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Journal articles on the topic 'Purine catabolism'

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Published: 10 December 2022

Last updated: 28 January 2023

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1

Tomlinson, Patricia Tolson, and Carol J. Lovatt. "Nucleotide Metabolism in ‘Washington’ Navel Orange Fruit: I. Pathways of Synthesis and Catabolism." Journal of the American Society for Horticultural Science 112, no. 3 (May 1987): 529–35. http://dx.doi.org/10.21273/jashs.112.3.529.

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Abstract The capacity of ‘Washington’ navel orange fruit [Citrus sinensis (L.) Osbeck] to synthesize and catabolize purines and pyrimidines was assessed. De novo biosynthesis of purine nucleotide was demonstrated by [14C] bicarbonate incorporation into purine nucleotides, blockage of this process by four known inhibitors, and assimilation of radiolabeled carbon from formate, both carbons of glycine, and carbon-3 of serine into the adenine ring. De novo synthesis of pyrimidines via the orotate pathway in young fruit was demonstrated by incorporation of [14C] bicarbonate and [6-14C]orotic acid into uridine nucleotides, release of 14CO2 from [7-14C]orotic acid, and blockage of these processes by 6-azauridine. Synthesis of purine and pyrimidine nucleotides via salvage reactions was demonstrated by incorporation of radiolabeled bases and ribonucleosides into nucleotides and into nucleic acids. Release of 14CO2 from radiolabeled adenine, adenosine, hypoxanthine, and xanthine, uric acid, urea (purines), uracil, and uridine (pyrimidines) provided evidence the pathways for catabolism (degradation) of purines and pyrimidines in navel orange fruit are similar to those found in microorganisms and animal tissues. To the best of our knowledge, this report is the first to assess the capacity of anabolic and catabolic pathways of purine and pyrimidine nucleotide metabolism in fruit of any species. De novo synthetic activities in orange fruit permit increases in the pools of purine and pyrimidine nucleotides using simple precursors. Further, the patterns of salvage and catabolism suggest riboside pools are reused predominantly as nucleotides, while the majority of base pools are degraded to permit recycling of carbon and nitrogen into other metabolites.

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2

Xi, Hualin, Barbara L. Schneider, and Larry Reitzer. "Purine Catabolism in Escherichia coliand Function of Xanthine Dehydrogenase in Purine Salvage." Journal of Bacteriology 182, no. 19 (October 1, 2000): 5332–41. http://dx.doi.org/10.1128/jb.182.19.5332-5341.2000.

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ABSTRACT Escherichia coli is not known to utilize purines, other than adenine and adenosine, as nitrogen sources. We reinvestigated purine catabolism because a computer analysis suggested several potential ς54-dependent promoters within a 23-gene cluster whose products have homology to purine catabolic enzymes. Our results did not provide conclusive evidence that the ς54-dependent promoters are active. Nonetheless, our results suggest that some of the genes are metabolically significant. We found that even though several purines did not support growth as the sole nitrogen source, they did stimulate growth with aspartate as the nitrogen source. Cells produced 14CO2 from minimal medium containing [14C]adenine, which implies allantoin production. However, neither ammonia nor carbamoyl phosphate was produced, which implies that purine catabolism is incomplete and does not provide nitrogen during nitrogen-limited growth. We constructed strains with deletions of two genes whose products might catalyze the first reaction of purine catabolism. Deletion of one eliminated 14CO2 production from [14C]adenine, which implies that its product is necessary for xanthine dehydrogenase activity. We changed the name of this gene to xdhA. The xdhA mutant grew faster with aspartate as a nitrogen source. The mutant also exhibited sensitivity to adenine, which guanosine partially reversed. Adenine sensitivity has been previously associated with defective purine salvage resulting from impaired synthesis of guanine nucleotides from adenine. We propose that xanthine dehydrogenase contributes to this purine interconversion.

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3

Sun, Runbin, Jingqiu Huang, Na Yang, Jun He, Xiaoyi Yu, Siqi Feng, Yuan Xie, Guangji Wang, Hui Ye, and Jiye Aa. "Purine Catabolism Shows a Dampened Circadian Rhythmicity in a High-fat Diet-Induced Mouse Model of Obesity." Molecules 24, no. 24 (December 10, 2019): 4524. http://dx.doi.org/10.3390/molecules24244524.

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High-calorie diet, circadian rhythms and metabolic features are intimately linked. However, the mediator(s) between nutritional status, circadian rhythms and metabolism remain largely unknown. This article aims to clarify the key metabolic pathways bridging nutritional status and circadian rhythms based on a combination of metabolomics and molecular biological techniques. A mouse model of high-fat diet-induced obesity was established and serum samples were collected in obese and normal mice at different zeitgeber times. Gas chromatography/mass spectrometry, multivariate/univariate data analyses and metabolic pathway analysis were used to reveal changes in metabolism. Metabolites involved in the metabolism of purines, carbohydrates, fatty acids and amino acids were markedly perturbed in accordance with circadian related variations, among which purine catabolism showed a typical oscillation. What’s more, the rhythmicity of purine catabolism dampened in the high-fat diet group. The expressions of clock genes and metabolic enzymes in the liver were measured. The mRNA expression of Xanthine oxidase (Xor) was highly correlated with the rhythmicity of Clock, Rev-erbα and Bmal1, as well as the metabolites involved in purine catabolism. These data showed that a high-fat diet altered the circadian rhythm of metabolic pathways, especially purine catabolism. It had an obvious circadian oscillation and a high-fat diet dampened its circadian rhythmicity. It was suggested that circadian rhythmicity of purine catabolism is related to circadian oscillations of expression of Xor, Uox and corresponding clock genes.

