic action of tyramine ("the cheese effect") caused the withdrawal of nonselective irreversible monoamine oxidase (MAO) inhibitors from use in psychiatric therapy. Tyramine 93-101 monoamine oxidase A Rattus norvegicus 175-192 11389684-4 2001 Daily treatment of confluent cells with 0.75 mM tyramine (a substrate of MAO and SSAO) or benzylamine (a substrate of SSAO) over 1 week caused the acquisition of typical adipocyte morphology. Tyramine 48-56 monoamine oxidase A Rattus norvegicus 73-76 9413928-1 1998 The relationship between monoamine oxidase (EC 1.4.3.4; MAO) and peroxidase (EC 1.11.1.7; POD) in the metabolism of tyramine was investigated using the crude mitochondrial fraction of rat intestine. Tyramine 116-124 monoamine oxidase A Rattus norvegicus 56-59 9413928-4 1998 A similar value was found for the oxidative deamination of tyramine catalysed by intestinal MAO. Tyramine 59-67 monoamine oxidase A Rattus norvegicus 92-95 9413928-10 1998 These results indicate that the peroxidase-dependent metabolism of tyramine in the gut may be driven by H2O2 produced by MAO activities and that MAO-A is mainly responsible for this process, as well as for the oxidative deamination of tyramine. Tyramine 67-75 monoamine oxidase A Rattus norvegicus 121-124 9413928-10 1998 These results indicate that the peroxidase-dependent metabolism of tyramine in the gut may be driven by H2O2 produced by MAO activities and that MAO-A is mainly responsible for this process, as well as for the oxidative deamination of tyramine. Tyramine 67-75 monoamine oxidase A Rattus norvegicus 145-150 9413928-10 1998 These results indicate that the peroxidase-dependent metabolism of tyramine in the gut may be driven by H2O2 produced by MAO activities and that MAO-A is mainly responsible for this process, as well as for the oxidative deamination of tyramine. Tyramine 235-243 monoamine oxidase A Rattus norvegicus 145-150 8255365-1 1993 The behavior of inhibitors of monoamine oxidase-A (MAO-A) is considered in terms of the possibility of having an effective antidepressant that does not give rise to hypertensive interactions with dietary tyramine. Tyramine 204-212 monoamine oxidase A Rattus norvegicus 51-56 8255365-4 1993 Selective inhibition of MAO-A by clorgyline results in a large increase in the amount of unchanged tyramine transported, whereas selective inhibition of MAO-B with L-deprenyl (selegiline) has no significant effect. Tyramine 99-107 monoamine oxidase A Rattus norvegicus 24-29 8255365-5 1993 The behavior of reversible MAO-A inhibitors can significantly reduce, but not entirely eliminate, these effects on the intestinal metabolism of tyramine, but only if the inhibition is competitive in nature. Tyramine 144-152 monoamine oxidase A Rattus norvegicus 27-32 8365114-7 1993 In the inhibition studies with selective MAO-A and MAO-B inhibitors, clorgyline and deprenyl, deamination of 5-HT, Bz and Tyr in both tissues was induced by MAO-A alone, MAO-B alone and both forms of the enzyme, respectively, indicating the same substrate specificity as that in rats. Tyramine 122-125 monoamine oxidase A Rattus norvegicus 41-46 8365114-7 1993 In the inhibition studies with selective MAO-A and MAO-B inhibitors, clorgyline and deprenyl, deamination of 5-HT, Bz and Tyr in both tissues was induced by MAO-A alone, MAO-B alone and both forms of the enzyme, respectively, indicating the same substrate specificity as that in rats. Tyramine 122-125 monoamine oxidase A Rattus norvegicus 157-162 20799605-2 2010 The MAOs from both studied biological sources show catalytic properties resembling those of the classical MAO of terrestrial vertebrates: they deaminate tyramine, tryptamine, serotonin, benzylamine and do not deaminate histamine, have sensitivity to chlorgiline, the specific inhibitor of the MAO A form, and deprenyl, the specific inhibitor of the MAO B form, and are not inhibited with 10(-2) M semicarbazide. Tyramine 153-161 