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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




Journal article


Biochemical and biophysical research communications

Publication Date





502 - 507


Department of Pharmacology, Oxford University, United Kingdom.


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