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Journal articles on the topic 'Nicotinamide adenine dinucleotide'

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Published: 4 June 2021

Last updated: 20 February 2023

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1

Alberty, R. A. "Thermodynamics of Reactions of Nicotinamide Adenine Dinucleotide and Nicotinamide Adenine Dinucleotide Phosphate." Archives of Biochemistry and Biophysics 307, no. 1 (November 1993): 8–14. http://dx.doi.org/10.1006/abbi.1993.1552.

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2

Micheli, Vanna, H. Anne Simmonds, and Carlo Ricci. "Regulation of nicotinamide–adenine dinucleotide synthesis in erythrocytes of patients with hypoxanthine–guanine phosphoribosyltransferase deficiency and a patient with phosphoribosylpyrophosphate synthetase superactivity." Clinical Science 78, no. 2 (February 1, 1990): 239–45. http://dx.doi.org/10.1042/cs0780239.

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1. The synthesis of nicotinamide–adenine dinucleotide from nicotinamide and nicotinic acid was compared over different time scales at both physiological (0.7 μmol/l) and high (0.2–3 mmol/l) substrate concentrations in erythrocytes from three patients with hypoxanthine–guanine phosphoribosyltransferase (hypoxanthine phosphoribosyltransferase, EC 2.4.2.8) deficiency (including one Lesch–Nyhan patient) and from one patient with phosphoribosylpyrophosphate synthetase superactivity. The above disorders are associated with grossly altered erythrocyte nicotinamide-adenine dinucleotide levels. 2. At the physiological substrate concentration and incubation times up to 2 h, nicotinamide proved the most efficient nicotinamide–adenine dinucleotide precursor for erythrocytes from both patients and control subjects. The conversion of nicotinamide to its mononucleotide, but not further metabolism, was impaired in phosphoribosylpyrophosphate synthetase-mutant cells. The Lesch–Nyhan and phosphoribosylpyrophosphate synthetase-mutant cells were unusual in that both showed no further stimulation of nucleotide synthesis at 18 mmol/l Pi compared with 1 mmol/l. 3. At the high substrate concentrations, using 18 mmol/l Pi, nicotinamide was a poor precursor in all instances. Using nicotinic acid, nucleotide formation was 30-fold that from nicotinamide, reaching its maximum at 0.2 mmol/l. Conversion of nicotinic acid to nicotinamide–adenine dinucleotide in the phosphoribosylpyrophosphate synthetase-mutant cells was again grossly impaired. 4. There was no evidence for increased nicotinamide–adenine dinucleotide breakdown in the phosphoribosylpyrophosphate synthetase-mutant cells under any of the above conditions. 5. These results suggest that the differing nicotinamide–adenine dinucleotide levels in the two disorders cannot be related directly to the altered phosphoribosylpyrophosphate levels. The problem appears to be one of decreased synthesis in the phosphoribosylpyrophosphate synthetase-mutant cells, whereas the synthetic capacity in intact hypoxanthine–guanine phosphoribosyltransferase-deficient cells is neither enhanced nor inhibited by the raised nicotinamide–adenine dinucleotide levels.

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3

Pankiewicz, K., L. Chen, R. Petrelli, K. Felczak, G. Gao, L. Bonnac, J. Yu, and E. Bennett. "Nicotinamide Adenine Dinucleotide Based Therapeutics." Current Medicinal Chemistry 15, no. 7 (March 1, 2008): 650–70. http://dx.doi.org/10.2174/092986708783885282.

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4

Frederick, David W., Sophie Trefely, Alexia Buas, Jason Goodspeed, Jay Singh, Clementina Mesaros, Joseph A. Baur, and Nathaniel W. Snyder. "Stable isotope labeling by essential nutrients in cell culture (SILEC) for accurate measurement of nicotinamide adenine dinucleotide metabolism." Analyst 142, no. 23 (2017): 4431–37. http://dx.doi.org/10.1039/c7an01378g.

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Nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP) are conserved metabolic cofactors that mediate reduction-oxidation (redox) reactions throughout all domains of life.

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5

Kova´rˇ, J., J. Tura´nek, C. Hlava´cˇ, V. Vala, and V. Kahle. "Liquid chromatographic separations of dimers of nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate." Journal of Chromatography A 319 (January 1985): 341–49. http://dx.doi.org/10.1016/s0021-9673(01)90570-9.

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6

Lee, H. J., and G. G. Chang. "Interactions of nicotinamide-adenine dinucleotide phosphate analogues and fragments with pigeon liver malic enzyme. Synergistic effect between the nicotinamide and adenine moieties." Biochemical Journal 245, no. 2 (July 15, 1987): 407–14. http://dx.doi.org/10.1042/bj2450407.