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4

Yin, Yuling, Riko Katahira, and Hiroshi Ashihara. "Metabolism of Purine Alkaloids and Xanthine in Leaves of Maté (Ilex paraguariensis)." Natural Product Communications 10, no. 5 (May 2015): 1934578X1501000. http://dx.doi.org/10.1177/1934578x1501000503.

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Accumulation and metabolism of purine alkaloids in leaves of maté ( Ilex paraguariensis) were investigated. In winter, leaves accumulated caffeine but not theobromine, indicating that caffeine is the end product of purine alkaloid synthesis in maté. To elucidate the purine alkaloid metabolism in maté leaves, the metabolic fate of [8-14C]theobromine, [8-14C]theophylline, [8-14C]caffeine and [8-14C] xanthine was investigated in the leaf disks of young and mature leaves. In young maté leaves, significant amounts of theobromine and theophylline were utilized for caffeine biosynthesis, but the conversion was not observed in mature leaves. A small amount of theophylline was converted to theobromine. Practically no caffeine catabolism was detected in maté leaves during a 24 h-incubation. Catabolism of theobromine and theophylline via 3-methylxanthine was observed mainly in mature leaves. Xanthine was catabolised extensively via ureides in both young and mature leaves, but limited amounts are also utilized for the synthesis of theobromine, theophylline and caffeine. Possible pathways for the metabolism of purine alkaloids in maté leaves are discussed.

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5

Muzychka, Oksana, Olexandr Kobzar, Oleg Shablykin, Volodymyr Brovarets, and Andriy Vovk. "5-Substituted N-(9H-purin-6-yl)-1,2-oxazole-3-carboxamides as xanthine oxidase inhibitors." Ukr. Bioorg. Acta 2020, Vol. 15, N1 15, no. 1 (June 30, 2020): 20–25. http://dx.doi.org/10.15407/bioorganica2020.01.020.

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Synthetic 6-substituted purine derivatives are known to exhibit diverse bioactivity. In this paper, a series of N-(9H-purin-6-yl)-1,2-oxazole-3-carboxamide derivatives were synthesized and evaluated in vitro against xanthine oxidase, an enzyme of purine catabolism. The introduction of aryl substituent at position 5 of the oxazole ring was found to increase the inhibition efficiency. Some of the inhibitors containing 5-substituted isoxazole and purine moieties were characterized by IC50 values in the nanomolar range. According to the kinetic data, the most active N-(9H-purin-6-yl)-5-(5,6,7,8-tetrahydronaphthalen-2-yl)-1,2-oxazole-3-carboxamide demonstrated a competitive type of inhibition with respect to the enzyme-substrate. Molecular docking was carried out to elucidate the mechanism of enzyme-inhibitor complex formation. The data obtained indicate that xanthine oxidase may be one of the possible targets for the bioactive purine carboxamides.

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6

Itakura, M., N. Maeda, and K. Yamashita. "Increased rate of purine biosynthesis in rat liver after bilateral adrenalectomy." American Journal of Physiology-Endocrinology and Metabolism 251, no. 4 (October 1, 1986): E373—E378. http://dx.doi.org/10.1152/ajpendo.1986.251.4.e373.

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In bilaterally adrenalectomized rat liver the increased rate of de novo purine synthesis was shown by the increased [14C]glycine incorporation into hepatic acid-soluble purines with unchanged rapidly miscible glycine pool size and its turnover rate and by the increased rate of chasing of radiolabeled purines. At 24 h after adrenalectomy, the rate of de novo purine synthesis increased by 70%, 5-phosphoribosyl-1-pyrophosphate (PRPP) content increased by 200%, the specific activity of amidophosphoribosyltransferase (EC 2.4.2. 14; ATase) did not change, ATP and GTP showed a 33 and 24% decrease, and AMP and ADP showed a 245 and 38% increase. Combined, the metabolic pool size data reflected an unchanged total inhibitory potential on ATase. Replacement with corticosterone acetate for 24 h partially restored some of these abnormalities. These results suggest that the increase in the rate of de novo purine synthesis in adrenalectomized rat liver is secondary to increased catabolism of purine ribonucleotides and mediated by increased PRPP concentrations.

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7

Pizzichin, M., M. L. Pandolfi, L. Terzuoli, L. Arezzini, and R. Pagani. "Purine nucleotide catabolism in rat liver." Biochemical Society Transactions 21, no. 2 (May 1, 1993): 189S. http://dx.doi.org/10.1042/bst021189s.

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8

HADANO, SHINJI, SATOSHI SAKAI, MASASHI OGASAWARA, and AKIRA ITO. "EFFECTS OF EXERCISE INTENSITY ON PURINE CATABOLISM." Japanese Journal of Physical Fitness and Sports Medicine 37, no. 3 (1988): 225–33. http://dx.doi.org/10.7600/jspfsm1949.37.225.

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9

Felici, C., I. Ciari, L. Terzuoli, B. Porcelli, C. Setacci, M. Giubbolini, and E. Marinello. "Purine Catabolism in Advanced Carotid Artery Plaque." Nucleosides, Nucleotides and Nucleic Acids 25, no. 9-11 (June 2006): 1291–94. http://dx.doi.org/10.1080/15257770600890772.

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10

Voloshchuk, Oksana, Halyna Kopylchuk, and Andriana Plytus. "Activity of purine nucleotide catabolic enzymes in the liver of rats under conditions of nutritional imbalance." Biolohichni systemy 12, no. 2 (December 23, 2020): 119–24. http://dx.doi.org/10.31861/biosystems2020.02.119.

