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Journal articles on the topic 'Pyridine nucleotides'

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Published: 4 June 2021
Last updated: 27 January 2023

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1

Abdellatif, Maha. "Sirtuins and Pyridine Nucleotides." Circulation Research 111, no. 5 (August 17, 2012): 642–56. http://dx.doi.org/10.1161/circresaha.111.246546.

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2

COSNIER, S., and K. LELOUS. "Amperometric detection of pyridine nucleotides via immobilized viologen-accepting pyridine nucleotide oxidoreductase or immobilized diaphorase." Talanta 43, no. 3 (March 1996): 331–37. http://dx.doi.org/10.1016/0039-9140(95)01755-0.

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3

O'Reilly, T., and D. F. Niven. "Pyridine nucleotide metabolism by extracts derived from Haemophilus parasuis and H. pleuropneumoniae." Canadian Journal of Microbiology 32, no. 9 (September 1, 1986): 733–37. http://dx.doi.org/10.1139/m86-133.

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A variety of biologically important pyridine nucleotides and precursors were examined for their capacities to serve as substrates for the synthesis of NAD by cell fractions derived from Haemophilus parasuis and H. pleuropneumoniae. Of the compounds tested, only NMN and nicotinamide riboside were converted to NAD. These reactions required ATP as co-substrate, and fractions from both organisms could also catalyze the ATP-dependent synthesis of NADP from NAD. In the absence of ATP, and depending on the pyridine compound under study, NAD, NMN, nicotinamide riboside, and also nicotinamide, were detected as products of catabolisra. It is concluded that these haemophili possess either three-membered pyridine nucleotide cycles or two-membered cycles with synthetic branches originating with nicotinamide riboside. It is also possible that the pyridine nucleotide cycles of both organisms have nonrecycling branches resulting in the "waste" of usable pyridine compound in the form of nicotinamide.
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4

Richter, C., and P. Meier. "Inhibition of pro-oxidant-induced mitochondrial pyridine nucleotide hydrolysis and calcium release by 4-hydroxynonenal." Biochemical Journal 269, no. 3 (August 1, 1990): 735–37. http://dx.doi.org/10.1042/bj2690735.

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Intra- and extra-mitochondrial Ca2+ participates in vital cellular processes. This work investigates the influence of 4-hydroxynonenal (HNE) on pro-oxidant-induced Ca2+ release from rat liver mitochondria. Ca2+ movements across the mitochondrial inner membrane, the pyridine nucleotide redox state and pyridine (nicotinamide) nucleotide hydrolysis were analysed. HNE did not influence Ca2+ uptake by mitochondria, but inhibited in a concentration-dependent manner Ca2+ release induced by t-butylhydroperoxide (tbh). Total inhibition was achieved with about 50 microM-HNE. Ca2+ release induced by the pro-oxidant alloxan was also inhibited by HNE. Oxidation of pyridine nucleotides, induced by tbh through the concerted action of glutathione peroxidase, glutathione reductase and the energy-linked transhydrogenase, was not affected by up to 50 microM-HNE. In contrast, HNE inhibited pyridine nucleotide hydrolysis in a concentration-dependent manner. The data suggest that HNE toxicity may be in part attributed to an impaired intramitochondrial Ca2+ homeostasis.
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5

Billington, Richard A., Santina Bruzzone, Antonio De Flora, Armando A. Genazzani, Friedrich Koch-Nolte, Mathias Ziegler, and Elena Zocchi. "Emerging Functions of Extracellular Pyridine Nucleotides." Molecular Medicine 12, no. 11-12 (November 2006): 324–27. http://dx.doi.org/10.2119/2006-00075.billington.

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6

Nakamura, Michinari, Aruni Bhatnagar, and Junichi Sadoshima. "Overview of Pyridine Nucleotides Review Series." Circulation Research 111, no. 5 (August 17, 2012): 604–10. http://dx.doi.org/10.1161/circresaha.111.247924.

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7

Janero, D. R., D. Hreniuk, H. M. Sharif, and K. C. Prout. "Hydroperoxide-induced oxidative stress alters pyridine nucleotide metabolism in neonatal heart muscle cells." American Journal of Physiology-Cell Physiology 264, no. 6 (June 1, 1993): C1401—C1410. http://dx.doi.org/10.1152/ajpcell.1993.264.6.c1401.