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The structural requirements of the NADP+ molecule as a coenzyme in the oxidative decarboxylation reaction catalysed by pigeon liver malic enzyme were studied by kinetic and fluorimetric analyses with various NADP+ analogues and fragments. The substrate L-malate had little effect on the nucleotide binding. Etheno-NADP+, 3-acetylpyridine-adenine dinucleotide phosphate, and nicotinamide-hypoxanthine dinucleotide phosphate act as alternative coenzymes for the enzyme. Their kinetic parameters were similar to that of NADP+. Thionicotinamide-adenine dinucleotide phosphate, 3-aminopyridine-adenine dinucleotide phosphate, 5′-adenylyl imidodiphosphate, nicotinamide-adenine dinucleotide 3′-phosphate and NAD+ act as inhibitors for the enzyme. The first two were competitive with respect to NADP+ and non-competitive with respect to L-malate; the other inhibitors were non-competitive with NADP+. All NADP+ fragments were inhibitory to the enzyme, with a wide range of affinity, depending on the presence or absence of a 2′-phosphate group. Compounds with this group bind to the enzyme 2-3 orders of magnitude more tightly than those without this group. Only compounds with this group were competitive inhibitors with respect to NADP+. We conclude that the 2′-phosphate group is crucial for the nucleotide binding of this enzyme, whereas the carboxyamide carbonyl group of the nicotinamide moiety is important for the coenzyme activity. There is a strong synergistic effect between the binding of the nicotinamide and adenosine moieties of the nucleotide molecule.

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7

Merk, Virginia, Eugen Speiser, Wolfgang Werncke, Norbert Esser, and Janina Kneipp. "pH-Dependent Flavin Adenine Dinucleotide and Nicotinamide Adenine Dinucleotide Ultraviolet Resonance Raman (UVRR) Spectra at Intracellular Concentration." Applied Spectroscopy 75, no. 8 (July 2, 2021): 994–1002. http://dx.doi.org/10.1177/00037028211025575.

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The ultraviolet resonance Raman spectra of the adenine-containing enzymatic redox cofactors nicotinamide adenine dinucleotide and flavin adenine dinucleotide in aqueous solution of physiological concentration are compared with the aim of distinguishing between them and their building block adenine in potential co-occurrence in biological materials. At an excitation wavelength of 266 nm, the spectra are dominated by the strong resonant contribution from adenine; nevertheless, bands assigned to vibrational modes of the nicotinamide and the flavin unit are found to appear at similar signal strength. Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively.

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8

Pankiewicz, K. W., R. Petrelli, R. Singh, and K. Felczak. "Nicotinamide Adenine Dinucleotide Based Therapeutics, Update." Current Medicinal Chemistry 22, no. 34 (November 19, 2015): 3991–4028. http://dx.doi.org/10.2174/0929867322666150821100720.

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9

Kim, Jinhyun, Sahng Ha Lee, Florian Tieves, Caroline E. Paul, Frank Hollmann, and Chan Beum Park. "Nicotinamide adenine dinucleotide as a photocatalyst." Science Advances 5, no. 7 (July 2019): eaax0501. http://dx.doi.org/10.1126/sciadv.aax0501.

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Nicotinamide adenine dinucleotide (NAD+) is a key redox compound in all living cells responsible for energy transduction, genomic integrity, life-span extension, and neuromodulation. Here, we report a new function of NAD+ as a molecular photocatalyst in addition to the biological roles. Our spectroscopic and electrochemical analyses reveal light absorption and electronic properties of two π-conjugated systems of NAD+. Furthermore, NAD+ exhibits a robust photostability under UV-Vis-NIR irradiation. We demonstrate photocatalytic redox reactions driven by NAD+, such as O2 reduction, H2O oxidation, and the formation of metallic nanoparticles. Beyond the traditional role of NAD+ as a cofactor in redox biocatalysis, NAD+ executes direct photoactivation of oxidoreductases through the reduction of enzyme prosthetic groups. Consequently, the synergetic integration of biocatalysis and photocatalysis using NAD+ enables solar-to-chemical conversion with the highest-ever-recorded turnover frequency and total turnover number of 1263.4 hour−1 and 1692.3, respectively, for light-driven biocatalytic trans-hydrogenation.

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10

Pehar, Mariana, Benjamin A. Harlan, Kelby M. Killoy, and Marcelo R. Vargas. "Nicotinamide Adenine Dinucleotide Metabolism and Neurodegeneration." Antioxidants & Redox Signaling 28, no. 18 (June 20, 2018): 1652–68. http://dx.doi.org/10.1089/ars.2017.7145.

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11

Petrelli, Riccardo, Yuk Yin Sham, Liqiang Chen, Krzysztof Felczak, Eric Bennett, Daniel Wilson, Courtney Aldrich, et al. "Selective inhibition of nicotinamide adenine dinucleotide kinases by dinucleoside disulfide mimics of nicotinamide adenine dinucleotide analogues." Bioorganic & Medicinal Chemistry 17, no. 15 (August 2009): 5656–64. http://dx.doi.org/10.1016/j.bmc.2009.06.013.

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12

Nesi, Marina, Marcella Chiari, Giacomo Carrea, Gianluca Ottolina, and Pier Giorgio Righetti. "Capillary electrophoresis of nicotinamide—adenine dinucleotide and nicotinamide—adenine dinucleotide phosphate derivatives in coated tubular columns." Journal of Chromatography A 670, no. 1-2 (June 1994): 215–21. http://dx.doi.org/10.1016/0021-9673(94)80297-1.

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13

Stockman, Brian J., Ian J. Lodovice, Douglas A. Fisher, Alexander S. Mccoll, and Zhi Xie. "A Nuclear Magnetic Resonance–Based Functional Assay for Nicotinamide Adenine Dinucleotide Synthetase." Journal of Biomolecular Screening 12, no. 4 (March 22, 2007): 457–63. http://dx.doi.org/10.1177/1087057107299717.