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The aim of the study was to investigate the activity of purine nucleotide catabolism enzymes, in particular, AMP-deaminase, 5'-nucleotidase, guanosine deaminase, and guanosine phosphorylase and xanthine oxidase in the cytosolic fraction of the liver of rats under conditions of different dietary supply of sucrose and dietary proteins. Enzyme activity was determined by photo colorimetric method: AMP-deaminase activity by the amount of ammonia formed by deamination of AMP, which has a maximum absorption at λ-540 nm and 5'-nucleotidase activity by the amount of Pn formed by hydrolysis of AMP at λ-8. The activity of guanosine phosphorylase, guanosine deaminase and xanthine oxidase was determined by spectrophotometric method. The results of studies have shown that due to consuming a high-sucrose diet in on the background of protein deficiency, the activation of purine nucleotide catabolism is observed and it can lead to disruption of the regulation of energy-dependent processes in liver cells. A critical factor influencing on the state of the purine nucleotide system and the activity of enzymes of their catabolism is alimentary protein deficiency.

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11

Rosiers, Christine Des, Stephan Nees, and Eckehart Gerlach. "Purine metabolism in cultured aortic and coronary endothelial cells." Biochemistry and Cell Biology 67, no. 1 (January 1, 1989): 8–15. http://dx.doi.org/10.1139/o89-002.

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Purine salvage pathways in cultured endothelial cells of macrovascular (pig aorta) and microvascular (guinea pig coronary system) origin were investigated by measuring the incorporation of radioactive purine bases (adenine or hypoxanthine) or nucleosides (adenosine or inosine) into purine nucleotides. These precursors were used at initial extracellular concentrations of 0.1, 5, and 500 μM. In both types of endothelial cells, purine nucleotide synthesis occurred with all four substrates. Aortic endothelial cells salvaged adenine best among purines and nucleosides when applied at 0.1 μM. At 5 and 500 μM, adenosine was the best precursor. In contrast, microvascular endothelial cells from the coronary system used adenosine most efficiently at all concentrations studied. The synthetic capacity of salvage pathways was greater than that of the de novo pathway. As measured using radioactive formate or glycine, de novo synthesis of purine nucleotides was barely detectable in aortic endothelial cells, whereas it readily occurred in coronary endothelial cells. Purine de novo synthesis in coronary endothelial cells was inhibited by physiological concentrations of purine bases and nucleosides, and by ribose or isoproterenol. The isoproterenol-induced inhibition was prevented by the β-adrenergic receptor antagonist propranolol. The end product of purine catabolism in aortic endothelial cells was found to be hypoxanthine, whereas coronary endothelial cells degraded hypoxanthine further to xanthine and uric acid, a reaction catalyzed by the enzyme xanthine dehydrogenase.Key words: purine metabolism, aortic endothelial cells, coronary endothelial cells, β-adrenergic receptor.

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12

Werner, Andrea K., and Claus-Peter Witte. "The biochemistry of nitrogen mobilization: purine ring catabolism." Trends in Plant Science 16, no. 7 (July 2011): 381–87. http://dx.doi.org/10.1016/j.tplants.2011.03.012.

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13

Fluri, R., and J. R. Kinghorn. "Induction control of purine catabolism in Schizosaccharomyces pombe." Current Genetics 9, no. 7 (July 1985): 573–78. http://dx.doi.org/10.1007/bf00381170.

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14

Carvalhal, Ana V., Sónia Sá Santos, and Manuel J. T. Carrondo. "Extracellular purine and pyrimidine catabolism in cell culture." Biotechnology Progress 27, no. 5 (June 21, 2011): 1373–82. http://dx.doi.org/10.1002/btpr.656.

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15

Kato, Misako, and Hiroshi Ashihara. "Biosynthesis and Catabolism of Purine Alkaloids in Camellia Plants." Natural Product Communications 3, no. 9 (September 2008): 1934578X0800300. http://dx.doi.org/10.1177/1934578x0800300907.

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A few Camellia plants accumulate caffeine, theobromine and theacrine. The present article reviews the distribution of purine alkaloids and biosynthetic pathways, including properties and genes of the caffeine synthase family of enzymes, and catabolism. Plant physiological studies and ecology-related studies are also summarized briefly.

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16

PIZZICHINI, MARIA, MARIA LUISA PANDOLFI, GIULIANO CINCI, LUCIA TERZUOLI, BRUNETTA PORCELLI, ROBERTO PAGANI, and ROSELLA FULCERI. "Study of purine catabolism using 14C-glycine as tracer." Biochemical Society Transactions 20, no. 4 (November 1, 1992): 376S. http://dx.doi.org/10.1042/bst020376s.

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17

Yang, Yu-dan, Ji-zhou Zhang, Cong Sun, Hong-mei Yu, Qi Li, and Min Hong. "Heroin affects purine nucleotides catabolism in rats in vivo." Life Sciences 78, no. 13 (February 2006): 1413–18. http://dx.doi.org/10.1016/j.lfs.2005.07.014.

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18

Zhang, J. D., F. X. Zhang, L. F. Guo, N. Li, and B. E. Shan. "Chronic alcohol administration affects purine nucleotide catabolism in vivo." Life Sciences 168 (January 2017): 58–64. http://dx.doi.org/10.1016/j.lfs.2016.11.008.

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19

TRITSCH, GEORGE L., and PAUL W. NISWANDER. "Purine Catabolism as a Source of Superoxide in Macrophages." Annals of the New York Academy of Sciences 451, no. 1 (October 1985): 279–90. http://dx.doi.org/10.1111/j.1749-6632.1985.tb27119.x.

