Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

This chapter describes the discovery of cyclic adenosine diphosphate–ribose (cADPR) as a novel endogenous Ca2+-mobilizing agent, and the way by which it fulfills most of the criteria necessary for it to be considered a second messenger. The enzymatic pathways for the synthesis and degradation of the metabolite are also summarized. The metabolic pathway of cADPR consists of synthesis from nicotinamide adenine dinucleotide (NAD+) by ADP–ribosyl cyclase and degradation by the cADPR hydrolase to ADP-ribose. CD38-like bifunctional enzymes are responsible for regulating the cellular concentration of cADPR. CD38 is an ecto-enzyme catalyzing the synthesis and the degradation of cADPR raises the possibility that cADPR may have extracellular functions. The properties of its intracellular receptor and the mechanism of its Ca2+-mobilizing activity are discussed. The physiological roles of cADPR in two specific cellular systems are reviewed in the chapter: the sea urchin egg, an invertebrate cell; and the pancreatic β cell, a mammalian system. © 1994 Academic Press Inc.

Original publication

DOI

10.1016/S0083-6729(08)60499-9

Type

Journal article

Journal

Vitamins and Hormones

Publication Date

01/01/1994

Volume

48

Pages

199 - 257