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Nicotinamide adenine dinucleotide synthetase (NadE) is an essential enzyme for bacterial pathogens and is thus a promising antibacterial target. It catalyzes the conversion of nicotinic acid adenine dinucleotide to nicotinamide adenine dinucleotide. Changes in chemical shifts that occur in the nicotinic acid ring as it is converted to nicotinamide can be used for monitoring the reaction. A robust nuclear magnetic resonance—based activity assay was developed using robotically controlled reaction initiation and quenching. The single-enzyme assay has less potential for false positives compared to a coupled activity assay and is especially well suited to the high concentration of compounds in fragment screens. The assay has been used to screen fragment libraries for NadE inhibitors. ( Journal of Biomolecular Screening 2007:457-463)

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14

VanLinden, Magali R., Renate Hvidsten Skoge, and Mathias Ziegler. "Discovery, metabolism and functions of NAD and NADP." Biochemist 37, no. 1 (February 1, 2015): 9–13. http://dx.doi.org/10.1042/bio03701009.

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Nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP) are two major players in metabolism as they participate as electron carriers in a multitude of redox reactions. Moreover, they act in life and death decisions on a cellular level in all known life forms. NAD and NADP both exist in two states; the oxidized forms are characterized by a positive charge on the nicotinamide (Nam) moiety, denoted NAD+ and NADP+ respectively. The reduced forms are denoted NADH and NADPH (Figure 1).

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15

Ghorbania, Fatemeh, Masoomeh Ghorbani, and Arezou Ghahghaee. "The Inhibitory Effects of Nucleosides, Nicotinamide Adenine Dinucleotide, Adenosine 5'-Triphosphate, Inosine, Nicotinamide Riboside and Nicotinamide Mononucleotide Against α-Amylase and α-Glucosidase Enzymes." SDRP Journal of Food Science & Technology 5, no. 3 (2020): 182–98. http://dx.doi.org/10.25177/jfst.5.4.ra.10644.

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Diabetes is a group of metabolic disorders characterized by a high blood sugar level over a prolonged period of time. Inhibition of carbohydrate hydrolyzing enzymes leads to decrease in the absorption of glucose which is considered as one of the effective managements of diabetes mellitus. Vegetable, fruit, milk and fish are good sources of nucleosides and inosine (INO), nicotinamide riboside (NR) and nicotinamide mononucleotide (NMN) with versatile health benefits. The well-adapted structural features of these compounds for the inhibition/activation of enzymes include several available hydrogen bond (H-bond) acceptors and donors, flexible backbone and hydrophobic nature. The substrates of α-amylase (α-Amy) and α-Glucosidase (α-Glu), known as key absorbing enzymes, have functional groups (OH groups) resembling nucleosides. Therefore, the present study was conducted to evaluate the inhibitory properties of nucleosides against αAmy and α-Glu. The median inhibition concentration (IC50) values for α-Glu in the presence of adenosine (ADN), adenosine triphosphate (AMP), NR, INO, adenosine triphosphate (ATP), nicotinamide adenine dinucleotide (NAD), Adenosine diphosphate (ADP)-ribose, ADP-glucose and NMN were determined 208.6±3.8, 254.1±5.2, 177.7±4.8, 192.1±5.2, 215.9±2.7, 65.4±1.3, 63.4±2.2, 75.6±4.2 and 196.1±2.6, respectively. The IC50 values α-Amy in the presence of ADN, AMP, NR, INO, ATP, NAD, ADP-ribose, ADP-glucose and NMN were determined 145.3±2.4, 202.3±3.9, 127.7±4.8, 163.5±3.6, 185.3±1.2, 80.4±2.8, 64.8±4.7, 51.1±1.6 and 166.5±1.4, respectively. Moreover, the Ki values of NAD were calculated as 13.8±0.8 and 18.6±2.4 µM for α-Glu and α-Amy in a competitive-mode and noncompetitive -mode inhibition. In addition, to communicate with the active site of α-Glu and α-Amy respectively, NR presented a binding energy of -7.8 and -6.8 kcal/mol, INO -7.3 and -6.9, ATP -8.3 and -7.3, NAD -10.0 and -8.5, ADP-ribose -8.7 and -7.4, ADP-glucose -8.9 and -7.6, cAMP -6.6 and -6.3 and NMN -6.8 and -7.0 kcal/mol. These antioxidant inhibitors may be potential anti-diabetic drugs, not only to reduce glycemic index, but also to limit the activity of the major reactive oxygen species (ROS) producing pathways. Key words: Nucleosides, NAD, hydrolyzing enzymes, enzyme inhibition, hyperglycemia

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16

Zhang, Xiao-Nan, Albert T. Lam, Qinqin Cheng, Valentine V. Courouble, Timothy S. Strutzenberg, Jiawei Li, Yiling Wang, et al. "Discovery of an NAD⁺ analogue with enhanced specificity for PARP1." Chemical Science 13, no. 7 (2022): 1982–91. http://dx.doi.org/10.1039/d1sc06256e.

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An analogue of nicotinamide adenine dinucleotide (NAD+) featuring an azido group at 3′-OH of adenosine moiety is found to possess high specificity for human PARP1-catalyzed protein poly-ADP-ribosylation.

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17

Eisenthal, Robert, Peter J. Channon, William J. D. Whish, and Roger Harrison. "The Trifluoroacetylpyridine Analog of Nicotinamide Adenine Dinucleotide." HETEROCYCLES 37, no. 3 (1994): 1459. http://dx.doi.org/10.3987/com-93-s150.