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20

Kristal, Bruce S., Karen E. Vigneau-Callahan, Alison J. Moskowitz, and Wayne R. Matson. "Purine Catabolism: Links to Mitochondrial Respiration and Antioxidant Defenses?" Archives of Biochemistry and Biophysics 370, no. 1 (October 1999): 22–33. http://dx.doi.org/10.1006/abbi.1999.1387.

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21

Mandava, Kiranmai, and Uma Rajeswari Batchu. "BIOCHEMICAL ROLE OF XANTHINE OXIDOREDUCTASE AND ITS NATURAL INHIBITORS: AN OVERVIEW." International Journal of Pharmacy and Pharmaceutical Sciences 8, no. 10 (August 12, 2016): 57. http://dx.doi.org/10.22159//ijpps.v8i10.13927.

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<p>Xanthine oxidoreductase (XOR) is a widely distributed housekeeping enzyme in mammals that catalyzes the last two steps in human purine catabolism to produce uric acid. The enzyme exists as a homodimer with independent electron transfer in each monomer. This has been studied extensively as a major constituent of the milk fat globule membrane (MFGM) which surrounds fat globules in cow's milk even though purine catabolism is the most accepted function of XOR. A huge number of literature highlights on the different catalytic forms of XOR and their importance in the generation of reactive oxygen species/reactive nitrogen species (ROS/RNS) and synthesis of uric acid which are involved in many physiological and pathological processes. However, a slight ambiguity resides in their biochemical functions. The aim of this article was to review the literature published on the structural, catalytical, physiological and pathological role of XOR and to resolve the ambiguity in biochemical processes and to firm up various natural inhibitors of XOR collectively. Uric acid, the product of purine catabolism shows antioxidant activity, and XOR-derived ROS and RNS play a role in innate immunity, milk secretion and also be involved in signaling and metabolism of xenobiotics. Furthermore, XOR is likely to be engaged in pathology because of excessive production of uric acid and ROS/RNS. This review also reports natural XOR inhibitors in plants which inhibit the enzyme to treat XOR associated pathology.</p>

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22

Giesecke, D., S. Gaebler, and M. Stangassinger. "Quantification and kinetics of purine catabolism in Dalmatian dogs at low and high purine intakes." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 92, no. 4 (January 1989): 631–36. http://dx.doi.org/10.1016/0305-0491(89)90242-3.

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23

Tullson, P. C., D. M. Whitlock, and R. L. Terjung. "Adenine nucleotide degradation in slow-twitch red muscle." American Journal of Physiology-Cell Physiology 258, no. 2 (February 1, 1990): C258—C265. http://dx.doi.org/10.1152/ajpcell.1990.258.2.c258.

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The catabolism of adenine nucleotides (AdN) in rat soleus muscle (predominantly slow twitch) is very different from that in fast-twitch muscle. AMP deaminase is highly inhibited during brief (3 min) intense (120 tetani/min) in situ stimulation, resulting in little inosine 5'-monophosphate (IMP) accumulation (0.21 mumol/g). Even with ligation of the femoral artery during the same brief intense contraction conditions there is surprisingly little increase in IMP (0.37 mumol/g), although AdN depletion is evident (-1.30 mumol/g). We have tested the hypothesis that accumulation of purine nucleosides and bases accounts for the AdN depletion by measuring purine degradation products using high-performance liquid chromatography. There was no stoichiometric accumulation of purine degradation products to account for the observed AdN depletion even though metabolite recovery was essentially quantitative. We hypothesis that under these conditions AdN are converted to a form different from purine nucleoside and base degradation products. In contrast to the inhibition of AMP deamination seen during brief ischemia, slow-twitch muscle depletes a substantial fraction (28%) of muscle AdN (1.75 mumol/g) that can be accounted for stoichiometrically as purine degradation products during an extended 10-min ischemic period of mild (12 tetani/min) contraction conditions. IMP accumulation (1 mumol/g) is most prominent with inosine, accounting for 23% (0.4 mumol/g) of the depleted AdN, showing that slow-twitch red muscle is capable of both AMP deamination and the subsequent production of purine nucleosides during an extended period of ischemic contractions. The present results indicate that AdN metabolism in the soleus muscle is complex, yielding expected degradation products or a loss of total purines, depending on contraction conditions.(ABSTRACT TRUNCATED AT 250 WORDS)

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24

Achterberg, P. W., A. S. Nieukoop, B. Schoutsen, and J. W. de Jong. "Different ATP-catabolism in reperfused adult and newborn rat hearts." American Journal of Physiology-Heart and Circulatory Physiology 254, no. 6 (June 1, 1988): H1091—H1098. http://dx.doi.org/10.1152/ajpheart.1988.254.6.h1091.

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Age-dependent differences in the effects of ischemia and reperfusion on ATP breakdown were studied in perfused adult and newborn (10 days old) rat hearts. No-flow ischemia (15 min at 37, 30, or 23 degrees C) was applied and reperfusion (20 min at 37 degrees C) was studied after ischemia at 23 or 37 degrees C. Hypothermia during ischemia protected both age groups to a similar degree against ATP decline, which was linear with temperature. Reperfusion after normothermic ischemia resulted in higher ATP levels in newborn hearts with less release of ATP catabolites (purines). We found no age-related differences in lactate release but large differences in purine release. During normoxia, adult hearts released mainly urate (80% of total) and inosine (7%), but newborns released hypoxanthine (64%) and inosine (15%). Early during reperfusion adult hearts released inosine (58%) and adenosine (18%), but newborns released inosine (53%) and hypoxanthine (38%). These data suggested a lower activity of the potentially deleterious enzyme xanthine oxidoreductase in newborn hearts, which was confirmed by enzymatic assay. ATP-catabolite release during reperfusion was less in newborn than adult hearts, and this coincided with lower xanthine oxidase activity.