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An oxidant burden established by hydrogen peroxide (H2O2) overload may elicit postischemic myocardial damage. We assess herein the influence of H2O2-induced oxidative stress on heart muscle pyridine nucleotide metabolism. Exposure of neonatal rat cardiomyocytes to 50 microM-1.0 mM H2O2 bolus rapidly shifted their pyridine-nucleotide redox balance toward oxidation. At least 30% of the observed NADPH oxidation was independent of glutathione cycle activity and appeared chemical in nature with H2O2 itself, and not a radical metabolite, acting as oxidant. Cell exposure to H2O2 also depleted cardiomyocyte pyridine nucleotides as a consequence of enhanced utilization. The oxidative stress activated one major route of pyridine nucleotide catabolism (i.e., protein ADP-ribosylation) without acute inhibitory effect upon the other (cleavage by NAD glycohydrolase). The limited NAD sparing by metal chelators and inhibitors of ADP-ribosylation reflected pyridine nucleotide utilization for repair of single-strand DNA breaks caused by hydroxyl-like radicals formed intracellularly through iron-dependent H2O2 reduction. Cardiomyocyte NAD depletion during H2O2-induced oxidative stress was independent of cell integrity and lipid peroxidation. The NAD lost after a discrete H2O2 "pulse" was only partly replenished over a 24-h postinjury period. These data demonstrate that cardiomyocyte pyridine nucleotide metabolism is a nonperoxidative injury target that is chronically affected by H2O2 overload. Derangement of myocardial pyridine nucleotide pools due to oxidative stress may contribute to ischemic heart injury in vivo by interfering with cardiac hydrogen metabolism and redox balance.
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8

Beslin, A., M. P. Vié, J. P. Blondeau, and J. Francon. "Identification by photoaffinity labelling of a pyridine nucleotide-dependent tri-iodothyronine-binding protein in the cytosol of cultured astroglial cells." Biochemical Journal 305, no. 3 (February 1, 1995): 729–37. http://dx.doi.org/10.1042/bj3050729.

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High-affinity 3,3′,5-tri-iodo-L-thyronine (T3) binding (Kd approximately 0.3 nM) to the cytosol of cultured rat astroglial cells was strongly activated in the presence of pyridine nucleotides. A 35 kDa pyridine nucleotide-dependent T3-binding polypeptide (35K-TBP) was photoaffinity labelled using underivatized [125I]T3 in the presence of pyridine nucleotides and the free-radical scavenger dithiothreitol. Maximum activations of T3 binding and 35K-TBP photolabelling were obtained at approx. 1 x 10(-7) M NADP+ or NADPH, or 1 x 10(-4) M NADH. NAD+ and other nucleotides were without effect. NADPH is the form which activates T3 binding and 35K-TBP photolabelling, since cytosol contains NADP(+)-reducing activity, and the activation of both processes in the presence of NADPH and NADP+ was prevented by an exogenous NADPH oxidation system. NADPH behaved as an allosteric activator of T3 binding. The NADPH oxidation system promoted the release of bound T3 in the absence of any change in the total concentration of the hormone. The 35K-TBP photolabelling and [125I]T3 binding were similarly inhibited by non-radioactive T3 (half-maximum effect at 0.5-1.0 nM T3). The concentrations of iodothyronine analogues that inhibited both processes were correlated (3,3′,5-tri-iodo-D-thyronine > or = T3 > L-thyroxine > tri-iodothyroacetic acid > 3,3′5′-tri-iodo-L-thyronine). Molecular sieving and density-gradient centrifugation of cytosol identified a 65 kDa T3-binding entity, which included the 35K-TBP. These results indicate that 35K-TBP is the cytosolic entity involved in the pyridine nucleotide-dependent T3 binding, and suggest that the sequestration and release of intracellular thyroid hormones are regulated by the redox state of astroglial cell compartment(s).
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9

Buillard, C., and J. L. Dreyer. "Inhibition of CA2+Efflux by Pyridine Nucleotides." Journal of Receptor Research 11, no. 1-4 (January 1991): 653–63. http://dx.doi.org/10.3109/10799899109066433.

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10

Liu, Man, Shamarendra Sanyal, Ge Gao, Iman S. Gurung, Xiaodong Zhu, Georgia Gaconnet, Laurie J. Kerchner, et al. "Cardiac Na + Current Regulation by Pyridine Nucleotides." Circulation Research 105, no. 8 (October 9, 2009): 737–45. http://dx.doi.org/10.1161/circresaha.109.197277.

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11

Kilfoil, Peter J., Srinivas M. Tipparaju, Oleg A. Barski, and Aruni Bhatnagar. "Regulation of Ion Channels by Pyridine Nucleotides." Circulation Research 112, no. 4 (February 15, 2013): 721–41. http://dx.doi.org/10.1161/circresaha.111.247940.

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12

Stepanov, G. F., L. O. Tereshchenko, E. V. Oleinik, G. S. Maryniuk, O. I. Budalenko, and E. S. Dubna. "Efficiency of ademethionine in oxidative stress in tissues of irradiated rats." Journal of Education, Health and Sport 11, no. 6 (June 30, 2021): 192–98. http://dx.doi.org/10.12775/jehs.2021.11.06.021.