monoamine oxidase A Rattus norvegicus 4-7 20799605-2 2010 The MAOs from both studied biological sources show catalytic properties resembling those of the classical MAO of terrestrial vertebrates: they deaminate tyramine, tryptamine, serotonin, benzylamine and do not deaminate histamine, have sensitivity to chlorgiline, the specific inhibitor of the MAO A form, and deprenyl, the specific inhibitor of the MAO B form, and are not inhibited with 10(-2) M semicarbazide. Tyramine 153-161 monoamine oxidase A Rattus norvegicus 106-109 20799605-2 2010 The MAOs from both studied biological sources show catalytic properties resembling those of the classical MAO of terrestrial vertebrates: they deaminate tyramine, tryptamine, serotonin, benzylamine and do not deaminate histamine, have sensitivity to chlorgiline, the specific inhibitor of the MAO A form, and deprenyl, the specific inhibitor of the MAO B form, and are not inhibited with 10(-2) M semicarbazide. Tyramine 153-161 monoamine oxidase A Rattus norvegicus 106-109 19198157-2 2008 It has been established that MAO of mink, like MAO of rat, has properties of classic mammalian MAO: it deaminates tyramine, tryptamine, serotonin, benzilamine, beta-phenylethylamine and does not deaminate histamine as well as does not have sensitivity to semicarbazide. Tyramine 114-122 monoamine oxidase A Rattus norvegicus 29-32 19198157-2 2008 It has been established that MAO of mink, like MAO of rat, has properties of classic mammalian MAO: it deaminates tyramine, tryptamine, serotonin, benzilamine, beta-phenylethylamine and does not deaminate histamine as well as does not have sensitivity to semicarbazide. Tyramine 114-122 monoamine oxidase A Rattus norvegicus 47-50 19198157-2 2008 It has been established that MAO of mink, like MAO of rat, has properties of classic mammalian MAO: it deaminates tyramine, tryptamine, serotonin, benzilamine, beta-phenylethylamine and does not deaminate histamine as well as does not have sensitivity to semicarbazide. Tyramine 114-122 monoamine oxidase A Rattus norvegicus 47-50 17056035-3 2006 Interaction with monoamine oxidase (MAO) was investigated by measuring the ability to modulate [(14)C]tyramine oxidation and hydrogen peroxide production. Tyramine 102-110 monoamine oxidase A Rattus norvegicus 36-39 17056035-7 2006 Like classical MAO-inhibitors, they were unable to produce hydrogen peroxide and to activate glucose uptake but prevented tyramine to do so in rodent or human adipocytes. Tyramine 122-130 monoamine oxidase A Rattus norvegicus 15-18 15075350-3 2004 In the presence of their substrates, tyramine for MAO and benzylamine for SSAO, intracellular synthesis of H(2)O(2) took place with concomitant inhibition of LPS/IFN-gamma-induced NOS2 protein synthesis, as detected by Western blotting, flow cytometry, and immunofluorescence microscopy analyses. Tyramine 37-45 monoamine oxidase A Rattus norvegicus 50-53 14625153-1 2003 BACKGROUND: The oral administration of monoamine oxidase (MAO) inhibitors has the potential to cause a hypertensive reaction after the ingestion of tyramine-containing compounds. Tyramine 148-156 monoamine oxidase A Rattus norvegicus 39-56 14625153-1 2003 BACKGROUND: The oral administration of monoamine oxidase (MAO) inhibitors has the potential to cause a hypertensive reaction after the ingestion of tyramine-containing compounds. Tyramine 148-156 monoamine oxidase A Rattus norvegicus 58-61 15000454-12 2003 These results show that the improvement of glucose tolerance induced by prolonged tyramine administration occurs in an insulin-depleted model and probably results from peripheral insulin-like actions of the oxidation of MAO/SSAO substrates, such as the stimulation of glucose uptake into adipocytes. Tyramine 82-90 monoamine oxidase A Rattus norvegicus 220-223 12754108-4 2003 In LPS/IFN-gamma-treated cells, the MAO substrates dopamine (DA) and tyramine caused a concentration-dependent