By Hon Cheung Lee (auth.), Hon Cheung Lee (eds.)

In the previous decade we have now witnessed the beginning and maturing of a box of study centering at the Ca2+ signaling capabilities of cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), which constructions and mechanisms of motion are actually specified between all Ca2+ messengers. quite a lot of physiological features are actually recognized to be mediated through them in cells spanning 3 organic kingdoms from protist, plant to animal. this is often the 1st booklet committed completely to the sector. the tale at the back of the emergence of the sector is informed and by way of entire reports of the enzymology, rules and gene buildings of ADP-ribosyl cyclases chargeable for metabolizing cADPR and NAADP. additionally coated is a few of the present method constructed for and popular within the box. the remainder of the publication specializes in and information the Ca2+ signaling mechanisms and particular physiological services of those messengers in a number of mobile systems.

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Lee HC and Aarhus R. 1991. ADP-ribosyl cyclase: an enzyme that cyclizes NAD+ into a calcium-mobilizing metabolite. Cell Regul. 2: 203-209. 22. Hellmich MR and Strum wasser F. 1991. Purification and characterization of a molluscan egg-specific NADase, a second-messenger enzyme. Cell Regul. 2: 193-202. 23. Glick DL. Hellmich MR, Beushausen S, Tempst P, Bayley Hand Strumwasser F. 1991. Primary structure of a molluscan egg-specific NADase, a second-messenger enzyme. Cell Regul. 2: 211-218. 24. Prasad GS, McRee DE, Stura EA, Levitt DG, Lee HC and Stout CD.

Munshi and Graeff function, cyclizing NAD to produce cADPR. Another member of this growing family is an ADP-ribosyl cyclase purified from Euglena, a membrane-bound enzyme of 40 kDa [4]. Enzymes are generally classified by the specific products they produce. Since cADPR is a newly identified metabolite, it is appropriate to group all the cADPR synthesizing enzymes together in a new family of ADP-ribosyl cyclases. Two of the members of this family, CD38 and CDlS7 have very similar catalytic properties, possessing both cADPR synthesizing and hydrolyzing activities [9, IS], while the other two members, the Aplysia and Euglena cyclases, lack the hydrolase activity [1,4].

38. Walseth TF. Aarhus R, Zeleznikar RJ, Jr. and Lee HC. 1991. Determination of endogenous levels of cyclic ADP-ribose in rat tissues. Biochirn. Biophys. Acta 1094: 113120. 39. Takahashi K, Kukimoto I, Tokita K, Inageda K, Inoue S, Kontani K, Hoshino S, Nishina H, Kanaho Y and Katada T. 1995. Accumulation of cyclic ADP-ribose measured by a specific radioimmunoassay in differentiated human leukemic HL-60 cells with all-transretinoic acid. FEBS Lett. 371: 204-208. 40. Graeff RM, Walseth TF and Lee HC.

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