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18

Lin, Hening. "Nicotinamide adenine dinucleotide: beyond a redox coenzyme." Organic & Biomolecular Chemistry 5, no. 16 (2007): 2541. http://dx.doi.org/10.1039/b706887e.

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19

Mohelnikova-Duchonova, Beatrice, Lenka Marsakova, David Vrana, Ivana Holcatova, Miroslav Ryska, Zdenek Smerhovsky, Alena Slamova, Miriam Schejbalova, and Pavel Soucek. "Superoxide Dismutase and Nicotinamide Adenine Dinucleotide Phosphate." Pancreas 40, no. 1 (January 2011): 72–78. http://dx.doi.org/10.1097/mpa.0b013e3181f74ad7.

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20

Jackson, J. B. "The proton-translocating nicotinamide adenine dinucleotide transhydrogenase." Journal of Bioenergetics and Biomembranes 23, no. 5 (October 1991): 715–41. http://dx.doi.org/10.1007/bf00785998.

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21

Arenas-Jal, Marta, J. M. Suñé-Negre, and Encarna García-Montoya. "Therapeutic potential of nicotinamide adenine dinucleotide (NAD)." European Journal of Pharmacology 879 (July 2020): 173158. http://dx.doi.org/10.1016/j.ejphar.2020.173158.

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22

Guillot, Benoit, Christian Jelsch, and Claude Lecomte. "The oxidized form of nicotinamide adenine dinucleotide." Acta Crystallographica Section C Crystal Structure Communications 56, no. 6 (June 1, 2000): 726–28. http://dx.doi.org/10.1107/s0108270100001220.

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23

Sharma, Ashutosh. "Photolytic oxidation of reduced nicotinamide adenine dinucleotide." Spectrochimica Acta Part A: Molecular Spectroscopy 48, no. 6 (June 1992): 893–97. http://dx.doi.org/10.1016/0584-8539(92)80086-c.

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24

Byers, S., D. Anderson, D. Brobst, and F. Cowan. "Automated assay for nicotinamide adenine dinucleotide (NAD+)†‡." Journal of Applied Toxicology 20, S1 (June 29, 2001): S19—S22. http://dx.doi.org/10.1002/1099-1263(200012)20:1+<::aid-jat694>3.0.co;2-j.

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25

Mukherjee, Sarmistha, Karthikeyani Chellappa, Andrea Moffitt, Joan Ndungu, Ryan W. Dellinger, James G. Davis, Beamon Agarwal, and Joseph A. Baur. "Nicotinamide adenine dinucleotide biosynthesis promotes liver regeneration." Hepatology 65, no. 2 (December 24, 2016): 616–30. http://dx.doi.org/10.1002/hep.28912.

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26

Bidwell, Joseph P., and John E. Stuehr. "Kinetic and thermodynamic study of the interactions of nickel(II) with nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate." Inorganic Chemistry 29, no. 6 (March 1990): 1143–47. http://dx.doi.org/10.1021/ic00331a007.

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27

Vinkovic, M., G. Dunn, G. E. Wood, J. Husain, S. P. Wood, and R. Gill. "Cleavage of nicotinamide adenine dinucleotide by the ribosome-inactivating protein fromMomordica charantia." Acta Crystallographica Section F Structural Biology Communications 71, no. 9 (August 25, 2015): 1152–55. http://dx.doi.org/10.1107/s2053230x15013540.

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The interaction of momordin, a type 1 ribosome-inactivating protein fromMomordica charantia, with NADP+and NADPH has been investigated by X-ray diffraction analysis of complexes generated by co-crystallization and crystal soaking. It is known that the proteins of this family readily cleave the adenine–ribose bond of adenosine and related nucleotides in the crystal, leaving the product, adenine, bound to the enzyme active site. Surprisingly, the nicotinamide–ribose bond of oxidized NADP+is cleaved, leaving nicotinamide bound in the active site in the same position but in a slightly different orientation to that of the five-membered ring of adenine. No binding or cleavage of NADPH was observed at pH 7.4 in these experiments. These observations are in accord with current views of the enzyme mechanism and may contribute to ongoing searches for effective inhibitors.

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28

Lucena-Cacace, Antonio, ManuelP Jiménez-García, and EvaM Verdugo-Sivianes. "Nicotinamide adenine dinucleotide+ metabolism biomarkers in malignant gliomas." Cancer Translational Medicine 2, no. 6 (2016): 189. http://dx.doi.org/10.4103/2395-3977.196912.

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29

Guillot, Benoit, Claude Lecomte, Alain Cousson, Christian Scherf, and Christian Jelsch. "High-resolution neutron structure of nicotinamide adenine dinucleotide." Acta Crystallographica Section D Biological Crystallography 57, no. 7 (June 21, 2001): 981–89. http://dx.doi.org/10.1107/s0907444901007120.

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30

Liu, Wujun, Siguo Wu, Shuhua Hou, and Zongbao (Kent) Zhao. "Synthesis of phosphodiester-type nicotinamide adenine dinucleotide analogs." Tetrahedron 65, no. 40 (October 2009): 8378–83. http://dx.doi.org/10.1016/j.tet.2009.08.007.