attenuation of NO(2)(-) and NO(3)(-). Tyramine 69-77 monoamine oxidase A Rattus norvegicus 36-39 12172644-1 2002 Incubation of rat liver mitochondria with 100-500 mM tyramine, a substrate for monoamine oxidases A and B (MAOs), in the presence of 30 mM Ca2+ induces matrix swelling, accompanied by collapse of membrane potential, efflux of endogenous Mg2+ and accumulated Ca2+ and oxidation of endogenous pyridine nucleotides. Tyramine 53-61 monoamine oxidase A Rattus norvegicus 79-105 12172644-6 2002 The MAO inhibitors clorgyline (50 mM) and pargyline (500 mM) completely protect against MPT induction by 100 mM tyramine but also inhibit the phenomenon, although with different efficacy, when it is induced by 100 mM Ca2+ in the absence of tyramine. Tyramine 112-120 monoamine oxidase A Rattus norvegicus 4-7 12172644-6 2002 The MAO inhibitors clorgyline (50 mM) and pargyline (500 mM) completely protect against MPT induction by 100 mM tyramine but also inhibit the phenomenon, although with different efficacy, when it is induced by 100 mM Ca2+ in the absence of tyramine. Tyramine 240-248 monoamine oxidase A Rattus norvegicus 4-7 11336106-4 2001 tyramine was potentiated by the MAO-A inhibitors clorgyline (0.1-1.0 mg/kg i.v.) Tyramine 0-8 monoamine oxidase A Rattus norvegicus 32-37 10582588-4 1999 In these experiments, incubation of rat brain mitochondria with tyramine (a mixed MAO-A/MAO-B substrate) for 15 min at 27 degrees C suppressed state 3 respiration by 32.8% and state 5 respiration by 40.1%. Tyramine 64-72 monoamine oxidase A Rattus norvegicus 82-87 10333983-14 1998 These results suggest that befloxatone is a potent reversible MAO-A inhibitor with antidepressant potential and a wide safety margin with regard to the potentiation of the pressor effect of tyramine. Tyramine 190-198 monoamine oxidase A Rattus norvegicus 62-67 9675034-5 1998 17beta-Estradiol treatment for 2 weeks significantly increased (P < 0.01) MAO activity in the hamster kidney (76.7 +/- 10.0 and 113.0 +/- 10.8% over controls for the substrates tyramine and kynuramine, respectively). Tyramine 180-188 monoamine oxidase A Rattus norvegicus 77-80 9258353-6 1997 This is in contrast to a large blood pressure rise in rats pretreated with phenelzine followed by tyramine, and in accord with the belief that an inhibitor selective for MAO A which is reversibly bound to the enzyme and therefore displaced by any ingested tyramine will not lead to the "cheese effect" (hypertension during treatment with MAO inhibitors usually caused by ingestion of foods containing tyramine). Tyramine 98-106 monoamine oxidase A Rattus norvegicus 170-175 9258353-6 1997 This is in contrast to a large blood pressure rise in rats pretreated with phenelzine followed by tyramine, and in accord with the belief that an inhibitor selective for MAO A which is reversibly bound to the enzyme and therefore displaced by any ingested tyramine will not lead to the "cheese effect" (hypertension during treatment with MAO inhibitors usually caused by ingestion of foods containing tyramine). Tyramine 98-106 monoamine oxidase A Rattus norvegicus 170-173 9258353-6 1997 This is in contrast to a large blood pressure rise in rats pretreated with phenelzine followed by tyramine, and in accord with the belief that an inhibitor selective for MAO A which is reversibly bound to the enzyme and therefore displaced by any ingested tyramine will not lead to the "cheese effect" (hypertension during treatment with MAO inhibitors usually caused by ingestion of foods containing tyramine). Tyramine 256-264 monoamine oxidase A Rattus norvegicus 170-175 9258353-6 1997 This is in contrast to a large blood pressure rise in rats pretreated with phenelzine followed by tyramine, and in accord with the belief that an inhibitor selective for MAO A which is reversibly bound to the enzyme and therefore displaced by any ingested tyramine will not lead to the "cheese effect" (hypertension