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25

LIU, Chang, Jian-kai LIU, Mu-jie KAN, Lin GAO, Hai-ying FU, Hang ZHOU, and Min HONG. "Morphine enhances purine nucleotide catabolism in vivo and in vitro." Acta Pharmacologica Sinica 28, no. 8 (August 2007): 1105–15. http://dx.doi.org/10.1111/j.1745-7254.2007.00592.x.

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26

Cohen, Amos, and Jerzy Barankiewicz. "PURINE NUCLEOTIDE AND DEOXYNUCLEOTIDE CATABOLISM IN HUMAN T LYMPHOCYTES: 36." Pediatric Research 19, no. 7 (July 1985): 749. http://dx.doi.org/10.1203/00006450-198507000-00056.

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27

Ramazzina, Ileana, Roberto Costa, Laura Cendron, Rodolfo Berni, Alessio Peracchi, Giuseppe Zanotti, and Riccardo Percudani. "An aminotransferase branch point connects purine catabolism to amino acid recycling." Nature Chemical Biology 6, no. 11 (September 19, 2010): 801–6. http://dx.doi.org/10.1038/nchembio.445.

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28

Schopf, Gerhard, Michael Havel, Roland Fasol, and Mathias M. Mtlller. "ENZYME ACTIVITIES OF PURINE CATABOLISM AND SALVAGE IN HUMAN MUSCLE: 184." Pediatric Research 19, no. 7 (July 1985): 774. http://dx.doi.org/10.1203/00006450-198507000-00204.

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29

Ashihara, Hiroshi, Hiroshi Sano, and Alan Crozier. "Caffeine and related purine alkaloids: Biosynthesis, catabolism, function and genetic engineering." Phytochemistry 69, no. 4 (February 2008): 841–56. http://dx.doi.org/10.1016/j.phytochem.2007.10.029.

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30

Yao, Jeffrey, George Dougherty, Matcheri Keshavan, Debra Montrose, Wayne Matson, Steve Rozen, Joseph McEvoy, Rima Kaddurah-Daouk, and Ravinder Reddy. "ABNORMAL PURINE CATABOLISM IN FIRST-EPISODE NEUROLEPTIC-NAÏVE PATIENTS WITH SCHIZOPHRENIA." Schizophrenia Research 102, no. 1-3 (June 2008): 209–10. http://dx.doi.org/10.1016/s0920-9964(08)70633-9.

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31

Rodilla, Francisco, Maria Jose Sanchez-Beltran, Roberto Izquierdo, Maria Dolores Gomez-Ruiz, and Jose Cabo. "Inhibition of purine catabolism by benzbromarone in isolated rat liver cells." Biochemical Pharmacology 37, no. 19 (October 1988): 3561–63. http://dx.doi.org/10.1016/0006-2952(88)90385-1.

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32

Villalobos-García, Daniel, and Rolando Hernández-Muñoz. "Catalase increases ethanol oxidation through the purine catabolism in rat liver." Biochemical Pharmacology 137 (August 2017): 107–12. http://dx.doi.org/10.1016/j.bcp.2017.05.011.

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33

Garcia-Gil, Mercedes, Marcella Camici, Simone Allegrini, Rossana Pesi, Edoardo Petrotto, and Maria Tozzi. "Emerging Role of Purine Metabolizing Enzymes in Brain Function and Tumors." International Journal of Molecular Sciences 19, no. 11 (November 14, 2018): 3598. http://dx.doi.org/10.3390/ijms19113598.

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The growing evidence of the involvement of purine compounds in signaling, of nucleotide imbalance in tumorigenesis, the discovery of purinosome and its regulation, cast new light on purine metabolism, indicating that well known biochemical pathways may still surprise. Adenosine deaminase is important not only to preserve functionality of immune system but also to ensure a correct development and function of central nervous system, probably because its activity regulates the extracellular concentration of adenosine and therefore its function in brain. A lot of work has been done on extracellular 5′-nucleotidase and its involvement in the purinergic signaling, but also intracellular nucleotidases, which regulate the purine nucleotide homeostasis, play unexpected roles, not only in tumorigenesis but also in brain function. Hypoxanthine guanine phosphoribosyl transferase (HPRT) appears to have a role in the purinosome formation and, therefore, in the regulation of purine synthesis rate during cell cycle with implications in brain development and tumors. The final product of purine catabolism, uric acid, also plays a recently highlighted novel role. In this review, we discuss the molecular mechanisms underlying the pathological manifestations of purine dysmetabolisms, focusing on the newly described/hypothesized roles of cytosolic 5′-nucleotidase II, adenosine kinase, adenosine deaminase, HPRT, and xanthine oxidase.

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34

Beier, Lars, Per Nygaard, Hanne Jarmer, and Hans H. Saxild. "Transcription Analysis of the Bacillus subtilis PucR Regulon and Identification of a cis-Acting Sequence Required for PucR-Regulated Expression of Genes Involved in Purine Catabolism." Journal of Bacteriology 184, no. 12 (June 15, 2002): 3232–41. http://dx.doi.org/10.1128/jb.184.12.3232-3241.2002.

