Brain Oxidase Research Articles

Effect of polyphenol extract from Zanthoxylum bungeanum Maxim. on endocrine hormones and monoamine oxidase activity in a mouse model of climacteric depression

Purpose: To investigate the effects of polyphenol extract from Zanthoxylum bungeanum Maxim. (ZPPC) on endocrine hormones, monoamine oxidase activity and behavior in a mouse model of climacteric depression.Methods: Institute of Cancer Research (ICR) female albino mice (n = 50) weighing 24 – 26 g (mean wt = 25.0 ± 1.0 g) were randomly assigned to five groups of ten rats each: normal control group, negative control, and ZPPC (50 mg/kg), ZPPC (100 mg/kg) and ZPPC (200 mg/kg) groups. Depression was induced in the mice via oral administration of moclobemide at a dose of 20 mg/kg, and intraperitoneal injection of imipramine (20 mg/kg) 1 h and 30 min, before treatment. Tail suspension, forced swimming and voluntary activity tests were performed on the mice. The activity of monoamine oxidase (MAO) in mouse brain and the levels of endocrine hormones were also determined.Results: Treatment of depressed mice with ZPPC significantly and dose-dependently increased their tail suspension and immobility time (p < 0.05). The activity of monoamine oxidase in the brains of mice in the negative control group was significantly higher than that of normal control mice, but was significantly and dose-dependently reduced by ZPPC treatment (p < 0.05). Similarly, treatment of depressed mice with ZPPC significantly and dose-dependently reduced their serum adrenocorticotropin and corticosterone levels (p < 0.05).Conclusion: The results of this study indicate that ZPPC exerts antidepressant effect via suppression of brain MAO activity.
 Keywords: Climacteric depression, Endocrine hormones, Menopause, Monoamine oxidase, Polyphenols

Differences in Activity of Cytochrome C Oxidase in Brain Between Sleep and Wakefulness

Increased mRNA level of subunit 1 cytochrome c oxidase (COXI) during wakefulness and after short-term sleep deprivation has been described in brain. We hypothesized that this might contribute to increased activity of cytochrome oxidase (COX) enzyme during wakefulness, as part of the mechanisms to provide sufficient amounts of adenosine triphosphate to meet increased neuronal energy demands. COX activity was measured in isolated mitochondria from different brain regions in groups of rats with 3 hours of spontaneous sleep, 3 hours of spontaneous wake, and 3 hours of sleep deprivation. The group with 3 hours of spontaneous wake was added to delineate the circadian component of changes in the enzyme activity. Northern blot analysis was performed to examine the mRNA levels of 2 subunits of the enzyme COXI and COXIV, encoded by mitochondrial and nuclear DNA, respectively. Laboratory of Biochemistry, Department of Animal Biology, and Center for Sleep and Respiratory Neurobiology, University of Pennsylvania. 2-month-old male Fischer rats (N = 21) implanted for polygraphic recording. For COX activity, there was a main effect by analysis of variance of experimental group (P < .0001) with significant increases in COX activity in wake and sleep-deprived groups as compared to the sleep group. A main effect of brain region was also significant (P < .001). There was no difference between brain regions in the degree of increase in enzyme activity in wakefulness. Both COXI and COXIV mRNA were increased with wakefulness as compared to sleep. There is an increase in COX activity after both 3 hours of spontaneous wake and 3 hours of sleep deprivation as compared with 3 hours of spontaneous sleep in diverse brain regions, which could be, in part, explained by the increased levels of bigenomic transcripts of the enzyme. This likely contributes to increased adenosine triphosphate production during wakefulness. ADP, adenosine diphosphate; ATP, adenosine triphosphate; COXI, cytochrome c oxidase subunit 1 mRNA; COX, cytochrome c oxidase (protein); CREB, cyclic AMP response element binding protein; DNA, deoxyribonucleic acid; EDTA, ethylenediaminetetraacetic acid; EEG, electroencephalography; EMG, electromyography; GABP, GA binding protein; HEPES, 4-(2-hydroxyethyl)piperazine-1-ethanesulfonic acid; mRNA, messenger ribonucleic acid; NADH, nicotinamid adenine dinucleotide, reduced; NDII, NADH dehydrogenase subunit 2 mRNA; NRF, nuclear respiratory factor.

Monoamine Oxidase in Neuropsychiatry and Behavior

Monoamine oxidase (MAO) catalyzes the oxidative deamination of a number of biogenic amines, including the key neurotransmitters serotonin (5-HT), norepinephrine (NE), and dopamine (DA) and the neuromodulator phenylethylamine (PEA). Two forms of MAO, designated “MAO A” and “MAO B,” have been identified on the basis of biochemical properties and, subsequently, by cloning the relevant genes. Of the two, MAO A exhibits a higher affinity for 5-HT and NE and for the inhibitor clorgyline (Johnston 1968), whereas MAO B has a higher affinity for PEA, benzylamine, and the inhibitor deprenyl (Knoll and Magyar 1972).

