PMID: 40139Jul 31, 1979

Modulatory role of catecholamines on tyrosine hydroxylase induction

Naunyn-Schmiedeberg's Archives of Pharmacology
M I Masana, M C Rubio

Abstract

The possible modulatory role of cytoplasmic catecholamines on tyrosine hydroxylase induction was studied. Rat superior cervical ganglia were kept in organ culture and after 48 h tyrosine hydroxylase activity was determined. Exposure to 10(-4) M carbachol during 4 h almost doubled the control activity. Incubation with 10(-5) M noradrenaline or 10(-5) M dopamine impaired the carbachol-mediated induction of the enzyme. This effect was not blocked by 10(-7) M propranolol, 2.4 X 10(-6) M haloperidol or 3.1 X 10(-6) M phentolamine. Inhibition of monoamine oxidase activity by 5.1 X 10(-4) M pargyline inhibited the effect of carbachol. When the pool of endogenous catecholamines was decreased by alpha-methyl-p-tyrosine, carbachol induced tyrosine hydroxylase to the same extent as in non-depleted ganglia. It is suggested that the long-term regulation of tyrosine hydroxylase is modulated by a strategic cytoplasmic pool of catecholamines.

References

Jan 1, 1983·Comparative Biochemistry and Physiology. C, Comparative Pharmacology and Toxicology·A C Jönsson, S Nilsson

Citations

Nov 1, 1966·Proceedings of the National Academy of Sciences of the United States of America·A Alousi, N Weiner
Apr 1, 1970·European Journal of Pharmacology·R A MuellerJ Axelrod
Aug 18, 1972·Science·B F WeissR J Wurtman

Related Concepts

Carboptic
Norepinephrine, (+, -)-Isomer
Pargyline Hydrochloride
Drug Interactions
Enzyme Induction
Catecholamines
Tyrosine 3-Monooxygenase
Methyltyrosines

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