Abstract
Mono-ADP-ribosylation is a posttranslational protein modification reaction that was originally discovered as a mechanism by which bacterial toxins interfere with signal transduction in human host cells [1, 2]. Mono-ADP-ribosylation is also used as a mechanism to regulate endogenous metabolism, as clearly demonstrated in photosynthetic bacteria [3]. Mammalian endogenous mono-ADP-ribosylation has also been studied and the responsible enzymes have been purified and defined at the molecular level [4–9].
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References
Ueda K. and Hayaishi O. 1985. ADP-ribosylation. Annu. Rev. Biochem. 54: 73–100.
Wreggett KA. 1986. Bacterial toxins and the role of ADP-ribosylation. J. Recept. Res. 6: 95–126.
Ludden PW. 1994. Reversible ADP-ribosylation as a mechanism of enzyme regulation in procaryotes. Mol. Cell. Biochem. 138: 123–129.
Yost DA and Moss J. 1983. Amino acid-specific ADP-ribosylation. Evidence for two distinct NAD:arginine ADP-ribosyltransferases in turkey erythrocytes. J. Biol. Chem. 258: 4926–4929.
Godeau F, Belin D, and Koide SS. 1984. Mono(adenosine diphosphate ribosyl) transferase in Xenopus tissues. Direct demonstration by a zymographic localization in sodium dodecyl sulfate-polyacrylamide gels. Anal. Biochem. 137: 287–296.
Peterson JE, Larew JS and Graves DJ. 1990. Purification and partial characterization of arginine-specirlc ADP- ribosyltransferase from skeletal muscle microsomal membranes. J. Biol. Chem. 265: 17062–17069.
Maehama T, Takahashi K, Ohoka Y, Ohtsuka T, Ui M and Katada T. 1991. Identification of a botulinum C3-like enzyme in bovine brain that catalyzes ADP-ribosylation of GTP-binding proteins. J. Biol. Chem. 266: 10062–10065.
Zolkiewska A, Nightingale MS and Moss J. 1992. Molecular characterization of NAD:arginine ADP-ribosyltransferase from rabbit skeletal muscle. Proc. Natl. Acad. Sci. USA 89: 11352–11356.
Tsuchiya M, Hara N, Yamada K, Osago H and Shimoyama M. 1994. Cloning and expression of cDNA for arginine-specific ADP- ribosyltransferase from chicken bone marrow cells. J. Biol. Chem. 269: 27451–27457.
Wang J, Nemoto E, Kots AY, Kaslow HR and Dennert G. 1994. Regulation of cytotoxic T cells by ecto-nicotinamide adenine dinucleotide (NAD) correlates with cell surface GPI-anchored/arginine ADP-ribosyltransferase. J. Immunol. 153: 4048–4058.
Greiner DL, Mordes JP, Handler ES, Angelillo M, Nakamura N and Rossini AA. 1987. Depletion of RT6.T T lymphocytes induces diabetes in resistant biobreeding/Worcester (BB/W) rats. J. Exp. Med. 166: 461–475.
Mehta K and Malavasi F. 2000. Human CD38 and related molecules, Chem. Immunol. 75, Karger, Basel, Switzerland.
Kim H. Jacobson EL and Jacobson MK. 1993. Synthesis and degradation of cyclic ADP-ribose by NAD glycohydrolases. Science 261. 1330–1333.
Howard M, Grimaldi JC, Bazan JF, Lund FE, Santos-Argumedo L, Parkhouse RM, Walseth TF and Lee HC. 1993. Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38. Science 262: 1056–1059.
Zocchi E, Franco L, Guida L, Benatti U, Bargellesi A, Malavasi F, Lee HC and De Flora A. 1993. A single protein immunologically identified as CD38 displays NAD+ glycohydrolase. ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities at the outer surface of human erythrocytes. Biochem. Biophys. Res. Commun. 196: 1459–1465.
Lee HC. 1997. Mechanisms of calcium signaling by cyclic ADP-ribose and NAADP. Physiol. Rev. 11: 1133–1164.
Wu Y, Kuzma J, Marechal E, Graeff R, Lee HC, Foster R and Chua NH. 1997. Abscisic acid signaling through cyclic ADP-ribose in plants. Science 278: 2126–2130.