Redox behavior of cytochrome oxidase in the rat brain measured by near-infrared spectroscopy.

Using near-infrared spectroscopy, we developed a new approach for measuring the redox state of cytochrome oxidase in the brain under normal blood-circulation conditions. Our algorithm does not require the absorption coefficient of cytochrome oxidase, which differs from study to study. We employed this method for evaluation of effects of changes in oxygen delivery on cerebral oxygenation in rats. When fractional inspired oxygen was decreased in a stepwise manner from 100 to <10%, at which point the concentration of oxygenated hemoglobin ([HbO2]) decreased by approximately 60%, cytochrome oxidase started to be reduced. Increases in arterial PO2 under hyperoxic conditions caused an increase in [HbO2], whereas further oxidation of cytochrome oxidase was not observed. The dissociation of the responses of hemogloblin and cytochrome oxidase was also clearly observed after the injection of epinephrine under severely hypoxic conditions; that is, cytochrome oxidase was reoxidized with increasing blood pressure, whereas hemoglobin oxygenation was not changed. These data indicated that oxygen-dependent redox changes in cytochrome oxidase occur only when oxygen delivery is extremely impaired. This is consistent with the in vitro data of our previous study.

Regional distribution of dopamine β-hydroxylase and monoamine oxidase in the brains of rats exposed to manganese

The regional distribution of dopamine β-hydroxylase (DBH) and monoamine oxidase (MAO) in rat brain was compared in control rats and rats given manganese in drinking-water (1 mg Mn/ml) for 30 days. In treated rats there was a significant accumulation of Mn in almost all regions of the brain except the hippocampus. Accumulation was highest in the hypothalamus, cortex and striatum. After Mn exposure, DBH activity was significantly decreased (in comparison with the controls) in the hypothalamus, striatum, mid-brain, cerebellum and cortex. A significant increase in MAO activity was found in the striatum, hypothalamus, mid-brain, hippocampus and medulla. The effects of Mn on these enzymes suggests the involvement of biogenic amines like dopamine, norepinephrine and serotonin during Mn toxicity. The effect of Mn is region specific and in certain regions the action of Mn on DBH differs from that on MAO. These different effects of Mn on DBH and MAO in different regions of the brain might explain the variable symptoms seen in Mn-induced neurotoxicity in humans.

4-chloro-3-hydroxyanthranilate inhibits brain 3-hydroxyanthranate oxidase

Quinolinic acid is synthesized from 3-hydroxyanthranilic acid via 3-hydroxyanthranilic acid oxidase. In liver, 4-chloro-3-hydroxyanthranilic acid inhibits 3-hydroxyanthranilic acid oxidase. To determine whether 4-chloro-3-hydroxyanthranilic acid also inhibits 3-hydroxyanthranilic acid oxidase in brain, 3-hydroxyanthranilic acid was injected into the cisterna magna of rats either with or without 4-chloro-3 hydroxyanthranilic acid. 3-Hydroxyanthranilic acid increased quinolinic acid concentrations throughout the brain. 4-Chloro-3-hydroxyanthranilic acid attenuated increases in brain quinolinic acid. These observations indicate that 4-chloro-3-hydroxyanthranilic acid inhibits 3-hydroxyanthranilic acid oxidase in brain. Quinolinic acid is a well established systemic metabolite of l-tryptophan which has been shown to be present in brain (Wolfensberger et al., 1983; Heyes and Markey, 1988a). QUIN has proved to be a convulsant (Lapin, 1982), neurotoxin (Schwarcz et al., 1983) and agonist of N-methyl-D-aspartate receptors (Perkins and Stone, 1983) when injected directly into the central nervous system of experimental animals. Therefore increased concentrations of QUIN in brain may have neoropathologic consequences. l-Tryptophan is converted to QUIN via the kynurenine pathway. The precursor of QUIN, 2-amino-3-carboxymuconic semialdehyde is synthesized from 3-hydroxyanthranilic acid (3-HAA) by the action of 3-hydroxyanthranilic acid oxidase (3-HAA/OX) in liver and brain (Foster et al., 1986; Okuno et al., 1987). QUIN is then formed from 2-amino-3-carboxymuconic semialdehyde by a spontaneous, non-enzymatic reaction. In liver, 3-HAA/OX is inhibited by 4-chloro-3-hydroxyantranilic acid (CL-HAA; Parli et al., 1980). In the present study, rats were given an intracisternal injection of 3-HAA and the resultant increases in regional brain QUIN concentrations quantified by gas chromatography/mass spectrometry (Heyes and Markey, 1988a,b). To determine whether CL-HAA inhibit 3-hydroxyanthranilic acid oxidase in brain, CL-HAA was co-administered with 3-HAA to see whether increases in QUIN were attenuated.

