Studies on dihydropteridine reductase activity in pheochromocytoma cells.

Abstract

The activity of dihydropteridine reductase (DPR) in pheochromocytoma cells has been studied. The activity of this enzyme in crude extracts of pheochromocytoma cells is approximately 50 nmol/min/mg protein. This activity is very much greater than the activity of tyrosine 3-monooxygenase (TH) in these extracts and the rate of conversion of tyrosine to DOPA in intact pheochromocytoma cells. Incubation of the cells with 56 mM-K+ or with cholera toxin has previously been shown to increase the rate of catecholamine synthesis and to cause a stable activation of TH in the cells. These treatments do not produce a stable activation of DPR, as assayed in vitro. Methotrexate inhibits DPR activity in vitro with an I50 of approximately 20 microM, but has no effect on the rate of DOPA formation in intact pheochromocytoma cells. Therefore, DPR does not appear to be the rate-limiting enzyme in the pathway of catecholamine synthesis in pheochromocytoma cells. Moreover, the activities of DPR and of TH are not regulated coordinately in these cells.

• Authors: B T Liang, K K Vaccaro, B A Perelle, R L Perlman
• Journal: Journal of neurochemistry (J Neurochem) Vol. 37 Issue 5 Pg. 1164-9 (Nov 1981) ISSN: 0022-3042 [Print] England
• PMID: 6117603 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Tyrosine 3-Monooxygenase
• Dihydropteridine Reductase
• NADH, NADPH Oxidoreductases
• Methotrexate

Topics

• Adrenal Gland Neoplasms (enzymology)
• Dihydropteridine Reductase (metabolism)
• Humans
• Kinetics
• Methotrexate (pharmacology)
• NADH, NADPH Oxidoreductases (metabolism)
• Pheochromocytoma (enzymology)
• Tyrosine 3-Monooxygenase (metabolism)