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ABSTRACT The PucR protein of Bacillus subtilis has previously been suggested to regulate the expression of 15 genes, pucABCDE, pucFG, pucH, pucI, pucJKLM, pucR, and gde, all of which encode proteins involved in purine catabolism. When cells are grown under nitrogen-limiting conditions, the expression of these genes is induced and intermediary compounds of the purine catabolic pathway affect this expression. By using pucR deletion mutants, we have found that PucR induces the expression of pucFG, pucH, pucI, pucJKLM, and gde while it represses the expression of pucR and pucABCDE. Deletions in the promoters of the five induced operons and genes combined with bioinformatic analysis suggested a conserved upstream activating sequence, 5′-WWWCNTTGGTTAA-3′, now named the PucR box. Potential PucR boxes overlapping the −35 and −10 regions of the pucABCDE promoter and located downstream of the pucR transcription start point were also found. The positions of these PucR boxes are consistent with PucR acting as a negative regulator of pucABCDE and pucR expression. Site-directed mutations in the PucR box upstream of pucH and pucI identified positions that are essential for the induction of pucH and pucI expression, respectively. Mutants with decreased pucH or increased pucR expression obtained from a library of clones containing random mutations in the pucH-to-pucR intercistronic region all contained mutations in or near the PucR box. The induction of pucR expression under nitrogen-limiting conditions was found to be mediated by the global nitrogen-regulatory protein TnrA. In other gram-positive bacteria, we have found open reading frames that encode proteins similar to PucR located next to other open reading frames encoding proteins with similarity to purine catabolic enzymes. Hence, the PucR homologues are likely to exert the same function in other gram-positive bacteria as PucR does in B. subtilis.

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Volek, Jeff S., William J. Kraemer, Martyn R. Rubin, Ana L. Gómez, Nicholas A. Ratamess, and Paula Gaynor. "l-Carnitinel-tartrate supplementation favorably affects markers of recovery from exercise stress." American Journal of Physiology-Endocrinology and Metabolism 282, no. 2 (February 1, 2002): E474—E482. http://dx.doi.org/10.1152/ajpendo.00277.2001.

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We examined the influence ofl-carnitine l-tartrate (LCLT) on markers of purine catabolism, free radical formation, and muscle tissue disruption after squat exercise. With the use of a balanced, crossover design (1 wk washout), 10 resistance-trained men consumed a placebo or LCLT supplement (2 g l-carnitine/day) for 3 wk before obtaining blood samples on six consecutive days (D1 to D6). Blood was also sampled before and after a squat protocol (5 sets, 15–20 repetitions) on D2. Muscle tissue disruption at the midthigh was assessed using magnetic resonance imaging (MRI) before exercise and on D3 and D6. Exercise-induced increases in plasma markers of purine catabolism (hypoxanthine, xanthine oxidase, and serum uric acid) and circulating cytosolic proteins (myoglobin, fatty acid-binding protein, and creatine kinase) were significantly ( P ≤ 0.05) attenuated by LCLT. Exercise-induced increases in plasma malondialdehyde returned to resting values sooner during LCLT compared with placebo. The amount of muscle disruption from MRI scans during LCLT was 41–45% of the placebo area. These data indicate that LCLT supplementation is effective in assisting recovery from high-repetition squat exercise.

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Tomczyk, Marta, Talita Glaser, Ewa M. Slominska, Henning Ulrich, and Ryszard T. Smolenski. "Purine Nucleotides Metabolism and Signaling in Huntington’s Disease: Search for a Target for Novel Therapies." International Journal of Molecular Sciences 22, no. 12 (June 18, 2021): 6545. http://dx.doi.org/10.3390/ijms22126545.

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Huntington’s disease (HD) is a multi-system disorder that is caused by expanded CAG repeats within the exon-1 of the huntingtin (HTT) gene that translate to the polyglutamine stretch in the HTT protein. HTT interacts with the proteins involved in gene transcription, endocytosis, and metabolism. HTT may also directly or indirectly affect purine metabolism and signaling. We aimed to review existing data and discuss the modulation of the purinergic system as a new therapeutic target in HD. Impaired intracellular nucleotide metabolism in the HD affected system (CNS, skeletal muscle and heart) may lead to extracellular accumulation of purine metabolites, its unusual catabolism, and modulation of purinergic signaling. The mechanisms of observed changes might be different in affected systems. Based on collected findings, compounds leading to purine and ATP pool reconstruction as well as purinergic receptor activity modulators, i.e., P2X7 receptor antagonists, may be applied for HD treatment.

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Terzuoli, Lucia, Brunetta Porcelli, Fabio Ponticelli, and Enrico Marinello. "Purine Nucleotide Catabolism in Rat Liver. Certain Preliminary Aspects of Uricase Reaction." Nucleosides, Nucleotides and Nucleic Acids 28, no. 3 (April 28, 2009): 193–203. http://dx.doi.org/10.1080/15257770902865381.

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Montalbini, P. "Effect of rust infection on purine catabolism enzyme levels in wheat leaves." Physiological and Molecular Plant Pathology 46, no. 4 (April 1995): 275–92. http://dx.doi.org/10.1006/pmpp.1995.1022.

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Ashihara, H., A. M. Monteiro, T. Moritz, F. M. Gillies, and A. Crozier. "Catabolism of caffeine and related purine alkaloids in leaves ofCoffea arabica L." Planta 198, no. 3 (1996): 334–39. http://dx.doi.org/10.1007/bf00620048.

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Suganuma, Tamaki. "Beyond Moco Biosynthesis―Moonlighting Roles of MoaE and MOCS2." Molecules 27, no. 12 (June 10, 2022): 3733. http://dx.doi.org/10.3390/molecules27123733.

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Molybdenum cofactor (Moco) biosynthesis requires iron, copper, and ATP. The Moco-containing enzyme sulfite oxidase catalyzes terminal oxidation in oxidative cysteine catabolism, and another Moco-containing enzyme, xanthine dehydrogenase, functions in purine catabolism. Thus, molybdenum enzymes participate in metabolic pathways that are essential for cellular detoxication and energy dynamics. Studies of the Moco biosynthetic enzymes MoaE (in the Ada2a-containing (ATAC) histone acetyltransferase complex) and MOCS2 have revealed that Moco biosynthesis and molybdenum enzymes align to regulate signaling and metabolism via control of transcription and translation. Disruption of these functions is involved in the onset of dementia and neurodegenerative disease. This review provides an overview of the roles of MoaE and MOCS2 in normal cellular processes and neurodegenerative disease, as well as directions for future research.