O-158 - Inhibition of monoamine oxidase in brain by various antidepressants

O-158 - Inhibition of monoamine oxidase in brain by various antidepressants

Influence of essential elements on manganese intoxication.

With a view to explore the influence of essential metals in manganese intoxication, the effect of calcium, iron or zinc supplementation on the uptake of manganese and on the activity of manganese sensitive enzymes, succinic dehydrogenase and cytochrome oxidase in brain and liver of rat was investigated. The choice of the two mitochondrial enzymes was based on the fact that the mitochondria are the chief site of manganese accumulation and their activity in brain, liver and blood of rats is significantly influenced by manganese.

Chronic effects of mercuric chloride on the activities of some enzymes in certain tissues of the fresh water murrel, [formula omitted][formula omitted

Alterations in the activities of some enzymes in the brain, gills, intestine, kidney, liver and muscles have been examined in the fresh water murrel, Channa punctatus , after exposure to a sublethal concentration of mercuric chloride (3 μg/1) for 15, 30 and 60 days. The results revealed that after 15 days of exposure amino acid oxidase activity was elevated in brain and liver and inhibited in intestine. The activity of xanthine oxidase was increased in gills, and inhibited in kidney. Thirty days exposure produced significant inhibition in the activities of malate dehydrogenase in liver, glutamate dehydrogenase in gills and brain, aminoacid oxidase in gills, and xanthine oxidase in liver and intestine. In contrast, glutamate dehydrogenase in intestine, kidney and liver and aminoacid oxidase in brain and liver were elevated. After 60 days of treatment, a decrease in the activity of glucose-6-phosphatase was recorded in gills, intestine, kidney and liver. Hexokinase activity in kidney and liver, and malate dehydrogenase in all the six tissues were inhibited. Glutamate dehydrogenase activity in intestine, kidney and liver remained higher than in control fish. In brain, kidney and liver the activity of aminoacid oxidase was elevated, but in gills the enzyme activity decreased. Xanthine oxidase activity was inhibited in intestine and liver.

Relative effects of hyperbaric oxygen on cations and catecholamine metabolism in rats: Protection by lithium against seizures

Analysis of lithium (Li +) in the brain and blood after intraperitoneal injection (i.p.) shows that initially its concentration is high in blood and negligible in the brain. Subsequently its concentration increases in the brain and disappears from the blood. Lithium itself affects neurological actions but the mechanisms remain obscure. It also modifies the toxic action of oxygen at high pressure (OHP), which causes convulsions, either suppressing or exacerbating it. These clearly separate effects correspond with the presence of Li + in the blood (suppression) or in the brain (exacerbating). Determination of the effect of Li + and OHP upon cations, catecholamines, ammonia, tyrosine hydroxylase, and monoamine oxidase in brain and blood tissue showed that there was very little correspondence between changes in the cations either with Li + or the toxic effects of OHP. On the other hand, OHP developed a sustained blood and brain hyperammonemia in rats which could be negatively modified by Li + in the blood. The latter effect also corresponded with a prolongation of convulsive latency. Changes in brain catecholamines, tyrosine hydroxylase, monoamine oxidase and tyrosine were effected by Li + and potentiated by OHP. These data suggest that Li + and OHP mediate their effects relatively more through developing hyperammoneic states in both blood and brain than by altering cation concentrations in these tissues.

Species differences in the deamination of dopamine and other substrates for monoamine oxidase in brain

Cortex and caudate specimens from human, non-human primate and rodent brains were examined for their ability to deaminate dopamine and for their sensitivity to irreversible monoamine oxidase (MAO) inhibitors. Using inhibition curves obtained with clorgyline, deprenyl and pargyline to estimate the relative proportions of MAO-A and MAO-B activity, dopamine was found to be deaminated predominantly by MAO-A in rat cortex and caudate. In contrast, dopamine was primarily an MAO-B substrate in human and vervet cortex and caudate. When clorgyline inhibition curves with tyramine or dopamine as substrate were compared in human, vervet and rat cortex, more pronounced species differences were found with dopamine than with tyramine. In all three species caudate tended to be more sensitive to inhibition by low concentrations of clorgyline than was cortex, suggesting a higher proportion of MAO-A activity in caudate. Similar species differences were also found when MAO-A activities were estimated using serotonin (5-HT): β-phenylethylamine (PEA) ratios (5-HT/5-HT + PEA). These ratios with selective substrates were highly correlated with clorgyline inhibition curves obtained with tyramine as substrate across 29 brain regions and tissues from different rodent and primate species (r=0.85, P<0.001). Data from both the substrate ratios and the clorgyline inhibition curves confirmed the relative predominance of MAO-B activity in primate brain regions (70–85%) as compared to rat brain regions (45%). Smaller species differences were observed in liver. Species differences in the proportion of brain MAO-A and B activities and in the deamination of dopamine and other substrates for MAO may have important implications in regard to the widespread use of rodent rather than primate models in the study of biogenic amine metabolism and of drugs affecting amine function.

