Abstract
The action of some neurotransmitters and their derivatives on succinate dehydrogenase and cytochrome oxidase of rat brain mitochondria was studied in vitro. Alpha--adrenoreceptor blocking agents phentolamine and dibenzyline abolished the inhibitory action of the native forms of catecholamines (norepinephrine, epinephrine, isoproterenol) on the enzymatic activity under study. Relationships among catecholamines, cyclic 3',5'--AMP, and cortisone in their influence on these enzymes were studied. The data obtained indicate the existence of alpha--type adrenoreceptors in the brain mitochondria which can be responsible for the regulatory influences of catecholamines on functional activity of mitochondria.
Publication types
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Comparative Study
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English Abstract
MeSH terms
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Animals
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Apomorphine / pharmacology
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Brain / drug effects
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Brain Chemistry*
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Cortisone / pharmacology
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Cyclic AMP / pharmacology
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Dopamine / pharmacology
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Electron Transport Complex IV / metabolism
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Epinephrine / pharmacology
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Isoproterenol / pharmacology
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Mitochondria / analysis*
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Mitochondria / drug effects
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Mitochondria / enzymology
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Neurotransmitter Agents / metabolism*
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Norepinephrine / pharmacology
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Phentolamine / pharmacology
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Propranolol / pharmacology
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Rats
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Receptors, Cell Surface / analysis*
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Serotonin / pharmacology
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Succinate Dehydrogenase / metabolism
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gamma-Aminobutyric Acid / pharmacology
Substances
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Neurotransmitter Agents
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Receptors, Cell Surface
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Serotonin
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gamma-Aminobutyric Acid
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Propranolol
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Cyclic AMP
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Succinate Dehydrogenase
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Electron Transport Complex IV
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Isoproterenol
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Apomorphine
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Cortisone
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Dopamine
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Norepinephrine
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Epinephrine
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Phentolamine