during treatment with MAO inhibitors usually caused by ingestion of foods containing tyramine). Tyramine 256-264 monoamine oxidase A Rattus norvegicus 170-173 9258353-6 1997 This is in contrast to a large blood pressure rise in rats pretreated with phenelzine followed by tyramine, and in accord with the belief that an inhibitor selective for MAO A which is reversibly bound to the enzyme and therefore displaced by any ingested tyramine will not lead to the "cheese effect" (hypertension during treatment with MAO inhibitors usually caused by ingestion of foods containing tyramine). Tyramine 256-264 monoamine oxidase A Rattus norvegicus 170-175 9258353-6 1997 This is in contrast to a large blood pressure rise in rats pretreated with phenelzine followed by tyramine, and in accord with the belief that an inhibitor selective for MAO A which is reversibly bound to the enzyme and therefore displaced by any ingested tyramine will not lead to the "cheese effect" (hypertension during treatment with MAO inhibitors usually caused by ingestion of foods containing tyramine). Tyramine 256-264 monoamine oxidase A Rattus norvegicus 170-173 9025956-6 1997 Following preincubation of rat liver homogenates with selective monoamine oxidase (MAO)-A and -B inhibitors, kinetic constants were obtained for metabolism of the mixed substrate, p-tyramine. Tyramine 180-190 monoamine oxidase A Rattus norvegicus 64-96 8914926-0 1996 The metabolism of tyramine by monoamine oxidase A/B causes oxidative damage to mitochondrial DNA. Tyramine 18-26 monoamine oxidase A Rattus norvegicus 30-49 8914926-2 1996 In this study, we examined whether the H2O2 formed during the two-electron oxidation of tyramine [4-(2-aminoethyl)phenol] (a substrate for monoamine oxidases A/B) may contribute to the intramitochondrial steady-state concentration of H2O2 ([H2O2]ss) and, thus, be involved in the oxidative impairment of mitochondrial matrix components. Tyramine 88-96 monoamine oxidase A Rattus norvegicus 139-161 8914926-2 1996 In this study, we examined whether the H2O2 formed during the two-electron oxidation of tyramine [4-(2-aminoethyl)phenol] (a substrate for monoamine oxidases A/B) may contribute to the intramitochondrial steady-state concentration of H2O2 ([H2O2]ss) and, thus, be involved in the oxidative impairment of mitochondrial matrix components. Tyramine 98-120 monoamine oxidase A Rattus norvegicus 139-161 8532118-3 1995 Total MAO activity measured using tyramine, increased postnatally up to 24 weeks of age and attained a plateau afterward. Tyramine 34-42 monoamine oxidase A Rattus norvegicus 6-9 8313392-1 1993 Severe side effects such as hepatotoxicity and potentiation of the sympathomimetic action of tyramine ("the cheese effect") caused the withdrawal of nonselective irreversible monoamine oxidase (MAO) inhibitors from use in psychiatric therapy. Tyramine 93-101 monoamine oxidase A Rattus norvegicus 194-197 8313392-4 1993 Being reversibly bound to MAO, these drugs may be displaced from their binding site in the intestine by ingested, indirectly sympathomimetic amines such as tyramine, thus avoiding the initiation of the hypertensive crises. Tyramine 156-164 monoamine oxidase A Rattus norvegicus 26-29 1397011-0 1992 Displacement of in vivo binding of [3H]brofaromine to rat intestinal monoamine oxidase A by orally administered tyramine. Tyramine 112-120 monoamine oxidase A Rattus norvegicus 69-88 1397011-1 1992 The reversibility of the interaction of inhibitors with monoamine oxidase (MAO) is thought to provide a safety valve with respect to tyramine potentiation. Tyramine 133-141 monoamine oxidase A Rattus norvegicus 56-73 1397011-1 1992 The reversibility of the interaction of inhibitors with monoamine oxidase (MAO) is thought to provide a safety valve with respect to tyramine potentiation. Tyramine 133-141 monoamine oxidase A Rattus norvegicus 75-78 1397011-5 1992 It was also found that tyramine was