Fatty acid abnormality in adrenoleukodystrophy.

Fatty acid abnormality in adrenoleukodystrophy.

ENZYMIC ACTIVITIES AND SODIUM, POTASSIUM AND COPPER CONCENTRATIONS IN MOUSE BRAIN AND LIVER AFTER CUPRIZONE TREATMENT IN VIVO

Abstract— The oral administration of cuprizone to mice induces status spongiosus in the CNS and giant mitochondria in the liver. The activities of monoamine oxidase and cytochrome oxidase in brain and liver are inhibited and succinate dehydrogenase activity is increased. There is an increase in sodium and decrease in potassium concentrations; brain dry weight and copper content are decreased. Animals treated with copper‐chelated cuprizone do not show any changes.

Partial separation and properties of mitochondrial monoamine oxidase in brain.

Journal Article Partial Separation and Properties of Mitochondrial Monoamine Oxidase in Brain Get access TOSHIHARU NAGATSU TOSHIHARU NAGATSU Department of Biochemistry, School of Dentistry, Aichi-Gakuin UniversityChikusa-ku, Nagoya Search for other works by this author on: Oxford Academic PubMed Google Scholar The Journal of Biochemistry, Volume 59, Issue 6, June 1966, Pages 606–612, https://doi.org/10.1093/oxfordjournals.jbchem.a128349 Published: 01 June 1966 Article history Received: 25 January 1966 Published: 01 June 1966

The uptake of labeled norepinephrine by isolated brain and other tissues of the cat

Summary Slices from brain and peripheral sympathetically innervated tissues of cats take up labeled norepinephrine to several times the concentration of this amine in the incubation media by a mechanism having the characteristics of active transport. The labeled norepinephrine remains in the cell in a site protected from metabolic degradation. Upon release from this site it is rapidly metabolized by monoamine oxidase in brain and o-methyl transferase in heart. Inhibition of metabolism by monoamine oxidase has no effect on uptake. Uptake is inhibited by reserpine and cardiac glycosides and may play a role in maintaining tissue stores of norepinephrine.

On the reported inhibition of monoamine oxidase by an agent with sedative properties.

1-Benzyl-2-methyl-5-methoxytryptamine has been reported, on the basis of indirect evidence, to inhibit monoamine oxidase. More direct experiments, however, demonstrate that the drug is devoid of the ability to block monoamine oxidase in brain in vitro or in vivo.

On the physiologic significance of monoamine oxidase in brain.

On the physiologic significance of monoamine oxidase in brain.

The distribution of serotonin, 5-hydroxytryptophan decarboxylase, and monoamine oxidase in brain.

The distribution of serotonin, 5-hydroxytryptophan decarboxylase, and monoamine oxidase in brain.

Pyruvate oxidase in brain

Research Article| December 01 1937 Pyruvate oxidase in brain: Co-carboxylase Rudolph Albert Peters Rudolph Albert Peters 1The Department of Biochemistry, Oxford Search for other works by this author on: This Site PubMed Google Scholar Biochem J (1937) 31 (12): 2240–2246. https://doi.org/10.1042/bj0312240 Views Icon Views Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Icon Share Facebook Twitter LinkedIn MailTo Cite Icon Cite Get Permissions Citation Rudolph Albert Peters; Pyruvate oxidase in brain: Co-carboxylase. Biochem J 1 December 1937; 31 (12): 2240–2246. doi: https://doi.org/10.1042/bj0312240 Download citation file: Ris (Zotero) Reference Manager EasyBib Bookends Mendeley Papers EndNote RefWorks BibTex toolbar search Search Dropdown Menu toolbar search search input Search input auto suggest filter your search All ContentAll JournalsBiochemical Journal Search Advanced Search This content is only available as a PDF. © 1937 CAMBRIDGE UNIVERSITY PRESS1937 Article PDF first page preview Close Modal You do not currently have access to this content.