Modulatory role of catecholamines on tyrosine hydroxylase induction.
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.
D000818:Animals; D002217:Carbachol / Q000494:pharmacology; D002395:Catecholamines / Q000502:physiology*; D004347:Drug Interactions; D004790:Enzyme Induction / Q000187:drug effects; D005260:Female; D066298:In Vitro Techniques; D008781:Methyltyrosines / Q000494:pharmacology; D009638:Norepinephrine / Q000494:pharmacology; D010293:Pargyline / Q000494:pharmacology; D051381:Rats; D014446:Tyrosine 3-Monooxygenase / Q000096:biosynthesis*
D002395:Catecholamines; D008781:Methyltyrosines; D002217:Carbachol; D010293:Pargyline; D014446:Tyrosine 3-Monooxygenase; D009638:Norepinephrine