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Introduction. Ionizing radiation in low doses of low intensity causes prolonged activation of lipid per oxidation and depletion of the antioxidant system in a living organism. Moreover, Ademethionine is currently being considered as a promising antioxidant.Method. Experimental studies were carried out on 60 sexually mature male Wistar rats. The animals were irradiated in a total dose of 1Gy on a γ-therapeutic device AGAT-R No. 83 (isotope 60Co). At the end of the total dose, the rats were injected intraperitoneally with Heptral (ademethionine) after 15 minutes, 12, 24, 36, 48, 60, 72, 84, 96, 108, 120, 132, 144, 156 hours after radiation exposure at the rate of 10 mg / kg mass. After the introduction of Heptral, the animals were taken into the experiment after 24 hours, 3, 7, 15 days. In homogenates of the spleen and thymus of animals, the amount of oxidized and reduced forms of pyridine nucleotides was determined.Results. Chronic γ-irradiation in a total dose of 1Gy leads to a significant decrease in the content of reduced forms of pyridine nucleotides in the spleen and thymus of rats. Administration of Heptral to irradiated animals normalized oxidative homeostasis. So, on the 7th day of the experiment, the amount of oxidized forms of pyridine nucleotides in the spleen was 47.3% lower, and reduced - 36.3% higher than in animals that did not receive treatment. At the end of the observation period, the reduction coefficient of pyridine nucleotides in the spleen slightly differed from the control level. In comparison with irradiated animals, which were not injected with Heptral, the NADP content was lower by 70.3%, and NADPH2 - higher by 48.8%.Conclusion. The course administration of Heptral to irradiated animals leads to the normalization of the reduction factor of pyridine nucleotides. According to its mechanism of action, Heptral can be used in the complex treatment of low- intensity radiation injuries in low doses.
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13

Hunt, Lee, and Julie E. Gray. "The relationship between pyridine nucleotides and seed dormancy." New Phytologist 181, no. 1 (September 30, 2008): 62–70. http://dx.doi.org/10.1111/j.1469-8137.2008.02641.x.

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14

Rao, Ch Mohan, and J. Samuel Zigler Jr. "LEVELS OF REDUCED PYRIDINE NUCLEOTIDES AND LENS PHOTODAMAGE." Photochemistry and Photobiology 56, no. 4 (October 1992): 523–28. http://dx.doi.org/10.1111/j.1751-1097.1992.tb02196.x.

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15

Ninfali, Paolino, Luciano Baronciani, and Francesca Sani. "Adenine and Pyridine Nucleotides in Erythroid Cell Development." Cellular Physiology and Biochemistry 5, no. 2 (1995): 96–106. http://dx.doi.org/10.1159/000154744.

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16

Pietro, Anthony San. "MECHANISM OF PHOTOCHEMICAL ACCUMULATION OF REDUCED PYRIDINE NUCLEOTIDES*." Annals of the New York Academy of Sciences 103, no. 2 (December 15, 2006): 1093–105. http://dx.doi.org/10.1111/j.1749-6632.1963.tb53761.x.

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17

AW, TAK YEE. "Postnatal Changes in Pyridine Nucleotides in Rat Hepatocytes." Pediatric Research 30, no. 1 (July 1991): 112???117. http://dx.doi.org/10.1203/00006450-199107010-00020.

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18

Mou, Zhonglin. "Extracellular pyridine nucleotides as immune elicitors in arabidopsis." Plant Signaling & Behavior 12, no. 11 (November 2, 2017): e1388977. http://dx.doi.org/10.1080/15592324.2017.1388977.

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19

Deng, Wei-Wei, Riko Katahira, and Hiroshi Ashihara. "Short Term Effect of Caffeine on Purine, Pyrimidine and Pyridine Metabolism in Rice (Oryza sativa) Seedlings." Natural Product Communications 10, no. 5 (May 2015): 1934578X1501000. http://dx.doi.org/10.1177/1934578x1501000510.