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31

Zhang, Fang-Jie, Qu-Ming Gu, Peicheng Jing, and Charles J. Sih. "Enzymatic cyclization of nicotinamide adenine dinucleotide phosphate (NADP)." Bioorganic & Medicinal Chemistry Letters 5, no. 19 (October 1995): 2267–72. http://dx.doi.org/10.1016/0960-894x(95)00393-8.

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32

Lee, Jaemoon, Hywyn Churchil, Woo-Baeg Choi, Joseph E. Lynch, F. E. Roberts, R. P. Volante, and Paul J. Reider. "A chemical synthesis of nicotinamide adenine dinucleotide (NAD+)." Chemical Communications, no. 8 (1999): 729–30. http://dx.doi.org/10.1039/a809930h.

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33

Murray, M. F., M. Nghiem, and A. Srinivasan. "HIV Infection Decreases Intracellular Nicotinamide Adenine Dinucleotide [NAD]." Biochemical and Biophysical Research Communications 212, no. 1 (July 1995): 126–31. http://dx.doi.org/10.1006/bbrc.1995.1945.

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34

Shabalin, Konstantin, Kirill Nerinovski, Alexander Yakimov, Veronika Kulikova, Maria Svetlova, Ljudmila Solovjeva, Mikhail Khodorkovskiy, et al. "NAD Metabolome Analysis in Human Cells Using 1H NMR Spectroscopy." International Journal of Molecular Sciences 19, no. 12 (December 6, 2018): 3906. http://dx.doi.org/10.3390/ijms19123906.

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Nicotinamide adenine dinucleotide (NAD) and its phosphorylated form, NADP, are the major coenzymes of redox reactions in central metabolic pathways. Nicotinamide adenine dinucleotide is also used to generate second messengers, such as cyclic ADP-ribose, and serves as substrate for protein modifications including ADP-ribosylation and protein deacetylation by sirtuins. The regulation of these metabolic and signaling processes depends on NAD availability. Generally, human cells accomplish their NAD supply through biosynthesis using different forms of vitamin B3: Nicotinamide (Nam) and nicotinic acid as well as nicotinamide riboside (NR) and nicotinic acid riboside (NAR). These precursors are converted to the corresponding mononucleotides NMN and NAMN, which are adenylylated to the dinucleotides NAD and NAAD, respectively. Here, we have developed an NMR-based experimental approach to detect and quantify NAD(P) and its biosynthetic intermediates in human cell extracts. Using this method, we have determined NAD, NADP, NMN and Nam pools in HEK293 cells cultivated in standard culture medium containing Nam as the only NAD precursor. When cells were grown in the additional presence of both NAR and NR, intracellular pools of deamidated NAD intermediates (NAR, NAMN and NAAD) were also detectable. We have also tested this method to quantify NAD+ in human platelets and erythrocytes. Our results demonstrate that 1H NMR spectroscopy provides a powerful method for the assessment of the cellular NAD metabolome.

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35

Albano, Jeri, Gabriel Dario Patarroyo - Aponte, and Ejaz Mahmood. "Case of acute hepatic injury and elevated ethanol levels in a non-alcoholic adult." BMJ Case Reports 12, no. 11 (November 2019): e229814. http://dx.doi.org/10.1136/bcr-2019-229814.

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Blood ethanol concentration is measured using different techniques. Gas chromatography/mass spectrometry is used in forensic laboratories to measure whole blood ethanol levels while enzyme immunoassay is often used in hospitals to measure serum or plasma ethanol levels. Lactic acidosis can theoretically cause false elevation of blood ethanol levels measured through enzymatic assay because this method measures the reduction of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide- hydrogen (NADH) via the action of a dehydrogenase. Here, we present a rare incidence of ethanol level elevation in a non-alcoholic adult male secondary to lactic acidosis from a rare form of large B-cell lymphoma with infiltration of the liver.

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36

Jiaul Haque, Al-Monsur, Jihye Kim, Gorachand Dutta, Sinyoung Kim, and Haesik Yang. "Redox cycling-amplified enzymatic Ag deposition and its application in the highly sensitive detection of creatine kinase-MB." Chemical Communications 51, no. 77 (2015): 14493–96. http://dx.doi.org/10.1039/c5cc06117b.

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37

Wang, Xiaobin, Yuqing Zhao, Qing Hua, Jiaojiao Lu, Feiyan Tang, Wenjie Sun, Feng Luan, Xuming Zhuang, and Chunyuan Tian. "An ultrasensitive electrochemiluminescence biosensor for the detection of total bacterial count in environmental and biological samples based on a novel sulfur quantum dot luminophore." Analyst 147, no. 8 (2022): 1716–21. http://dx.doi.org/10.1039/d2an00153e.

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38

Janoš, Pavel, Jiří Henych, Jan Pfeifer, Nikola Zemanová, Věra Pilařová, David Milde, Tomáš Opletal, Jakub Tolasz, Marek Malý, and Václav Štengl. "Nanocrystalline cerium oxide prepared from a carbonate precursor and its ability to breakdown biologically relevant organophosphates." Environmental Science: Nano 4, no. 6 (2017): 1283–93. http://dx.doi.org/10.1039/c7en00119c.

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39

Lipka, Pawel, Andrzej Zatorski, Kyoichi A. Watanabe, and Krzysztof W. Pankeiwicz. "Synthesis of Methylene-Bridged Analogues of Nicotinamide Riboside, Nicotinamide Mononucleotide and Nicotinamide Adenine Dinucleotide." Nucleosides and Nucleotides 15, no. 1-3 (January 1996): 149–67. http://dx.doi.org/10.1080/07328319608002377.

