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PubMed1993

[Effect of preliminary administration of phenobarbital on the toxicity of GABA-lytics in mice].

The toxicity of picrotoxin bicuculline, but not of 3-mercaptopropionic acid decreased in mice pretreated during three days with phenobarbital and benzonal. The antidotal effectiveness of diazepam by picrotoxin and bicuculline exposure increased significantly. It has been suggested, that the modulation of detoxication systems may be the cause of increased tolerance against GABA-antagonists.

3-Mercaptopropionic Acid↗
PubMed1975

Brain carbonic acid acidosis after acetazolamide.

In cats in barbiturate anesthesia extracellular pH and potassium were continously recorded from brian cortex by implanted microelectrodes. Implantation of the electrodes preserved the low permeability of the blood-brain-barrier to HCO3-minus and H+ions as indicated by the development of brain acidosis by I.V. injection of HCO3-minus. Acetazolamide (25 mg/kg) i.v. was followed by a marked brain acidosis which after 10 min had progressed to a drop in pH of 0.203 plus or minus 0.046 (x bar plus or minus S.D., n equals 8). The slowness ofthe development of acidosis points to a direct effect of the carbonic anhydrase inhibition on the brain tissue. As a further support for this conclusion was considered the finding of a prolonged response time of brain pH to HCO3-minus i.v. to CO2-minus inhalation, and to hyperventilation after the acetazolamide inhibtion. No changes in brain extracelllular potassium were found.

Acetazolamide↗
PubMed1994

Transcriptional regulation of rat alpha 1-acid glycoprotein gene by phenobarbital.

Phenobarbital induces gene transcription of both cytochrome P450IIB (the barbiturate-inducible cytochrome P450 in mammals) and alpha 1-acid glycoprotein, one of the major acute-phase proteins in rats and humans. Analysis of the 5'-regulatory sequences of cytochrome P450IIB and alpha 1-acid glycoprotein genes in rats revealed the presence of a consensus sequence of 10 base pairs, termed the phenobarbital-responsive element or Barbie box, located in a region extending from positions -136 to -127 from the transcription start site of the alpha 1-acid glycoprotein gene. A 17-base pair oligonucleotide probe specific for alpha 1-acid glycoprotein and including the consensus sequence showed, in mobility shift assays, slight binding to liver nuclear protein from untreated animals. This binding was strongly and specifically increased with protein extracts from phenobarbital-treated rats. Transfection of rat primary hepatocytes with the pAGPcat construct induced basal expression of chloramphenicol acetyltransferase activity, which was increased by phenobarbital and dexamethasone treatment of cells. Induction of chloramphenicol acetyltransferase activity by phenobarbital was abolished when hepatocytes were transfected by constructs with a mutation or deletion of the Barbie box sequence. These results strongly suggest that the Barbie box sequence is involved in alpha 1-acid glycoprotein gene regulation by phenobarbital.

Animals↗
PubMed1986

Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium.

A unique cytochrome P-450-dependent fatty acid monooxygenase from Bacillus megaterium ATCC 14581 is strongly induced by phenobarbital (Narhi, L. O., and Fulco, A. J. (1982) J. Biol. Chem. 257, 2147-2150) and many other barbiturates (Kim, B.-H., and Fulco, A. J. (1983) Biochem. Biophys. Res. Commun. 116, 843-850). This monooxygenase has now been purified to homogeneity from pentobarbital-induced bacteria as a single polypeptide with a molecular weight of 119,000 +/- 5,000 daltons. In the presence of NADPH and O2, it can catalyze the oxygenation of long chain fatty acids without the aid of any other protein. The enzyme has a catalytic center activity of 4,600 nmol of fatty acid oxygenated per nmol of P-450 (the highest activity yet reported for a P-450-dependent monooxygenase) and also functions as a highly active cytochrome c reductase in the presence of NADPH. The purified holoenzyme is a soluble protein containing 40 mol % hydrophobic amino acid residues and 1 mol each of FAD and FMN/mol of heme. It is isolated and purified in the low spin form but is converted to the high spin form in the presence of long chain fatty acids. The enzyme, which catalyzes the omega-2 hydroxylation of saturated fatty acids and the hydroxylation and epoxidation of unsaturated fatty acids has its highest affinity (Km = 2 +/- 1 microM) for the C15 and C16 chain lengths.

Amino Acid Sequence↗
PubMed1992

Ionic iodinated contrast medium and amobarbital sodium mixtures: potential for precipitation.