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Skachkov, Dmitry, Vladimir Konvay, Mikhail Zabolotnykh, and Ekaterina Kornienko. "Disclosure of the Mechanisms of Metabolic Disorders in Highly Productive Cows as a Way to Improve Milk Production Technology." BIO Web of Conferences 37 (2021): 00174. http://dx.doi.org/10.1051/bioconf/20213700174.

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The aim of this study was to study the molecular mechanisms of metabolic disorders that develop in highly productive cows. It was found that in the blood serum of animals with subclinical ketosis (SCK), which are in the eighth month of pregnancy, the concentration of β-hydroxybutyrate is increased, the content of iron, calcium and phosphorus is reduced, its iron-binding capacity against the background of the absence of phenomena of hepatocellular insufficiency, violation of the integrity of hepatocytes, hypoplastic anemia. The aggravation of ketoacidosis in fresh cows with rumen acidosis is facilitated by the development of carbohydrate deficiency in them, due to their increased oxidation in the reactions of anaerobic glycolysis, accompanied by excessive catabolism of purine mononucleotides to uric acid. Excessive lipid peroxidation of membrane structures under conditions of increased catabolism of purine nucleotides, along with the accumulation of acylglycerols in the liver caused by cobalamin deficiency, leads to the development of syndromes of impaired hepatocyte integrity and hepatocellular insufficiency. A decrease in the liver's ability to store iron ions and synthesize proteins that provide an increase in the iron-binding capacity of blood plasma in conditions of cobalamin deficiency contributes to the development of hypoplastic anemia not only in cows, but also in calves born from them.

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Ji, Peng, Eric B Nonnecke, Nicole Doan, Bo Lönnerdal, and Bie Tan. "Excess Iron Enhances Purine Catabolism Through Activation of Xanthine Oxidase and Impairs Myelination in the Hippocampus of Nursing Piglets." Journal of Nutrition 149, no. 11 (August 2, 2019): 1911–19. http://dx.doi.org/10.1093/jn/nxz166.

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Abstract Background Few studies have addressed the risk of nutritional iron overexposure in infancy. We previously found that excess dietary iron in nursing piglets resulted in iron overload in the liver and hippocampus and diminished socialization with novel conspecifics in a test for social novelty preference. Objectives This experiment aimed to identify metabolites and metabolic pathways affected by iron overload in the liver and hippocampus of nursing piglets. Methods Liver and hippocampal tissues collected from 22-d-old piglets (Hampshire × Yorkshire crossbreed; 5.28 ± 0.53 kg body weight; 50% male) that received orally 0 (NI group) or 50 mg iron/(d · kg body weight) (HI group) from postnatal day (PD) 2 to PD21 were analyzed for mRNA and protein expression and enzyme activity of xanthine oxidase (XO). Untargeted metabolomics was performed using GC-MS. Expression of myelin basic protein (MBP) in the hippocampus was determined using western blot. Results There were 108 and 126 metabolites identified in the hippocampus and liver, respectively. Compared with NI, HI altered 15 metabolites (P < 0.05, q < 0.2) in the hippocampus, including a reduction in myo-inositol (0.86-fold) and N-acetylaspartic acid (0.84-fold), 2 metabolites important for neuronal function and myelination. Seven metabolites involved in purine and pyrimidine metabolism (e.g., hypoxanthine, xanthine, and β-alanine) were coordinately changed in the hippocampus (P < 0.05, q < 0.2), suggesting that iron excess enhanced purine catabolism. The mRNA expression (2.3-fold) (P < 0.05) and activity of XO, a rate-limiting enzyme in purine degradation, was increased. Excess iron increased hippocampal lipid peroxidation by 74% (P < 0.05) and decreased MBP by 44% (P = 0.053). The hepatic metabolome was unaffected. Conclusions In nursing piglets, excess iron enhances hippocampal purine degradation through activation of XO, which may induce oxidative stress and alter energy metabolism in the developing brain.

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Sakaguchi, Yoshihiko, Tetsuya Hayashi, Yumiko Yamamoto, Keisuke Nakayama, Kai Zhang, Shaobo Ma, Hideyuki Arimitsu, and Keiji Oguma. "Molecular Analysis of an Extrachromosomal Element Containing the C2 Toxin Gene Discovered in Clostridium botulinum Type C." Journal of Bacteriology 191, no. 10 (March 6, 2009): 3282–91. http://dx.doi.org/10.1128/jb.01797-08.

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ABSTRACT Clostridium botulinum cultures are classified into seven types, types A to G, based on the antigenicity of the neurotoxins produced. Of these seven types, only types C and D produce C2 toxin in addition to the neurotoxin. The C2 toxin consists of two components designated C2I and C2II. The genes encoding the C2 toxin components have been cloned, and it has been stated that they might be on the cell chromosome. The present study confirmed by using pulsed-field gel electrophoresis and subsequent Southern hybridization that these genes are on a large plasmid. The complete nucleotide sequence of this plasmid was determined by using a combination of inverse PCR and primer walking. The sequence was 106,981 bp long and contained 123 potential open reading frames, including the c2I and c2II genes. The 57 products of these open reading frames had sequences similar to those of well-known proteins. It was speculated that 9 these 57 gene products were related to DNA replication, 2 were responsible for the two-component regulatory system, and 3 were σ factors. In addition, a total of 20 genes encoding proteins related to diverse processes in purine catabolism were found in two regions. In these regions, there were 9 and 11 genes rarely found in plasmids, indicating that this plasmid plays an important role in purine catabolism, as well as in C2 toxin production.