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40

Slama, James T., and Anne M. Simmons. "Carbanicotinamide adenine dinucleotide: synthesis and enzymological properties of a carbocyclic analog of oxidized nicotinamide adenine dinucleotide." Biochemistry 27, no. 1 (January 1988): 183–93. http://dx.doi.org/10.1021/bi00401a028.

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41

Bergel, Alain, and Maurice Comtat. "Thin-layer spectroelectrochemical study of the reversible reaction between nicotinamide adenine dinucleotide and flavin adenine dinucleotide." Journal of Electroanalytical Chemistry and Interfacial Electrochemistry 302, no. 1-2 (March 1991): 219–31. http://dx.doi.org/10.1016/0022-0728(91)85042-n.

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42

Piechowicz, Joanna, Andrzej Gamian, Danuta Zwolińska, and Dorota Polak-Jonkisz. "Adenine Nucleotide Metabolites in Uremic Erythrocytes as Metabolic Markers of Chronic Kidney Disease in Children." Journal of Clinical Medicine 10, no. 21 (November 8, 2021): 5208. http://dx.doi.org/10.3390/jcm10215208.

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Chronic kidney disease (CKD) is associated with multifaceted pathophysiological lesions including metabolic pathways in red blood cells (RBC). The aim of the study was to determine the concentration of adenine nucleotide metabolites, i.e., nicotinamide adenine dinucleotide (NAD)-oxidized form, nicotinamide adenine dinucleotide hydrate (NADH)-reduced form, nicotinic acid mononucleotide (NAMN), β-nicotinamide mononucleotide (NMN), nicotinic acid adenine dinucleotide (NAAD), nicotinic acid (NA) and nicotinamide (NAM) in RBC and to determine a relationship between NAD metabolites and CKD progression. Forty-eight CKD children and 33 age-matched controls were examined. Patients were divided into groups depending on the CKD stages (Group II-stage II, Group III- stage III, Group IV- stage IV and Group RRT children on dialysis). To determine the above-mentioned metabolites concentrations in RBC liquid chromatography-mass spectrometry was used. Results: the only difference between the groups was shown concerning NAD in RBC, although the values did not differ significantly from controls. The lowest NAD values were found in Group II (188.6 ± 124.49 nmol/mL, the highest in group IV (324.94 ± 63.06 nmol/mL. Between Groups II and IV, as well as III and IV, the differences were statistically significant (p < 0.032, p < 0.046 respectively). Conclusions. CKD children do not have evident abnormalities of RBC metabolism with respect to adenine nucleotide metabolites. The significant differences in erythrocyte NAD concentrations between CKD stages may suggest the activation of adaptive defense mechanisms aimed at erythrocyte metabolic stabilization. It seems that the implementation of RRT has a positive impact on RBC NAD metabolism, but further research performed on a larger population is needed to confirm it.

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Takizawa, Kohei, Koji Muramatsu, Kouji Maruyama, Kenichi Urakami, Takashi Sugino, Masatoshi Kusuhara, Ken Yamaguchi, Hiroyuki Ono, and Yuko Kitagawa. "Metabolic Profiling of Human Gastric Cancer Cells Treated With Salazosulfapyridine." Technology in Cancer Research & Treatment 19 (January 1, 2020): 153303382092862. http://dx.doi.org/10.1177/1533033820928621.

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Purpose: The adhesion molecule cluster of differentiation 44v9 interacts with and stabilizes the cystine/glutamate exchanger protein, which functions as a transporter of cystine. Stabilized cystine/glutamate exchanger increases extracellular cystine uptake and enhances glutathione production. Augmented levels of reduced glutathione mitigate reactive oxygen species and protect cancer cells from apoptosis. Salazosulfapyridine blocks cystine/glutamate exchanger activity and mitigates the supply of cystine to increase intracellular ROS production, thereby increasing cell susceptibility to apoptosis. This enhances the effect of anticancer drugs such as cisplatin. Currently, salazosulfapyridine is being developed as a promising anticancer agent. In the present study, we elucidated the molecular mechanism associated with salazosulfapyridine by investigating the salazosulfapyridine-induced changes in glutathione metabolism in cultured gastric cancer cell lines. Methods: The effect of salazosulfapyridine treatment on glutathione metabolism was investigated in 4 gastric cancer (AGS, MKN1, MKN45, and MKN74) and 2 colorectal cancer (HCT15 and HCT116) cell lines using metabolomic analyses. In addition, the effect of inhibition of the reduced form of nicotinamide adenine dinucleotide phosphate by 2-deoxyglucose on glutathione metabolism was evaluated. Results: Under hypoxia, enhanced glycolysis resulted in lactate accumulation with an associated reduction in nicotinamide adenine dinucleotide phosphate. Salazosulfapyridine treatment decreased the cysteine content and inhibited the formation of glutathione. Combined treatment with salazosulfapyridine and 2-deoxyglucose significantly inhibited cell proliferation. 2-Deoxyglucose, an inhibitor of glycolysis, depleted nicotinamide adenine dinucleotide phosphate required for the formation of glutathione. Conclusions: Our results indicate that in cancer cells having a predominant glycolytic pathway, metabolomic analyses under hypoxic conditions enable the profiling of global metabolism. In addition, inhibiting the supply of nicotinamide adenine dinucleotide phosphate by blocking glycolysis is a potential treatment strategy for cancer, in addition to cystine blockade by salazosulfapyridine.