relatively more effective in partially MAO-inhibited rats. Tyramine 23-31 monoamine oxidase A Rattus norvegicus 75-78 1905757-2 1991 By using tyramine as a substrate, the presence of MAO in these cells was demonstrated. Tyramine 9-17 monoamine oxidase A Rattus norvegicus 50-53 1356240-5 1992 +/- 7.5 pmol tritiated H2O/mg protein/min) and a higher Km of MAO (59 +/- 2.9 nM tyramine) than normal animals (46 +/- 1.7 nM tyramine). Tyramine 81-89 monoamine oxidase A Rattus norvegicus 62-65 2299343-0 1990 Monoamine oxidase (MAO)-A but not MAO-B inhibitors potentiate tyramine-induced catecholamine release from PC12 cells. Tyramine 62-70 monoamine oxidase A Rattus norvegicus 0-25 1817165-4 1991 Like the observations on adrenergic neurones, non-selective and selective MAO-A inhibitors potentiate the catecholamine-releasing property of tyramine in PC12 cells. Tyramine 142-150 monoamine oxidase A Rattus norvegicus 74-79 1817165-8 1991 In the final analysis the inter-relationship between MAO-A activity and the presence of tyramine-releasable pool of catecholamines in adrenergic neurons and PC12 cells may have a genetic basis and could be important in illuminating the differentiation of neural crest into adrenergic neurones and adrenal medulla on the one hand and chromaffin cells to PC12 cells on the other. Tyramine 88-96 monoamine oxidase A Rattus norvegicus 53-58 1884793-1 1991 In experiments on conscious normotensive male Wistar rats the new antidepressants, reversible MAO-A inhibitors, pyrazidole and incazane, as well as moclobemid increased the pressor effect of orally administered tyramine. Tyramine 211-219 monoamine oxidase A Rattus norvegicus 94-99 1884793-4 1991 The potentiation by the studied MAO-A inhibitors of the pressor effect of tyramine reflects the inhibition of the activity of MAO-A and the first-pass metabolism of tyramine in the gut and liver, as well as the inhibition of intraneuronal MAO activity in noradrenergic nerve endings and the potentiation of sympathetic activity. Tyramine 74-82 monoamine oxidase A Rattus norvegicus 32-37 1884793-4 1991 The potentiation by the studied MAO-A inhibitors of the pressor effect of tyramine reflects the inhibition of the activity of MAO-A and the first-pass metabolism of tyramine in the gut and liver, as well as the inhibition of intraneuronal MAO activity in noradrenergic nerve endings and the potentiation of sympathetic activity. Tyramine 74-82 monoamine oxidase A Rattus norvegicus 126-131 1884793-4 1991 The potentiation by the studied MAO-A inhibitors of the pressor effect of tyramine reflects the inhibition of the activity of MAO-A and the first-pass metabolism of tyramine in the gut and liver, as well as the inhibition of intraneuronal MAO activity in noradrenergic nerve endings and the potentiation of sympathetic activity. Tyramine 74-82 monoamine oxidase A Rattus norvegicus 32-35 1884793-4 1991 The potentiation by the studied MAO-A inhibitors of the pressor effect of tyramine reflects the inhibition of the activity of MAO-A and the first-pass metabolism of tyramine in the gut and liver, as well as the inhibition of intraneuronal MAO activity in noradrenergic nerve endings and the potentiation of sympathetic activity. Tyramine 165-173 monoamine oxidase A Rattus norvegicus 32-37 1884793-4 1991 The potentiation by the studied MAO-A inhibitors of the pressor effect of tyramine reflects the inhibition of the activity of MAO-A and the first-pass metabolism of tyramine in the gut and liver, as well as the inhibition of intraneuronal MAO activity in noradrenergic nerve endings and the potentiation of sympathetic activity. Tyramine 165-173 monoamine oxidase A Rattus norvegicus 32-35 2251787-2 1990 It was shown that in experimental catatonia (as compared with rats of the corresponding control group) there was a dramatic increase in the brain stem of the rate of oxidative deamination of beta-phenylethylamine catalyzed by