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As part of our studies on the physiological and ecological function of caffeine, we investigated the effect of exogenously supplied caffeine on purine, pyrimidine and pyridine metabolism in rice seedlings. We examined the effect of 1 mM caffeine on the in situ metabolism of 14C-labelled adenine, guanine, inosine, uridine, uracil, nicotinamide and nicotinic acid. The segments of 4-day-old dark-grown seedlings were incubated with these labelled compounds for 6 h. For purines, the incorporation of radioactivity from [8-14C]adenine and [8-14C]guanine into nucleotides was enhanced by caffeine; in contrast, incorporation into CO2 were reduced. The radioactivity in ureides (allantoin and allantoic acid) from [8-14C]guanine and [8-14C]inosine was increased by caffeine. For pyrimidines, caffeine enhanced the incorporation of radioactivity from [2-14C]uridine into nucleotides, which was accompanied by a decrease in pyrimidine catabolism. Such difference was not found in the metabolism of [2-14C]uracil. Caffeine did not influence the pyridine metabolism of [carbonyl-14C]-nicotinamide and [2-14C]nicotinic acid. The possible control steps of caffeine on nucleotide metabolism in rice are discussed.
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20

Zerez, CR, MD Wong, NA Lachant, and KR Tanaka. "Impaired erythrocyte phosphoribosylpyrophosphate formation in hemolytic anemia due to pyruvate kinase deficiency." Blood 72, no. 2 (August 1, 1988): 500–506. http://dx.doi.org/10.1182/blood.v72.2.500.500.

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Abstract RBCs from patients with hemolytic anemia due to pyruvate kinase (PK) deficiency are characterized by a decreased total adenine and pyridine nucleotide content. Because phosphoribosylpyrophosphate (PRPP) is a precursor of both adenine and pyridine nucleotides, we investigated the ability of intact PK-deficient RBCs to accumulate PRPP. The rate of PRPP formation in normal RBCs (n = 11) was 2.89 +/- 0.80 nmol/min.mL RBCs. In contrast, the rate of PRPP formation in PK-deficient RBCs (n = 4) was markedly impaired at 1.03 +/- 0.39 nmol/min.mL RBCs. Impaired PRPP formation in these cells was not due to the higher proportion of reticulocytes. To study the mechanism of impaired PRPP formation, PK deficiency was simulated by incubating normal RBCs with fluoride. In normal RBCs, fluoride inhibited PRPP formation, caused adenosine triphosphate (ATP) depletion, prevented 2,3-diphosphoglycerate (DPG) depletion, and inhibited pentose phosphate shunt (PPS) activity. These results together with other data suggest that impaired PRPP formation is mediated by changes in ATP and DPG concentration, which lead to decreased PPS and perhaps decreased hexokinase and PRPP synthetase activities. Impaired PRPP formation may be a mechanism for the decreased adenine and pyridine nucleotide content in PK-deficient RBCs.
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21

Zerez, CR, MD Wong, NA Lachant, and KR Tanaka. "Impaired erythrocyte phosphoribosylpyrophosphate formation in hemolytic anemia due to pyruvate kinase deficiency." Blood 72, no. 2 (August 1, 1988): 500–506. http://dx.doi.org/10.1182/blood.v72.2.500.bloodjournal722500.

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RBCs from patients with hemolytic anemia due to pyruvate kinase (PK) deficiency are characterized by a decreased total adenine and pyridine nucleotide content. Because phosphoribosylpyrophosphate (PRPP) is a precursor of both adenine and pyridine nucleotides, we investigated the ability of intact PK-deficient RBCs to accumulate PRPP. The rate of PRPP formation in normal RBCs (n = 11) was 2.89 +/- 0.80 nmol/min.mL RBCs. In contrast, the rate of PRPP formation in PK-deficient RBCs (n = 4) was markedly impaired at 1.03 +/- 0.39 nmol/min.mL RBCs. Impaired PRPP formation in these cells was not due to the higher proportion of reticulocytes. To study the mechanism of impaired PRPP formation, PK deficiency was simulated by incubating normal RBCs with fluoride. In normal RBCs, fluoride inhibited PRPP formation, caused adenosine triphosphate (ATP) depletion, prevented 2,3-diphosphoglycerate (DPG) depletion, and inhibited pentose phosphate shunt (PPS) activity. These results together with other data suggest that impaired PRPP formation is mediated by changes in ATP and DPG concentration, which lead to decreased PPS and perhaps decreased hexokinase and PRPP synthetase activities. Impaired PRPP formation may be a mechanism for the decreased adenine and pyridine nucleotide content in PK-deficient RBCs.
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22

CICIRELLI, MICHAEL F., and L. DENNIS SMITH. "Energy Metabolism and Pyridine Nucleotide Levels during Xenopus Oocyte Maturation*, 1. (xenopus oocytes/pyridine nucleotides/energy metabolism/meiotic cell division)." Development, Growth and Differentiation 27, no. 3 (June 1985): 283–94. http://dx.doi.org/10.1111/j.1440-169x.1985.00283.x.

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23

González-García, Jorge, Sanja Tomić, Alberto Lopera, Lluís Guijarro, Ivo Piantanida, and Enrique García-España. "Aryl-bis-(scorpiand)-aza receptors differentiate between nucleotide monophosphates by a combination of aromatic, hydrogen bond and electrostatic interactions." Organic & Biomolecular Chemistry 13, no. 6 (2015): 1732–40. http://dx.doi.org/10.1039/c4ob02084g.