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Tóth, Balázs, Iordan Iordanov, and László Csanády. "Ruling out pyridine dinucleotides as true TRPM2 channel activators reveals novel direct agonist ADP-ribose-2′-phosphate." Journal of General Physiology 145, no. 5 (April 27, 2015): 419–30. http://dx.doi.org/10.1085/jgp.201511377.

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Transient receptor potential melastatin 2 (TRPM2), a Ca2+-permeable cation channel implicated in postischemic neuronal cell death, leukocyte activation, and insulin secretion, is activated by intracellular ADP ribose (ADPR). In addition, the pyridine dinucleotides nicotinamide-adenine-dinucleotide (NAD), nicotinic acid–adenine-dinucleotide (NAAD), and NAAD-2′-phosphate (NAADP) have been shown to activate TRPM2, or to enhance its activation by ADPR, when dialyzed into cells. The precise subset of nucleotides that act directly on the TRPM2 protein, however, is unknown. Here, we use a heterologously expressed, affinity-purified–specific ADPR hydrolase to purify commercial preparations of pyridine dinucleotides from substantial contaminations by ADPR or ADPR-2′-phosphate (ADPRP). Direct application of purified NAD, NAAD, or NAADP to the cytosolic face of TRPM2 channels in inside-out patches demonstrated that none of them stimulates gating, or affects channel activation by ADPR, indicating that none of these dinucleotides directly binds to TRPM2. Instead, our experiments identify for the first time ADPRP as a true direct TRPM2 agonist of potential biological interest.

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Gasperi, Valeria, Matteo Sibilano, Isabella Savini, and Maria Catani. "Niacin in the Central Nervous System: An Update of Biological Aspects and Clinical Applications." International Journal of Molecular Sciences 20, no. 4 (February 23, 2019): 974. http://dx.doi.org/10.3390/ijms20040974.

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Niacin (also known as “vitamin B3” or “vitamin PP”) includes two vitamers (nicotinic acid and nicotinamide) giving rise to the coenzymatic forms nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP). The two coenzymes are required for oxidative reactions crucial for energy production, but they are also substrates for enzymes involved in non-redox signaling pathways, thus regulating biological functions, including gene expression, cell cycle progression, DNA repair and cell death. In the central nervous system, vitamin B3 has long been recognized as a key mediator of neuronal development and survival. Here, we will overview available literature data on the neuroprotective role of niacin and its derivatives, especially focusing especially on its involvement in neurodegenerative diseases (Alzheimer’s, Parkinson’s, and Huntington’s diseases), as well as in other neuropathological conditions (ischemic and traumatic injuries, headache and psychiatric disorders).

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Rutter, Guy A., and Elisa A. Bellomo. "Ca2+ signalling: a new route to NAADP." Biochemical Journal 411, no. 1 (March 13, 2008): e1-e3. http://dx.doi.org/10.1042/bj20080282.

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NAADP (nicotinic acid–adenine dinucleotide phosphate) is a derivative of NADP (nicotinamide–adenine dinucleotide phosphate), which differs by the presence of a nicotinic acid instead of a nicotinamide moiety. This small structural difference makes NAADP one of the most powerful second messengers known, able to mobilize intracellular Ca2+ in a wide range of cellular models, ranging from invertebrates to mammals. Despite this, our understanding of NAADP homoeostasis, metabolism and physiological action is still limited. A new report by Vasudevan and colleagues in this issue of the Biochemical Journal provides important new data by describing a new synthetic activity in sperm cells which may turn out to represent the most physiologically relevant route to this second messenger.

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Pankiewicz, Krzysztof W., and Krzysztof Felczak. "From ribavirin to NAD analogues and back to ribavirin in search for anticancer agents." Heterocyclic Communications 21, no. 5 (October 1, 2015): 249–57. http://dx.doi.org/10.1515/hc-2015-0133.

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AbstractRibavirin, a broad-spectrum antiviral agent is used in the clinic alone or in combination with other antivirals and/or interferons. Numerous structural analogues of ribavirin have been developed, among them tiazofurin, which is inactive against viruses but is a potent anticancer drug. Tiazofurin was found to inhibit nicotinamide adenine dinucleotide (NAD)-dependent inosine monophosphate dehydrogenase (IMPDH) after metabolic conversion into tiazofurin adenine dinucleotide (TAD), which binds well but could not serve as IMPDH cofactor. TAD showed high selectivity against human IMPDH vs. other cellular dehydrogenases. Mycophenolic acid (MPA) was even more specific, binding at the cofactor-binding domain of IMPDH. Ribavirin adenine dinucleotide, however, did not show any significant inhibition at the enzymatic level. We synthesized numerous NAD analogues in which natural nicotinamide riboside was replaced by tiazofurin, MPA moiety, or benzamide riboside, and the adenosine moiety as well as the pyrophosphate linker were broadly modified. Some of these compounds were found to be low nanomolar inhibitors of the enzyme and sub-micromolar inhibitors of cancer cell line proliferation. The best were as potent as tyrosine kinase inhibitor gleevec heralded as a ‘magic bullet’ against chronic myelogenous leukemia. In recent years, ribavirin was rediscovered as a potential anticancer agent against number of tumors including leukemia. It was clearly established that its antitumor activity is related to the inhibition of an oncogene, the eukaryotic translation initiation factor (eIF4E).

