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Cyclic adenosine 5'-diphosphate ribose (cADPR) is a potent Ca2+ releasing agent in a number of tissues. A particular bifunctional NAD+ glycohydrolase is responsible for both the cyclase and hydrolase activity necessary for its synthesis from beta-NAD and degradation to ADPR. We now report that ADPR, the end-product of this enzyme, releases Ca2+ at high concentrations (above 100 microM), and at lower concentrations (10-100 microM) inhibits the hydrolysis of cADPR and potentiates the production of cADPR from NAD+. This evidence suggests that ADPR may be an important modulator of the NAD+ glycohydrolase responsible for the production of cADPR.

Original publication

DOI

10.1006/bbrc.1996.0924

Type

Journal article

Journal

Biochem Biophys Res Commun

Publication Date

25/06/1996

Volume

223

Pages

502 - 507

Keywords

ADP-ribosyl Cyclase, ADP-ribosyl Cyclase 1, Adenosine Diphosphate Ribose, Animals, Antigens, CD, Antigens, Differentiation, Calcium, Cyclic ADP-Ribose, Enzyme Inhibitors, Female, Kinetics, Microsomes, N-Glycosyl Hydrolases, NAD, Ovum, Sea Urchins