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24

Zhang, Xudong, and Zhonglin Mou. "Function of extracellular pyridine nucleotides in plant defense signaling." Plant Signaling & Behavior 3, no. 12 (December 2008): 1143–45. http://dx.doi.org/10.4161/psb.3.12.7185.

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25

Oka, Shin-ichi, Chiao-Po Hsu, and Junichi Sadoshima. "Regulation of Cell Survival and Death by Pyridine Nucleotides." Circulation Research 111, no. 5 (August 17, 2012): 611–27. http://dx.doi.org/10.1161/circresaha.111.247932.

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26

Charczuk, Roland, Christoph Tamm, Bruno Suri, and Thomas A. Bickle. "An unusual base pairing between pyrimidine and pyridine nucleotides." Nucleic Acids Research 14, no. 23 (1986): 9530. http://dx.doi.org/10.1093/nar/14.23.9530.

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27

Roome, Peter W., and Julian A. Peterson. "The reduction of putidaredoxin reductase by reduced pyridine nucleotides." Archives of Biochemistry and Biophysics 266, no. 1 (October 1988): 32–40. http://dx.doi.org/10.1016/0003-9861(88)90233-0.

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28

Wahlberg, Gustaf, Ulf Adamson, and Jan Svensson. "Pyridine nucleotides in glucose metabolism and diabetes: a review." Diabetes/Metabolism Research and Reviews 16, no. 1 (January 2000): 33–42. http://dx.doi.org/10.1002/(sici)1520-7560(200001/02)16:1<33::aid-dmrr79>3.0.co;2-s.

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29

CIVELEK, Vildan N., Jude T. DEENEY, Kari KUBIK, Vera SCHULTZ, Keith TORNHEIM, and Barbara E. CORKEY. "Temporal sequence of metabolic and ionic events in glucose-stimulated clonal pancreatic β-cells (HIT)." Biochemical Journal 315, no. 3 (May 1, 1996): 1015–19. http://dx.doi.org/10.1042/bj3151015.

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Stimulation of insulin release by glucose requires increased metabolism of glucose and a rise in cytosolic free Ca2+ in the pancreatic β-cell. It is accompanied by increases in respiratory rate, pyridine and flavin nucleotide reduction state, intracellular pH and the ATP/ADP ratio. To test alternative proposals of the regulatory relationships among free Ca2+, mitochondrial metabolism and cellular energy state, we determined the temporal sequence of these metabolic and ionic changes following addition of glucose to clonal pancreatic β-cells (HIT). Combined measurements of the native fluorescence of reduced pyridine nucleotides and oxidized flavin, intracellular pH, and free Ca2+ were performed together with simultaneous measurement of O2 tension or removal of samples for assay of the ATP/ADP ratio. The initial changes were detected in three phases. First, decreases occurred in the ATP/ADP ratio (< 3 s) and increases in pyridine (2±1 s) and flavin (2±1 s) nucleotide reduction. Next, increases in the O2 consumption rate (20±5 s), the ATP/ADP ratio (29±12 s) and internal pH (48±5 s) were observed. Finally, cytosolic free Ca2+ rose (114±10 s). Maximal changes in the ATP/ADP ratio, O2 consumption and pyridine and flavin nucleotide fluorescence preceded the beginning of the Ca2+ change. These relationships are consistent with a model in which phosphorylation of glucose is the initial event which generates the signals that lead to an increase in respiration, a rise in the ATP/ADP ratio and finally influx of Ca2+. Our results indicate that Ca2+ does not function as the initiator of increased mitochondrial respiration.
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30

Shiraishi, Noriyuki, and Yoshiaki Hirano. "Combination of Copper Ions and Nucleotide Generates Aggregates from Prion Protein Fragments in the N-Terminal Domain." Protein & Peptide Letters 27, no. 8 (September 24, 2020): 782–92. http://dx.doi.org/10.2174/0929866527666200225124829.