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Yamada, Kentaro, Chizuko Inada, Shuichi Otabe, Naoko Takane, Hideki Hayashi, and Kyohei Nonaka. "Effects of free radical scavengers on cytokine actions on islet cells." Acta Endocrinologica 128, no. 4 (April 1993): 379–84. http://dx.doi.org/10.1530/acta.0.1280379.

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We investigated the effect of free radical scavengers on the actions of cytokines on islet cells. Interferon-γ and tumor necrosis factor-α reduced the nicotinamide adenine dinucleotide content of mouse islet cells; the combination of interferon-γ (4×105 U/I) and tumor necrosis factor-α (4×105 U/I) caused nicotinamide adenine dinucleotide reduction by ∼40%. Dimethyl urea and dimethyl sulfoxide prevented the decrease, whereas superoxide dismutase, catalase, and mannitol were not effective. Dimethyl urea and dimethyl sulfoxide protected islet cells from the synergistic cytotoxic action of interferon-γ and tumor necrosis factor-α. Major histocompatibility complex class II antigen induction by interferon-γ and tumor necrosis factor-α was also inhibited by dimethyl urea and dimethyl sulfoxide, but not by superoxide dismutase, catalase and mannitol. Since superoxide dismutase of a membrane-penetrable form attenuated the class II antigen induction, the inefficiency of superoxide dismutase, catalase and mannitol may be attributable to their inability to penetrate islet cells. These results suggest that the intracellular generation of free oxygen radicals is involved in islet cell cytotoxicity and class II molecule expression by interferon-γ and tumor necrosis factor-α, and that nicotinamide adenine dinucleotide reduction may be associated with islet cell dysfunction caused by the cytokines.

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French, Samuel W. "Mechanisms of Alcoholic Liver Injury." Canadian Journal of Gastroenterology 14, no. 4 (2000): 327–32. http://dx.doi.org/10.1155/2000/801735.

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There have been numerous recent advances in the understanding of the mechanisms of alcoholic liver disease pathogenesis. Endotoxin-induced Kupffer cell activation plays a role in cytokine-mediated inflammatory changes in the liver, and this can be blocked by a diet high in saturated fat, by a diet containing lactobacillus, which does not produce endotoxin, by neomycin antibiotic sterilization of the gut, by eliminating Kupffer cells, or by removing tumour necrosis factor-alpha with antibody or by using tumour necrosis factor-alpha knockout mice. The fatty liver component is mainly the result of the nicotinamide adenine dinucleotide/reduced nicotinamide adenine dinucleotide redox shift to the reduced state by ethanol oxidation generation of reduced nicotinamide adenine dinucleotide, although this too can be blocked by a diet high in saturated fat. Hepatocytic enlargement occurs due to ethanol-induced inhibition of the ubiquitin-proteasome pathway of cytoplasmic protein degradation and the retention of oxidized proteins in hepatocytes. The liver is scarred by stellate cells that have been activated by inflammatory cytokines and growth factors produced by activated Kupffer cells, and by bile ductule metaplasia. Mallory bodies and balloon cell degeneration develop through the ethanol-induced oxidative stress-protein kinase activation pathway, inhibition of phosphatase activity and inhibition of the ubiquitin-proteasome pathway.

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Kinoshita, Hiroyuki, Naoyuki Matsuda, Hikari Kaba, Noboru Hatakeyama, Toshiharu Azma, Katsutoshi Nakahata, Yasuhiro Kuroda, Kazuaki Tange, Hiroshi Iranami, and Yoshio Hatano. "Roles of Phosphatidylinositol 3-Kinase-Akt and NADPH Oxidase in Adenosine 5′-Triphosphate–Sensitive K + Channel Function Impaired by High Glucose in the Human Artery." Hypertension 52, no. 3 (September 2008): 507–13. http://dx.doi.org/10.1161/hypertensionaha.108.118216.

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The present study was designed to examine roles of the phosphatidylinositol 3-kinase-Akt pathway and reduced nicotinamide-adenine dinucleotide phosphate oxidases in the reduced ATP-sensitive K + channel function via superoxide produced by high glucose in the human artery. We evaluated the activity of the phosphatidylinositol 3-kinase-Akt pathway, as well as reduced nicotinamide-adenine dinucleotide phosphate oxidases, the intracellular levels of superoxide and ATP-sensitive K + channel function in the human omental artery without endothelium. Levels of the p85-α subunit and reduced nicotinamide-adenine dinucleotide phosphate oxidase subunits, including p47phox, p22phox, and Rac-1, increased in the membrane fraction from arteries treated with d -glucose (20 mmol/L) accompanied by increased intracellular superoxide production. High glucose simultaneously augmented Akt phosphorylation at Ser 473, as well as Thr 308 in the human vascular smooth muscle cells. A phosphatidylinositol 3-kinase inhibitor LY294002, as well as tiron and apocynin, restored vasorelaxation and hyperpolarization in response to an ATP-sensitive K + channel opener levcromakalim. Therefore, it can be concluded that the activation of the phosphatidylinositol 3-kinase-Akt pathway, in combination with the translocation of p47phox, p22phox, and Rac-1, contributes to the superoxide production induced by high glucose, resulting in the impairment of ATP-sensitive K + channel function in the human visceral artery.

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