Takasawa S. Nata K. Yonekura H and Okamoto H. 1993. Cyclic ADP-ribose in insulin secretion from pancreatic beta cells. Science 259: 370–373.
Liberman 1957. The mechanism of the specific depression of an enzyme activity in cells in tissue culture. J. Biol. Chem. 225: 883–898.
Green S and Dobrjansky A. 1971. pH-dependent inactivation of nicotinamide-adenine dinucleotide glycohydrolase by its substrate, oxidized nicotinamide-adenine dinucleotide. Biochemistry 10: 2496–2500.
Han MK, Lee JY, Cho YS, Song YM, An NH, Kim HR and Kim UH. 1996. Regulation of NAD+ glycohydrolase activity by NAD+-dependent auto-ADP- ribosylation. Biochem. J. 318:903–908.
Han MK, Cho YS, Kim YS, Yim CY and Kim UH. 2000. Interaction of two classes of ADP-ribose transfer reactions in immune signaling. J. Biol. Chem. 275: 20799–20805.
Franco L. Guida L, Bruzzone S. Zocchi E, Usai C and De Flora A. 1998. The transmembrane glycoprotein CD38 is a catalytically active transporter responsible for generation and influx of the second messenger cyclic ADP-ribose across membranes. FASEB J. 12: 1507–1520.
Franco L, Zocchi E, Usai C, Guida L, Bruzzone S, Costa A and De Flora A. 2001. Paracrine roles of NAD+ and cyclic ADP-ribose in increasing intracellular calcium and enhancing cell proliferation of 3T3 fibroblasts. J. Biol. Chem. 276: 21642–21648.
Han MK, Kim SJ, Park YR, Shin YM, Park HJ, Park KJ, Park KH, Kim HK, Jang SI, An NH and Kim UH. 2002. Antidiabetic Effect of a Prodrug of Cysteine, L-2-Oxothiazolidine-4- carboxylic Acid, through CD38 Dimerization and Internalization. J. Biol. Chem. 277:5315–5321.
Bruzzone S, Guida L, Zocchi E, Franco L and De Flora A. 2001. Connexin 43 hemi channels mediate Ca2+-regulated transmembrane NAD+ fluxes in intact cells. FASEB J. 15: 10–12.
Kim UH, Kim MK, Kim JS, Han MK, Park BH and Kim HR. 1993. Purification and characterization of NAD glycohydrolase from rabbit erythrocytes. Arch. Biochem. Biophys. 305: 147–152.
Santos-Argumedo L, Teixeira C, Preece G, Kirkham PA and Parkhouse RM. 1993. A B lymphocyte surface molecule mediating activation and protection from apoptosis via calcium channels. J. Immunol. 151:3119–3130.
Guse AH, da Silva CP, Berg I, Skapenko AL, Weber K, Heyer P, Hohenegger M, Ashamu GA. Schulze-Koops H, Potter BV and Mayr GW. 1999. Regulation of calcium signalling in T lymphocytes by the second messenger cyclic ADP-ribose. Nature 398: 70–73.
An NH, Han MK, Urn C, Park BH, Park BJ, Kim HK and Kim UH. 2001. Significance of ecto-cyclase activity of CD38 in insulin secretion of mouse pancreatic islet cells. Biochem. Biophys. Res. Commun. 282: 781–786.
Ikehata F, Satoh J, Nata K, Tohgo A, Nakazawa T, Kato I, Kobayashi S, Akiyama T, Takasawa S, Toyota T and Okamoto H. 1998. Autoantibodies against CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase) that impair glucose-induced insulin secretion in noninsulin- dependent diabetes patients. J. Clin. Invest. 102: 395–401.
Yagui K, Shimada F, Mimura M, Hashimoto N, Suzuki Y, Tokuyama Y, Nata K, Tohgo A, Ikehata F, Takasawa S, Okamoto H, Makino H, Saito Y and Kanatsuka A. 1998. A missense mutation in the CD38 gene, a novel factor for insulin secretion: association with Type II diabetes mellitus in Japanese subjects and evidence of abnormal function when expressed in vitro. Diabetologia 41: 1024–1028.
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Kim, UH., Han, MK., Yim, CY. (2002). ADP-Ribosylation and CD38 Signaling. In: Lee, H.C. (eds) Cyclic ADP-Ribose and NAADP. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0269-2_19
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DOI: https://doi.org/10.1007/978-1-4615-0269-2_19
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