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1.
Biull Eksp Biol Med ; 91(5): 576-8, 1981 May.
Article in Russian | MEDLINE | ID: mdl-6114762

ABSTRACT

Neuroleptics, particularly haloperidol and perphenazine, inhibit the activity of brain Ca, Mg-ATPase to a greater extent than the antidepressants benactizin and amphetamine. The actomyosin-like Ca-ATPase is far less sensitive to the psychotropic drugs than Ca,Mg-AtPase. It is suggested that the inhibition of brain Ca,Mg-AtPase by neuroleptics may play a certain role in their antipsychotic action.


Subject(s)
Brain/enzymology , Calcium-Transporting ATPases/metabolism , Psychotropic Drugs/pharmacology , Amphetamine/pharmacology , Animals , Benactyzine/pharmacology , Ca(2+) Mg(2+)-ATPase , Chlorpromazine/pharmacology , Guinea Pigs , Haloperidol/pharmacology , Imipramine/pharmacology , In Vitro Techniques , Perphenazine/pharmacology , Trazodone/pharmacology
2.
Farmakol Toksikol ; 42(1): 7-11, 1979.
Article in Russian | MEDLINE | ID: mdl-217728

ABSTRACT

Levomepromazine, chlorpromazine (10 and 30 mg/kg), etaperaxine, haloperidol (3 and 10 mg/kg) inhibited the exploratory-motor reactions of rats and the brain Na, K-ATPase activity an hour after their administration. The effects of tranquilizers as well as of antidepressants on the exploratory reactions and on the enzyme activity were not found to stand in a clearcut relation to each other. The stimulating effect of amphethamine (3 mg/kg) was accompanied by activation and suppressive action (10 mg/kg)--by inhibition of the enzyme. It is suggested that the inhibition of the brain Na, K-ATPase activity by psychotropic drugs may play a role in the mechanism of their sedative action.


Subject(s)
Brain/drug effects , Exploratory Behavior/drug effects , Psychotropic Drugs/pharmacology , Sodium-Potassium-Exchanging ATPase/metabolism , Amphetamine/pharmacology , Animals , Benactyzine/pharmacology , Chlorpromazine/pharmacology , Diazepam/pharmacology , Haloperidol/pharmacology , Imipramine/pharmacology , Iproniazid/pharmacology , Male , Methotrimeprazine/pharmacology , Perphenazine/pharmacology , Rats , Trazodone/pharmacology
3.
Ukr Biokhim Zh ; 48(3): 326-31, 1976.
Article in Russian | MEDLINE | ID: mdl-134479

ABSTRACT

The activity of Na+, K+-ATPase from bovine brain in vitro was studied as affected by some neuroleptics (levomepromazine, chlorpromazine, perphenazine and haloperidol), antidepressants (imipramine and iproniazid) and psychostimulants (amphetamine) as well as by benactyzine and procaine. The degree of the enzyme inhibition by these drugs estimated by means of I 50 and apparent inhibitor constants (Ki) or rate constants (k) was different. Sensitivity of the brain Na+, K+-ATPase to the drugs decreased in the following order: levomepromazine, chlorpromazine, perphenazine, haloperidol, imipramine, iproniazid, benactyzine, procaine and amphetamine. Competition for the enzyme was revealed between sodium and some of the drugs investigated (levomepromazine, chlorpromazine, perphenazine and impramine) as well as between potassium and other drugs (haloperidol, genactyzine and amphetamine). It is suggested that the inhibition of the brain Na+, K+-ATPase by psychotropic drugs may be a part in the biochemical mechanism of their sedative-tranquilizing activity.


Subject(s)
Adenosine Triphosphatases/metabolism , Brain/enzymology , Psychotropic Drugs/pharmacology , Adenosine Triphosphatases/antagonists & inhibitors , Amphetamine/pharmacology , Animals , Benactyzine/pharmacology , Brain/drug effects , Cattle , Chlorpromazine/pharmacology , Enzyme Activation/drug effects , Enzyme Repression/drug effects , Haloperidol/pharmacology , Imipramine/pharmacology , In Vitro Techniques , Iproniazid/pharmacology , Methotrimeprazine/pharmacology , Perphenazine/pharmacology , Potassium/metabolism , Procaine/pharmacology , Sodium/metabolism
4.
Ukr Biokhim Zh ; 47(4): 458-64, 1975.
Article in Russian | MEDLINE | ID: mdl-128866

ABSTRACT

A method is presented for obtaining the preparation of N+, K+-ATPase from the cattle brain. The specific activity of the preparation is 5 units (mu mole Pi per 1 min) per 1 mg of protein. A water-soluble derivate of carbodiimide is shown to inhibit reversibly both Na+, K+-ATPase and K+-phosphatase. ATP, Na+ and K+ manifest a protective effect against inhibition, and Na+ and K+ revealed a competition with the inhibitor for the enzyme. p-Chloromercuribenzoate inhibits irreversibly Na+, K+-ATPase and K+-phosphatase activities. The substrates ATP and p-nitrophenylphosphate protected these activities against inhibition. The phosphororganic compound O-n-butyl-S-(beta-ethyl-mercaptoethyl)-methyl thiophosphate has no significant effect on the Na+, K+-ATPase and K+-phosphatase activities.


Subject(s)
Adenosine Triphosphatases/metabolism , Brain/enzymology , Adenosine Triphosphatases/isolation & purification , Animals , Binding Sites , Carbodiimides/pharmacology , Cattle , Chloromercuribenzoates/pharmacology , Enzyme Activation , Nitrophenols/pharmacology , Organophosphorus Compounds/pharmacology , Potassium/pharmacology , Protein Binding , Sodium/pharmacology
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