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Roles of Nicotinamide Adenine Dinucleotide (NAD + ) in Biological Systems

Author

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  • Palmiro Poltronieri

    (Institute of Sciences of Food Productions, CNR-ISPA, Ecotekne, via prov.le Lecce-Monteroni km 7, 73100 Lecce, Italy)

  • Nataša Čerekovic

    (Institute of Sciences of Food Productions, CNR-ISPA, Ecotekne, via prov.le Lecce-Monteroni km 7, 73100 Lecce, Italy)

Abstract

NAD + has emerged as a crucial element in both bioenergetic and signaling pathways since it acts as a key regulator of cellular and organism homeostasis. NAD + is a coenzyme in redox reactions, a donor of adenosine diphosphate-ribose (ADPr) moieties in ADP-ribosylation reactions, a substrate for sirtuins, a group of histone deacetylase enzymes that use NAD + to remove acetyl groups from proteins; NAD + is also a precursor of cyclic ADP-ribose, a second messenger in Ca ++ release and signaling, and of diadenosine tetraphosphate (Ap4A) and oligoadenylates (oligo2′-5′A), two immune response activating compounds. In the biological systems considered in this review, NAD + is mostly consumed in ADP-ribose (ADPr) transfer reactions. In this review the roles of these chemical products are discussed in biological systems, such as in animals, plants, fungi and bacteria. In the review, two types of ADP-ribosylating enzymes are introduced as well as the pathways to restore the NAD + pools in these systems.

Suggested Citation

  • Palmiro Poltronieri & Nataša Čerekovic, 2018. "Roles of Nicotinamide Adenine Dinucleotide (NAD + ) in Biological Systems," Challenges, MDPI, vol. 9(1), pages 1-14, January.
    • Handle: RePEc:gam:jchals:v:9:y:2018:i:1:p:3-:d:127694
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    References listed on IDEAS

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    1. Peter J. Calcraft & Margarida Ruas & Zui Pan & Xiaotong Cheng & Abdelilah Arredouani & Xuemei Hao & Jisen Tang & Katja Rietdorf & Lydia Teboul & Kai-Ting Chuang & Peihui Lin & Rui Xiao & Chunbo Wang &, 2009. "NAADP mobilizes calcium from acidic organelles through two-pore channels," Nature, Nature, vol. 459(7246), pages 596-600, May.
    2. Palmiro Poltronieri, 2017. "ADP-Ribosylation Reactions in Animals, Plants, and Bacteria," Challenges, MDPI, vol. 8(1), pages 1-5, June.
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    Cited by:

    1. Masanao Miwa & Chieri Ida & Sachiko Yamashita & Kenichi Kouyama & Yasuhito Kuroda & Takayuki Eguchi & Narumi Ohta & Teruaki Sato & Masataka Tsuda & Masakazu Tanaka, 2018. "In Vivo Level of Poly(ADP-ribose)," Challenges, MDPI, vol. 9(1), pages 1-15, May.
    2. Helen R. Davison & Jack Pilgrim & Nicky Wybouw & Joseph Parker & Stacy Pirro & Simon Hunter-Barnett & Paul M. Campbell & Frances Blow & Alistair C. Darby & Gregory D. D. Hurst & Stefanos Siozios, 2022. "Genomic diversity across the Rickettsia and ‘Candidatus Megaira’ genera and proposal of genus status for the Torix group," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    3. Palmiro Poltronieri, 2020. "Emerging Concepts on the Role of ADP-Ribosylation," Challenges, MDPI, vol. 11(1), pages 1-4, February.

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