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Background: It has been previously found that PrP23-98, which contains four highly conserved octarepeats (residues 60-91) and one partial repeat (residues 92-96), polymerizes into amyloid-like and proteinase K-resistant spherical aggregates in the presence of NADPH plus copper ions. Objective: We aimed to determine the requirements for the formation of these aggregates. Methods: In this study, we performed an aggregation experiment using N-acetylated and Camidated PrP fragments of the N-terminal domain, Octa1, Octa2, Octa3, Octa4, PrP84−114, and PrP76−114, in the presence of NADPH with copper ions, and focused on the effect of the number of copper-binding sites on aggregation. Results: Among these PrP fragments, Octa4, containing four copper-binding sites, was particularly effective in forming aggregates. We also tested the effect of other pyridine nucleotides and adenine nucleotides on the aggregation of Octa4. ATP was equally effective, but NADH, NADP, ADP, and AMP had no effect. Conclusion: The phosphate group on the adenine-linked ribose moiety of adenine nucleotides and pyridine nucleotides is presumed to be essential for the observed effect on aggregation. Efficient aggregation requires the presence of the four octarepeats. These insights may be helpful in the eventual development of therapeutic agents against prion-related disorders.
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Viviano-Posadas, Alejandro O., Ulises Romero-Mendoza, Iván J. Bazany-Rodríguez, Rocío V. Velázquez-Castillo, Diego Martínez-Otero, Joanatan M. Bautista-Renedo, Nelly González-Rivas, Rodrigo Galindo-Murillo, María K. Salomón-Flores, and Alejandro Dorazco-González. "Efficient fluorescent recognition of ATP/GTP by a water-soluble bisquinolinium pyridine-2,6-dicarboxamide compound. Crystal structures, spectroscopic studies and interaction mode with DNA." RSC Advances 12, no. 43 (2022): 27826–38. http://dx.doi.org/10.1039/d2ra05040d.

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A dicationic pyridine-2,6-dicarboxamide-based compound 1 bearing two N-alkylquinolinium units was synthesized, determined by single-crystal X-ray diffraction, and studied as a fluorescent receptor for nucleotides and inorganic phosphorylated anions in pure water.
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32

Zhang, Xudong, and Zhonglin Mou. "Extracellular pyridine nucleotides inducePRgene expression and disease resistance in Arabidopsis." Plant Journal 57, no. 2 (January 2009): 302–12. http://dx.doi.org/10.1111/j.1365-313x.2008.03687.x.

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33

Osma, Natalia, Federico Maldonado, Igor Fernández-Urruzola, Theodore Train Packard, and May Gómez. "Variability of respiration and pyridine nucleotides concentration in oceanic zooplankton." Journal of Plankton Research 38, no. 3 (February 16, 2016): 537–50. http://dx.doi.org/10.1093/plankt/fbw001.

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34

Lieckfeldt, E., S. J. Jung, G. Peine, and P. Hoffmann. "Pyridine Nucleotides in Selected Plant Species Ecological and Evolutionary Aspects." Biochemie und Physiologie der Pflanzen 182, no. 5 (January 1987): 393–405. http://dx.doi.org/10.1016/s0015-3796(87)80008-2.

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35

Klaidman, Lori K., Suman K. Mukherjee, and James D. Adams. "Oxidative changes in brain pyridine nucleotides and neuroprotection using nicotinamide." Biochimica et Biophysica Acta (BBA) - General Subjects 1525, no. 1-2 (February 2001): 136–48. http://dx.doi.org/10.1016/s0304-4165(00)00181-1.

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36

STUBBERFIELD, COLIN R., STEPHEN M. A. FORROW, EULALIO ZAERA, and GERALD M. COHEN. "Redox cycling quinones induce an interconversion of hepatocyte pyridine nucleotides." Biochemical Society Transactions 16, no. 5 (October 1, 1988): 866–67. http://dx.doi.org/10.1042/bst0160866.

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37

Sokolove, Patricia M. "Oxidation of mitochondrial pyridine nucleotides by aglycone derivatives of adriamycin." Archives of Biochemistry and Biophysics 284, no. 2 (February 1991): 292–97. http://dx.doi.org/10.1016/0003-9861(91)90298-w.

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38

Tucker, Kristal R., Samantha L. Cavolo, and Edwin S. Levitan. "Elevated mitochondria-coupled NAD(P)H in endoplasmic reticulum of dopamine neurons." Molecular Biology of the Cell 27, no. 21 (November 2016): 3214–20. http://dx.doi.org/10.1091/mbc.e16-07-0479.

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Pyridine nucleotides are redox coenzymes that are critical in bioenergetics, metabolism, and neurodegeneration. Here we use brain slice multiphoton microscopy to show that substantia nigra dopamine neurons, which are sensitive to stress in mitochondria and the endoplasmic reticulum (ER), display elevated combined NADH and NADPH (i.e., NAD(P)H) autofluorescence. Despite limited mitochondrial mass, organellar NAD(P)H is extensive because much of the signal is derived from the ER. Remarkably, even though pyridine nucleotides cannot cross mitochondrial and ER membranes, inhibiting mitochondrial function with an uncoupler or interrupting the electron transport chain with cyanide (CN−) alters ER NAD(P)H. The ER CN− response can occur without a change in nuclear NAD(P)H, raising the possibility of redox shuttling via the cytoplasm locally between neuronal mitochondria and the ER. We propose that coregulation of NAD(P)H in dopamine neuron mitochondria and ER coordinates cell redox stress signaling by the two organelles.
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39

Muller-Steffner, Hélène M., Angélique Augustin, and Francis Schuber. "Mechanism of Cyclization of Pyridine Nucleotides by Bovine Spleen NAD+Glycohydrolase." Journal of Biological Chemistry 271, no. 39 (September 27, 1996): 23967–72. http://dx.doi.org/10.1074/jbc.271.39.23967.

