Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.6.1.19 (GABA transaminase)
 808 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The formation and catabolism of aldehydes were compared in the hemispheres and brain stem of rats preferring ethanol (EP) or water (WP) and of those which were high tolerant (HT) and low tolerant to the hypnotic effect of ethanol. It was shown that aldehyde dehydrogenase was more active in the brain stem of HT-EP rats than that of HT-WR or LT-EP animals, whereas GABA aminotransferase is most active in the hemispheres and brain stem of LT-EP rats. The total activity of succinic semialdehyde reductase was equal in all the groups studied; however kinetic analysis suggest that the enzyme has a higher affinity for the substrate and coenzyme in the brain stem of HT-EP rats. Ethanol administered to HT-EP animals suppressed aldehyde dehydrogenase in the brain stem, unchanged GABA aminotransferase and activates succinic semialdehyde reductase in the two brain structures.
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PMID:[The activities of aldehyde dehydrogenase, GABA-aminotransferase and succinic semialdehyde reductase in the brain of rats with different preferences and tolerances for ethanol]. 130 80

The role of GABAergic neurons in the differential sensitivity to ethanol between the AT (Alcohol Tolerant) and ANT (Alcohol Nontolerant) rat lines developed for low and high degree of motor impairment from ethanol, was studied by comparing the effect of ethanol (2 or 4 g/kg, IP) on GABA turnover in different regions of the brain in these rat lines. GABA turnover was estimated from the accumulation of GABA after inhibition of GABA aminotransferase with aminooxyacetic acid (AOAA, 50 mg/kg, IP) given 10 min after administration of ethanol. The rats were killed two hours after the AOAA treatment with focused microwaves. The concentrations of GABA, aspartate, glutamate, glutamine and taurine were analyzed with HPLC. The saline-treated ANT rats were found to have a higher concentration of GABA in the striatum and a higher rate of GABA accumulation in the cerebellum than the AT rats. Ethanol suppressed the accumulation of GABA in both lines, but the suppression was significantly greater in the AT rats than in the ANT rats. In specific regions, this line difference was significant in the cerebral cortex and cerebellum with the higher ethanol dose. No line differences were found in the brain or tail blood ethanol concentration. AOAA increased the concentration of glutamine, decreased that of aspartate and glutamate, and did not modify that of taurine. The AOAA-induced changes in the concentrations of these amino acids were, however, minor relative to those found in the concentrations of GABA. The results that GABAergic mechanisms are involved in the differential sensitivity to the motor-impairing effects of ethanol between the AT and ANT rats.
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PMID:GABA turnover in the brain of rat lines developed for differential ethanol-induced motor impairment. 262 44

Ethanol in the presence of disulfiram (N,N,N',N'-tetraethylthiuram disulfide, an inhibitor of aldehyde dehydrogenase) inhibited liver beta-alanine-oxoglutarate aminotransferase (beta-AlaAT I) activity yet activated tyrosine aminotransferase (TAT) in weanling rats in vivo. The effect on beta-AlaAT I was followed by the inhibitory expression of beta-AlaAT I mRNA. The beta-AlaAT I activity was reduced with a pseudo-first-order profile with time, and the half-life was calculated to be 12.3 +/- 0.83 h with the rate constant (Kd) of 0.056 +/- 0.004 h-1. The synthesis of beta-AlaAT I in rat liver was estimated to be 1.56 x 10(-10) mol/g of wet tissue per hour at a steady state. A combination of ethanol and disulfiram also reduced beta-alanine-pyruvate aminotransferase (beta-AlaAT II) activity to 60% of the control after 24 h.
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PMID:Inhibitory effect of ethanol administration on beta-alanine-2-oxoglutarate aminotransferase (GABA aminotransferase) in disulfiram-pretreated rats. 959 Dec 43