Overview of the mammalian ADP-ribosyl-transferases clostridia toxin-like (ARTCs) family

Girolamo, Maria Di; Fabrizio, Gaia

doi:10.1016/j.bcp.2019.07.004

Cited by 28 publications

(33 citation statements)

References 110 publications

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“…Despite the very low NAD + concentrations in these compartments [55], ARTCs as well as cADPr hydrolases, such as CD38, can metabolize NAD + in the extracellular space and in serum. Since this review focuses on the influence of ADP-ribosylation on carbohydrate metabolism the reader is referred to other reviews describing extracellular NAD + consumption [45,56]. SIRTs remove acyl marks (most commonly acetylation) from proteins using NAD + as an acceptor, thereby generating OAADPR and NAM [39,57].…”

Section: Introductionmentioning

confidence: 99%

Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation

Hopp

Grüter

Hottiger

2019

Cells

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Cells constantly adapt their metabolic pathways to meet their energy needs and respond to nutrient availability. During the last two decades, it has become increasingly clear that NAD+, a coenzyme in redox reactions, also mediates several ubiquitous cell signaling processes. Protein ADP-ribosylation is a post-translational modification that uses NAD+ as a substrate and is best known as part of the genotoxic stress response. However, there is increasing evidence that NAD+-dependent ADP-ribosylation regulates other cellular processes, including metabolic pathways. In this review, we will describe the compartmentalized regulation of NAD+ biosynthesis, consumption, and regeneration with a particular focus on the role of ADP-ribosylation in the regulation of glucose metabolism in different cellular compartments.

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Section: Introductionmentioning

confidence: 99%

Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation

Hopp

Grüter

Hottiger

2019

Cells

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“…They are GPI-anchored to the cell membrane, or secreted into the extracellular space [135]. The family is constituted by several members with distinct tissue distribution and preferentially expressed on epithelial and inflammatory cells, such as lymphocytes and leukocytes [136,137]. The best characterized are ARTC1 and ARTC2, the latter only found in rodents.…”

Section: Ecto-adp-ribosyltransferasesmentioning

confidence: 99%

Enzymology of extracellular NAD metabolism

Gasparrini

Sorci

Raffaelli

2021

Cell. Mol. Life Sci.

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Extracellular NAD represents a key signaling molecule in different physiological and pathological conditions. It exerts such function both directly, through the activation of specific purinergic receptors, or indirectly, serving as substrate of ectoenzymes, such as CD73, nucleotide pyrophosphatase/phosphodiesterase 1, CD38 and its paralog CD157, and ecto ADP ribosyltransferases. By hydrolyzing NAD, these enzymes dictate extracellular NAD availability, thus regulating its direct signaling role. In addition, they can generate from NAD smaller signaling molecules, like the immunomodulator adenosine, or they can use NAD to ADP-ribosylate various extracellular proteins and membrane receptors, with significant impact on the control of immunity, inflammatory response, tumorigenesis, and other diseases. Besides, they release from NAD several pyridine metabolites that can be taken up by the cell for the intracellular regeneration of NAD itself. The extracellular environment also hosts nicotinamide phosphoribosyltransferase and nicotinic acid phosphoribosyltransferase, which inside the cell catalyze key reactions in NAD salvaging pathways. The extracellular forms of these enzymes behave as cytokines, with pro-inflammatory functions. This review summarizes the current knowledge on the extracellular NAD metabolome and describes the major biochemical properties of the enzymes involved in extracellular NAD metabolism, focusing on the contribution of their catalytic activities to the biological function. By uncovering the controversies and gaps in their characterization, further research directions are suggested, also to better exploit the great potential of these enzymes as therapeutic targets in various human diseases.

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“…[5] Ribose 5-ADP (2, in Scheme 2) is an example of a reducing sugar nucleotide, and it is found in post-translational modification processes where a single ADP-ribosyl unit or an oligomeric structure is attached to a protein. [6,7] Unconvential naming of sugar nucleotides is applied in this work to emphasise the position of the dinucleotide moiety in the sugar ring.…”

Section: Introductionmentioning

confidence: 99%

“…[18] Biological processes of reducing sugar nucleotides utilise the carbonyl group of the acyclic form as a means to attach a monomeric or polymeric ADP-ribosyl structure to a protein. [6,7] In chemical reactions, the pyrophosphate moiety is the predominant reaction site, and an intramolecular displacement at the phosphate occurs. [15,16] As an evidence of such a reaction, a nucleoside monophosphate (4,4b) is released as the major product (Scheme 2).…”

Section: Introductionmentioning

confidence: 99%