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Effect of ACTH and Dibutyryl Cyclic AMP on Catecholamine Synthesizing Enzymes in the Adrenals of Hypophysectomized Rats

MAINTENANCE of normal levels of adrenal medullary enzymes concerned with the synthesis of catecholamines requires an intact pituitary–adrenocortical system. Wurtman and Axelrod 1,2 showed that after hypophysectomy there is a striking decrease in adrenal levels of phenylethanolamine-N-methyl transfer...

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Published in:Nature (London) 1971-04, Vol.230 (5294), p.462-464
Main Authors: GEWIRTZ, GEORGE P, KVET ANSKÝ, RICHARD, WEISE, VIRGINIA K, KOPIN, IRWIN J
Format: Article
Language:English
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Summary:MAINTENANCE of normal levels of adrenal medullary enzymes concerned with the synthesis of catecholamines requires an intact pituitary–adrenocortical system. Wurtman and Axelrod 1,2 showed that after hypophysectomy there is a striking decrease in adrenal levels of phenylethanolamine-N-methyl transferase (PNMT), the enzyme which converts noradrenaline to adrenaline. This decrease is prevented or reversed by treatment with ACTH or glucocorticoids. Dopamine-β-hydroxylase, which is responsible for the formation of noradrenaline from dopamine, was shown by Kvetňanský et al. 3 to be decreased in the adrenal glands of hypophysectomized rats; levels of this enzyme are also restored by treatment with ACTH 4 or dexamethasone (Gewirtz et al. , unpublished observations). Tyrosine hydroxylase, the enzyme which converts tyrosine to 3,4-dihydroxyphenylalanine (DOPA), is also diminished in the adrenals of hypophysectomized rats and restored by ACTH treatment 3,5 . Unlike those of dopamine-β-hydroxylase and PNMT, however, tyrosine hydroxylase levels are not increased by treatment with dexamethasone 5 . Thus ACTH seems to have an effect on adrenal tyrosine hydroxylase which is not mediated by corticosteroids.
ISSN:0028-0836
1476-4687
DOI:10.1038/230462a0