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40

Morgan, Wingston A., Bram Prins, and Andries S. Koster. "Relationship between acute toxicity of (bis)aziridinylbenzoquinones and cellular pyridine nucleotides." Archives of Toxicology 71, no. 9 (August 6, 1997): 582–87. http://dx.doi.org/10.1007/s002040050430.

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41

Stocchi, Vilberto, Nada Kolb, Luigi Cucchiarini, Maria Segni, Mauro Magnani, and Giorgio Fornaini. "Adenine and pyridine nucleotides during rabbit reticulocyte maturation and cell aging." Mechanisms of Ageing and Development 39, no. 1 (June 1987): 29–44. http://dx.doi.org/10.1016/0047-6374(87)90084-4.

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42

JOHANSSON, Fredrik I., Agnieszka M. MICHALECKA, Ian M. MØLLER, and Allan G. RASMUSSON. "Oxidation and reduction of pyridine nucleotides in alamethicin-permeabilized plant mitochondria." Biochemical Journal 380, no. 1 (May 15, 2004): 193–202. http://dx.doi.org/10.1042/bj20031969.

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The inner mitochondrial membrane is selectively permeable, which limits the transport of solutes and metabolites across the membrane. This constitutes a problem when intramitochondrial enzymes are studied. The channel-forming antibiotic AlaM (alamethicin) was used as a potentially less invasive method to permeabilize mitochondria and study the highly branched electron-transport chain in potato tuber (Solanum tuberosum) and pea leaf (Pisum sativum) mitochondria. We show that AlaM permeabilized the inner membrane of plant mitochondria to NAD(P)H, allowing the quantification of internal NAD(P)H dehydrogenases as well as matrix enzymes in situ. AlaM was found to inhibit the electron-transport chain at the external Ca2+-dependent rotenone-insensitive NADH dehydrogenase and around complexes III and IV. Nevertheless, under optimal conditions, especially complex I-mediated NADH oxidation in AlaM-treated mitochondria was much higher than what has been previously measured by other techniques. Our results also show a difference in substrate specificities for complex I in mitochondria as compared with inside-out submitochondrial particles. AlaM facilitated the passage of cofactors to and from the mitochondrial matrix and allowed the determination of NAD+ requirements of malate oxidation in situ. In summary, we conclude that AlaM provides the best method for quantifying NADH dehydrogenase activities and that AlaM will prove to be an important method to study enzymes under conditions that resemble their native environment not only in plant mitochondria but also in other membrane-enclosed compartments, such as intact cells, chloroplasts and peroxisomes.
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43

Pétriacq, Pierre, Guillaume Tcherkez, and Bertrand Gakière. "Pyridine nucleotides induce changes in cytosolic pools of calcium in Arabidopsis." Plant Signaling & Behavior 11, no. 11 (November 1, 2016): e1249082. http://dx.doi.org/10.1080/15592324.2016.1249082.

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44

Zhang, Zhiquan, Jia Yu, and Robert C. Stanton. "A Method for Determination of Pyridine Nucleotides Using a Single Extract." Analytical Biochemistry 285, no. 1 (October 2000): 163–67. http://dx.doi.org/10.1006/abio.2000.4701.

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45

Coulombe, Roger A., Donald P. Briskin, Randal J. Keller, W. Robert Thornley, and Raghubir P. Sharma. "Vanadate-dependent oxidation of pyridine nucleotides in rat liver microsomal membranes." Archives of Biochemistry and Biophysics 255, no. 2 (June 1987): 267–73. http://dx.doi.org/10.1016/0003-9861(87)90393-6.

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46

Olsson, Thomas, Carl-Magnus Larsson, Marie Larsson, and Jan-Eric Tillberg. "Preparation of algal extracts for bacterial luciferase assay of pyridine nucleotides." Plant Science 45, no. 3 (January 1986): 189–94. http://dx.doi.org/10.1016/0168-9452(86)90138-x.

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47

Barr, Rita, Anna Stina Sandelius, Frederick L. Crane, and D. James Morré. "Oxidation of reduced pyridine nucleotides by plasma membranes of soybean hypocotyl." Biochemical and Biophysical Research Communications 131, no. 2 (September 1985): 943–48. http://dx.doi.org/10.1016/0006-291x(85)91330-0.

