Effects of Two Substituted Hydrazine Monoamine Oxidase (MAO) Inhibitors on Neurotransmitter Amines, γ-Aminobutyric Acid, and Alanine in Rat Brain

1993 ◽  
Vol 82 (9) ◽  
pp. 934-937 ◽  
Author(s):  
Naoto Yamada ◽  
Saburo Takahashi ◽  
Kathryn G. Todd ◽  
Glen B. Baker ◽  
Paul R. Paetsch
Keyword(s):  
Monoamine Oxidase ◽  
Rat Brain ◽  
Aminobutyric Acid ◽  
Mao Inhibitors

scholarly journals Hydrogen Peroxide Production by Monoamine Oxidase during Ischemia-Reperfusion in the Rat Brain

1993 ◽  
Vol 13 (1) ◽  
pp. 125-134 ◽  
Author(s):  
Steven G. Simonson ◽  
Jing Zhang ◽  
Andrew T. Canada ◽  
Ying-Fu Su ◽  
Helene Benveniste ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Monoamine Oxidase ◽  
Rat Brain ◽  
Ischemia Reperfusion ◽  
Mao Inhibitors ◽  
Hydrogen Peroxide Production ◽  
Threefold Increase ◽  
Brain Reperfusion ◽  
Improvement In Survival

Monoamine oxidase (MAO) as a source of hydrogen peroxide (H2O2) was evaluated during ischemiareperfusion in vivo in the rat brain. H2O2 production was assessed with and without inhibition of MAO during and after 15 min of ischemia. Metabolism of H2O2 by catalase during ischemia and reperfusion was measured in forebrain homogenates using aminotriazole (ATZ), an irreversible H2O2-dependent inhibitor of catalase. Catecholamine and glutathione concentrations in forebrain were measured with and without MAO inhibitors. During ischemia, forebrain blood flow was reduced to 8% of baseline and H2O2 production decreased as measured at the microperoxisome. During reperfusion, a rapid increase in H2O2 generation occurred within 5 min as measured by a threefold increase in oxidized glutathione (GSSG). The H2O2-dependent rates of ATZ inactivation of catalase between control and ischemia–reperfusion were similar, indicating that H2O2 was more available to glutathione peroxidase than to catalase in this model. MAO inhibitors eliminated the biochemical indications of increased H2O2 production and increased the catecholamine concentrations. Mortality was 67% at 48 h after ischemiareperfusion, and there was no improvement in survival after inhibition of MAO. We conclude that MAO is an important source of H2O2 generation early in brain reperfusion, but inhibition of the enzyme does not improve survival in this model despite ablating H2O2 production.

Inhibition of Rat Brain Monoamine Oxidase Activities by Psoralen and Isopsoralen: Implications for the Treatment of Affective Disorders

2001 ◽  
Vol 88 (2) ◽  
pp. 75-80 ◽  
Author(s):  
Ling Dong Kong ◽  
Ren Xiang Tan ◽  
Anthony Yiu Ho Woo ◽  
Christopher Hon Ki Cheng2Note
Keyword(s):  
Monoamine Oxidase ◽  
Rat Brain ◽  
Affective Disorders ◽  
Brain Monoamine

Development of Monoamine Oxidase and Aldehyde Dehydrogenase in Reaggregating Cultures of Fetal Rat Brain Cells

1989 ◽  
Vol 16 (3) ◽  
pp. 281-286
Author(s):  
Olof Tottmar ◽  
Maria Söderbäck ◽  
Anders Aspberg
Keyword(s):  
Monoamine Oxidase ◽  
Rat Brain ◽  
Aldehyde Dehydrogenase ◽  
Brain Cells ◽  
Mao B ◽  
Adult Rat ◽  
Fetal Rat ◽  
Adult Rat Brain ◽  
Mao A ◽  
Fetal Rat Brain

The development of monoamine oxidase (MAO) and aldehyde dehydrogenase (ALDH) in reaggregation cultures of fetal rat brain cells was compared with that of enzymatic markers for glial and neuronal cells. Only MAO-A was detected in the cultures during the first week, but, during the following three weeks, the activity of MAO-B increased more rapidly than that of MAO-A. The ratio MAO-A/MAO-B in four-week aggregates was close to that found in the adult rat brain. The activity of ALDH started to increase rapidly after 15 days, and the developmental pattern was intermediate to those of the glial and neuronal markers. The activity after four weeks was close to that found in the adult rat brain. Epidermal growth factor (EGF) caused a slight decrease in the activities of the low-Km ALDH (after four weeks) and the neuronal marker, choline acetyltransferase (after two weeks), whereas the other markers were not affected. By contrast, the activities of MAO-A and MAO-B were greatly increased during almost the entire culture period. It is suggested that this effect of EGF was the result of increased mitotic activity and/or biochemical differentiation of other cell types present in the cell aggregates, e.g. capillary endothelial cells.

m-Sulfonate Benzene Diazonium Chloride: A Powerful Affinity Label for the ?-Aminobutyric Acid Binding Site from Rat Brain

1992 ◽  
Vol 59 (4) ◽  
pp. 1405-1413 ◽  
Author(s):  
Marie-Jeanne Bouchet ◽  
Patrice Jacques ◽  
Brigitte Ilien ◽  
Maurice Goeldner ◽  
Christian Hirth
Keyword(s):  
Binding Site ◽  
Rat Brain ◽  
Aminobutyric Acid ◽  
Affinity Label ◽  
Benzene Diazonium

Localization in rat brain of binding sites for parkinsonian toxin MPTP: similarities with [3H]parygyline binding to monoamine oxidase

1985 ◽  
Vol 330 (2) ◽  
pp. 337-342 ◽  
Author(s):  
Thomas C. Rainbow ◽  
Bruce Parsons ◽  
Caroline M. Wieczorek ◽  
Scott Manaker
Keyword(s):  
Monoamine Oxidase ◽  
Rat Brain ◽  
Binding Sites

The effect of γ-aminobutyric acid on 3H-flunitrazepam binding in rat brain

1978 ◽  
Vol 50 (4) ◽  
pp. 445-447 ◽  
Author(s):  
G.J. Wastek ◽  
R.C. Speth ◽  
T.D. Reisine ◽  
H.I. Yamamura
Keyword(s):  
Rat Brain ◽  
Aminobutyric Acid
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