When a small amount of diatrizoate meglumine, an ionic iodinated contrast medium, is left in a catheter system before injection of amobarbital sodium or when the contrast medium is intentionally mixed with amobarbital sodium, a potentially dangerous situation occurs. The authors showed in vitro that a dense precipitate forms in this situation. This is due to an acid-base reaction between the relatively acidic contrast medium and basic barbiturate and the subsequent formation of insoluble amobarbital.

Amobarbital↗
PubMed1991

Substance use among senior medical students. A survey of 23 medical schools.

Senior students at 23 regionally distributed medical schools received an anonymous questionnaire designed to examine current and prior use of tobacco, alcohol, and nine other drugs. The overall response rate was 67% (N = 2046). Substance use prevalence rates during the 30 days preceding the survey included alcohol, 87.5%; marijuana, 10.0%; cigarettes, 10.0%; cocaine, 2.8%; tranquilizers, 2.3%; opiates other than heroin, 1.1%; psychedelics other than LSD (lysergic acid diethylamide), 0.6%; amphetamines, 0.3%; barbiturates, 0.2%; LSD, 0.1%; and heroin, 0.0%. Compared with national, age-related comparison groups, senior medical students reported less use of all substances during the past 30 days and the past 12 months, except for alcohol, tranquilizers, and psychedelics other than LSD. Substantial new drug use after entry into medical school was reported only for tranquilizers. Seven students (0.2%) admitted to current dependence on a substance other than tobacco, four of these implicating marijuana. Thirty-three students (1.6%) believed that they currently needed help for substance abuse. Only 25.7% were aware of any policy on substance abuse at their own school.

Adult↗
PubMed1983

Specific high-affinity binding sites for [3H]Ro 5-4864 in rat brain and kidney.

The binding of the novel ligand [3H]Ro 5-4864 to membrane preparations of rat kidney and brain was studied. [3H]Ro 5-4864 binds with high affinity (Kd = 0.6 nM) to a single saturable population of benzodiazepine recognition sites on renal membranes. Binding is rapidly reversible and, based on its pharmacological spectrum, takes place at the peripheral-type, Ro 5-4864-sensitive receptor. Specific high-affinity (Kd = 1.1 nM) [3H] Ro 5-4864 binding to the peripheral-type benzodiazepine binding site can also be demonstrated using rat brain membranes. [3H] Ro 5-4864 lacks stereospecificity with regard to chiral activity in position 3. A comparison of benzodiazepine inhibitory potency and structural features reveals that whereas a 4'-substitution assures specificity for the peripheral-type receptor, an N-methyl moiety is essential for optimal activity. [3H]Ro 5-4864 binding to brain membranes is temperature sensitive and is not modulated by barbiturates, convulsants, gamma-aminobutyric acid and chloride anions. The pyrazolopyridine derivative tracazolate inhibits [3H] Ro 5-4864 binding. The regional and subcellular distribution of binding is distinctly different from that previously demonstrated for [3H]benzodiazepine binding in the brain. The olfactory bulb shows the highest binding density, whereas the cerebral cortical, striatal and hippocampal areas are lowest among those areas studied. In the brain, [3H]Ro 5-4864 binding was found to sediment with the nuclear fraction. In conclusion, the present study shows that [3H]Ro 5-4864 is a selective ligand of the peripheral-type benzodiazepine binding site that can unequivocally be demonstrated in the kidney as well as the brain. The physiological significance of these findings, however, remain to be established.

Animals↗
PubMed1981

Regional and subcellular localization in rat brain of the enzymes that can synthesize gamma-hydroxybutyric acid.

Rat brain contains two major NADPH-linked aldehyde reductases that can reduce succinate semialdehyde to 4-hydroxybutyrate. One of these enzymes appears to be fairly specific for succinate semialdehyde and is not significantly inhibited by classic aldehyde reductase inhibitors such as barbiturates. The other enzyme can reduce several aromatic aldehydes and is strongly inhibited by barbiturates and branched-chain fatty acids. Using one such inhibitor, it was possible to distinguish between and measure the two enzyme activities separately in various rat brain regions and in subcellular fractions. Both enzymes are mainly cytoplasmic but there is some activity in the synaptosomal fraction. The activity of the specific succinic semialdehyde reductase is highest in the cerebellum, where it represents 21% of the total activity, and lowest in the cortex, where it represents about 11% of the total activity.

Animals↗