MAO-III; there was also a statistically significant (albeit less expressed than in the experiments with beta-phenylethylamine) increase in the rate of deamination of tyramine and a decrease in the rate of deamination of serotonin. Tyramine 392-400 monoamine oxidase A Rattus norvegicus 226-229 2251787-3 1990 In the systems with MAO-II beta we detected statistically significant increase in the rates of deamination of tyramine and beta-phenylethylamine in experimental catatonia as compared with corresponding control. Tyramine 110-118 monoamine oxidase A Rattus norvegicus 20-23 2299343-2 1990 Selective monoamine oxidase (MAO)-A (clorgyline and moclobemide) and not MAO-B inhibitors (l-deprenyl, AGN 1135, and Ro 16-6491) potentiate the catecholamine-releasing action of tyramine significantly more than that of K+. Tyramine 178-186 monoamine oxidase A Rattus norvegicus 10-35 2299343-3 1990 The potentiation of tyramine-induced [3H]noradrenaline release from PC12 cells by MAO-A inhibitors has been linked to the presence of MAO-A in these cells, for which tyramine and noradrenaline are substrates. Tyramine 20-28 monoamine oxidase A Rattus norvegicus 82-87 2299343-3 1990 The potentiation of tyramine-induced [3H]noradrenaline release from PC12 cells by MAO-A inhibitors has been linked to the presence of MAO-A in these cells, for which tyramine and noradrenaline are substrates. Tyramine 20-28 monoamine oxidase A Rattus norvegicus 134-139 2299343-3 1990 The potentiation of tyramine-induced [3H]noradrenaline release from PC12 cells by MAO-A inhibitors has been linked to the presence of MAO-A in these cells, for which tyramine and noradrenaline are substrates. Tyramine 166-174 monoamine oxidase A Rattus norvegicus 82-87 2299343-3 1990 The potentiation of tyramine-induced [3H]noradrenaline release from PC12 cells by MAO-A inhibitors has been linked to the presence of MAO-A in these cells, for which tyramine and noradrenaline are substrates. Tyramine 166-174 monoamine oxidase A Rattus norvegicus 134-139 2127505-0 1990 The effect of various monoamine oxidase (MAO) inhibitors on the response of blood pressure of rats and cats to tyramine. Tyramine 111-119 monoamine oxidase A Rattus norvegicus 22-39 2248060-6 1990 This effect was almost completely eliminated by desipramine, suggesting that coadministration of a norepinephrine uptake inhibitor with a reversible MAO inhibitor is likely to reduce the risk of tyramine-induced hypertensive crisis. Tyramine 195-203 monoamine oxidase A Rattus norvegicus 149-152 2248079-5 1990 Interaction of MAO inhibitors and monoamine reuptake inhibitors with tyramine is discussed on the basis of experiments in conscious rats. Tyramine 69-77 monoamine oxidase A Rattus norvegicus 15-18 2127505-0 1990 The effect of various monoamine oxidase (MAO) inhibitors on the response of blood pressure of rats and cats to tyramine. Tyramine 111-119 monoamine oxidase A Rattus norvegicus 41-44 2127505-2 1990 It occurs mainly as a result of the interaction of MAO inhibitor with tyramine in foodstuffs. Tyramine 70-78 monoamine oxidase A Rattus norvegicus 51-54 2127505-3 1990 Anaesthetised rats and cats were used in order to investigate and compare the influence of the effect of tyramine by selective MAO type-B inhibitors with that produced by non-selective and A-selective MAO inhibitors on the one hand, and on the other hand, different MAO-B inhibitors with (-)deprenyl. Tyramine 105-113 monoamine oxidase A Rattus norvegicus 127-130 2127505-4 1990 (-)Deprenyl was the only one which inhibited the effect of tyramine in the experimental animals used, while other MAO inhibitors potentiated the tyramine effect. Tyramine 145-153 monoamine oxidase A Rattus norvegicus 114-117 35126867-7 2022 Tyramine and benzylamine activation of hexose uptake was vanadate-dependent and was also limited, while MAO was increased and SSAO decreased. Tyramine 0-8 monoamine oxidase A Rattus norvegicus 104-107