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48

Kovalev, Sergey A., Iu M. Chubirko, V. A. Verikovsky, V. E. Malikov, M. A. Arzumanyan, and G. V. Sukoyan. "DECREASED REDOX-POTENTIAL AND HYPERPRODUCTION OF SUPEROXIDE ANION IN BLOOD PREDICTS CARDIAC ARRHYTHMIAS AFTER DIRECT SURGICAL MYOCARDIAL REVASCULARIZATION." Medical Journal of the Russian Federation 25, no. 1 (February 15, 2019): 16–21. http://dx.doi.org/10.18821/0869-2106-2019-25-1-16-21.

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The aim of investigation was the evaluation of prognostic value of redox-potential decreasing and hyperproduction of superoxide anion in plasma with or without of total pool of pyridine nucleotides decreasing in the in-hospital complications after direct surgical myocardial revascularization. 303 patients (248 male and 48 female), mean age 58,6±6,8 years with diagnosis of ischemic heart disease and sinus rhythm without marked left ventricular dysfunction which undergoing coronary bypass graft surgery were included in the multicentral prospective study. European System for Cardiac Operative Risk Evaluation (EuroScore) and the incidence rates of post-procedural ischemic stroke CHADS2 and CHA2DS2-VASc score were calculated. Total pyridine nucleotide pool, redox-potential, hyperproduction of superoxide anion and activity of NADPH-oxidase in blood plasma were determinate before and one year after cardiac surgery. For statistical analysis the SPSS version 23.0 (SPSS Inc. Chicago, Ill) was used, all variables are expressed as mean±standard deviation (SD). The maximum of appearance of postoperative atrial fibrillation (POAF) developed in 34% patients after 1-2 days from cardiac surgery. In the cohort of patients with POAF complicated with decease of redox-potential NAD/NADH by 23% (р
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49

Zerez, CR, NA Lachant, SJ Lee, and KR Tanaka. "Decreased erythrocyte nicotinamide adenine dinucleotide redox potential and abnormal pyridine nucleotide content in sickle cell disease." Blood 71, no. 2 (February 1, 1988): 512–15. http://dx.doi.org/10.1182/blood.v71.2.512.512.

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Abstract RBCs from individuals with sickle cell disease are more susceptible to oxidant damage. Because key antioxidant defense reactions are linked to the pyridine nucleotides nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP), we tested the hypothesis that the RBC redox potential as manifested by the NADH/[NAD+ + NADH] and NADPH/[NADP+ + NADPH] ratios is decreased in sickle erythrocytes. Our data demonstrate that sickle RBCs have a significant decrease in the NADH/[NAD+ + NADH] ratio compared with normal RBCs (P less than .00005). Interestingly, sickle RBCs also had a significant increase in total NAD content compared with normal RBCs (P less than .00005). In contrast, although sickle RBCs had a significant increase in the total NADP content compared with normal RBCs (P less than .00005), sickle RBCs had no significant alteration in the NADPH/[NADP+ + NADPH] ratio. High reticulocyte controls demonstrated that these changes were not related to cell age. Thus, sickle RBCs have a decrease in NAD redox potential that may be a reflection of their increased oxidant sensitivity. The changes in these pyridine nucleotides may have further metabolic consequences for the sickle erythrocyte.
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50

Zerez, CR, NA Lachant, SJ Lee, and KR Tanaka. "Decreased erythrocyte nicotinamide adenine dinucleotide redox potential and abnormal pyridine nucleotide content in sickle cell disease." Blood 71, no. 2 (February 1, 1988): 512–15. http://dx.doi.org/10.1182/blood.v71.2.512.bloodjournal712512.

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RBCs from individuals with sickle cell disease are more susceptible to oxidant damage. Because key antioxidant defense reactions are linked to the pyridine nucleotides nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP), we tested the hypothesis that the RBC redox potential as manifested by the NADH/[NAD+ + NADH] and NADPH/[NADP+ + NADPH] ratios is decreased in sickle erythrocytes. Our data demonstrate that sickle RBCs have a significant decrease in the NADH/[NAD+ + NADH] ratio compared with normal RBCs (P less than .00005). Interestingly, sickle RBCs also had a significant increase in total NAD content compared with normal RBCs (P less than .00005). In contrast, although sickle RBCs had a significant increase in the total NADP content compared with normal RBCs (P less than .00005), sickle RBCs had no significant alteration in the NADPH/[NADP+ + NADPH] ratio. High reticulocyte controls demonstrated that these changes were not related to cell age. Thus, sickle RBCs have a decrease in NAD redox potential that may be a reflection of their increased oxidant sensitivity. The changes in these pyridine nucleotides may have further metabolic consequences for the sickle erythrocyte.
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