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T. Nagatsu, M. Levitt, S. Udenfriend (1964)
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Nakanishi: cAMP-dependent inhibition of biopterin transport Pteridines Vol. 7, 1996, pp. 35-37 Short Communication Nobuo Nakanishi Departments of Biochemistry, Meikai University School of Dentistry, Sakado, Saitama 350-02, Japan (Received November 22 , 1995) Introduction Cyclic AMP (cAMP), one of the major intracellular messengers, stimulates catecholamine biosynthesis. Tyrosine hydroxylase, a rate-limiting enzyme in catecholamine synthesis ( 1), is ac tivated by phosphorylation with cAMP-dependent protein kinase (protein kinase A) (2), and expression of this enzyme is enhanced by the protein kinase A pathway (3 ). Biosynthesis of tetrahydrobiopioterin (BH4), an essential cofactor for tyrosine hydroxylase (I), is also enhanced by cyclic AMP (4-8 ) and when the amount of BH4 is increased in this manner within the cell it may engage cooperativity with stimulated tyrosine hydroxylase in catecholamine biosvnthesis. BH4 has also been reported to have other func tions such as stimulation of monoamine neurotransmitter release in the brain (9, 10), cofactor activity for nitric oxide synthase (11, 12 ) and stimulation of erythroleukemia cell proliferation (13, 14 ), indicating that BH4 has a wide range of activity, both in the extracellular fluid as well as possibility within those cells which do not produce BH4 themselves. Since BH4 synthesis
Pteridines – de Gruyter
Published: Feb 1, 1996
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