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Journal articles on the topic 'Pyridine nucleotides'

Author: Grafiati

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 det

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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

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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 cardiom

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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 i

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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,

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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 c

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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

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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

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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 та Barbara E. CORKEY. "Temporal sequence of metabolic and ionic events in glucose-stimulated clonal pancreatic β-cells (HIT)". Biochemical Journal 315, № 3 (1 травня 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 fluorescenc

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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

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31

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 fu

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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 d

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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 Ris

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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, si

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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

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