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Marutyan, Seda V., Gayane H. Petrosyan, Syuzan A. Marutyan, Liparit A. Navasardyan, and Armen H. Trchounian. "INFLUENCE OF X-RAY AND MICROWAVE RADIATION ON DEAMINATION OF PURINE NUCLEOTIDES IN YEAST CELLS CANDIDA GUILLIERMONDII NP-4." IZVESTIYA VYSSHIKH UCHEBNYKH ZAVEDENII KHIMIYA KHIMICHESKAYA TEKHNOLOGIYA 62, no. 2 (February 7, 2019): 48–52. http://dx.doi.org/10.6060/ivkkt.20196202.5894.

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In metabolism of living cells a key role play purine nucleotides which cells can be supplied either by de novo synthesis from lower molecular weight precursors, or by alternate ways of nucleotide synthesis or so-called "nucleotide salvage pathways", which allow reusing of intermediate products of nucleotide metabolism in nucleotide synthesis. This way is important in the post-stress repair period, saving energy and substrates in the repairing cells. Purine nucleotides are allosteric inhibitors of enzymes of nucleotide salvage pathways, therefore the increase in their catabolism leads to a decrease of their amount in the cells, which contributes to the intensive work of the nucleotide salvage pathways and provides substrates for DNA synthesis. Investigation of deamination of purine nucleotides in yeasts Candida guilliermondii NP-4 irradiated with X-rays, millimeter and decimeter electromagnetic waves, as well as after post-radiation incubation of cells has been realized. It has been shown that under the influence of X-ray and microwave irradiation in yeasts, the intensity of deamination of purine nucleotide-polyphosphates - ADP, ATP, GDF and GTP, has changed, which in all probability is an adaptive mechanism in the repair of yeasts after irradiation, provides the work of nucleotide salvage pathways, and can be associated with the metabolism of these compounds.

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Jenuth, Jack P., Ellen R. Mably, and Floyd F. Snyder. "Modelling of purine nucleoside metabolism during mouse embryonic development. Relative routes of adenosine, deoxyadenosine, and deoxyguanosine metabolism." Biochemistry and Cell Biology 74, no. 2 (March 1, 1996): 219–25. http://dx.doi.org/10.1139/o96-022.

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The individual activities for adenosine kinase, deoxyadenosine kinase, adenosine deaminase, deoxyguanosine kinase, and purine nucleoside phosphorylase were determined during days 7 to 13 of mouse embryonic development. Adenosine deaminase increased 74-fold between days 7 and 9; deoxyadenosine kinase increased 5.4-fold during the same interval. Adenosine kinase, deoxyguanosine kinase, and purine nucleoside phosphorylase exhibited less than 2-fold changes in activity between days 7 and 13. Using Michaelis constants for each enzyme and the maximal velocities determined from enzyme assay, the relative routes of adenosine and deoxyadenosine metabolism via phosphorylation or deamination were modeled as a function of nucleoside concentration for days 7 through 13. For days 7 and 8, phosphorylation of adenosine is the principle route of metabolism at physiological concentrations. A switch occurred at day 9 and following where deamination is at least 5-fold greater than phosphorylation at all substrate concentrations. Deoxyadenosine phosphorylation was at most 10% of deamination at day 7 and then declined to less than 1% for days 9 to 13. Phosphorolysis was the principle route of deoxyguanosine metabolism through the 7 to 13 day period. Thus catabolism rather than phosphorylation was the principle pathway for purine deoxynucleoside metabolism during this period.Key words: mouse embryo, purine nucleoside metabolism.

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Shatova, O. P., Eu V. Butenko, Eu V. Khomutov, D. S. Kaplun, I. Eu Sedakov, and I. I. Zinkovych. "Metformin impact on purine metabolism in breast cancer." Biomeditsinskaya Khimiya 62, no. 3 (2016): 302–5. http://dx.doi.org/10.18097/pbmc20166203302.

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Large-scale epidemiological and clinical studies have demonstrated the efficacy of metformin in oncology practice. However, the mechanisms of implementation of the anti-tumor effect of this drug there is still need understanding. In this study we have investigated the effect of metformin on the activity of adenosine deaminase and respectively adenosinergic immunosuppression in tumors and their microenvironment. The material of the study was taken during surgery of breast cacer patients receiveing metformin, and also patients which did not take this drug. The adenosine deaminase activity and substrate (adenosine) and products (inosine, hypoxanthine) concentrations were determined by HPLC. Results of this study suggest that metformin significantly alters catabolism of purine nucleotides in the node breast adenocarcinoma tisue. However, the metformin-induced increase in the adenosine deaminase activity is not sufficient to reduce the level of adenosine in cancer tissue. Thus, in metformin treated patients the adenosine concentration remained unchanged, and inosine and hypoxanthine concentration significantly increased.

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Yao, Jeffrey K., George G. Dougherty, Ravinder D. Reddy, Matcheri S. Keshavan, Debra M. Montrose, Wayne R. Matson, Joseph McEvoy, and Rima Kaddurah-Daouk. "Homeostatic Imbalance of Purine Catabolism in First-Episode Neuroleptic-Naïve Patients with Schizophrenia." PLoS ONE 5, no. 3 (March 3, 2010): e9508. http://dx.doi.org/10.1371/journal.pone.0009508.

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Close, Dan M., Connor J. Cooper, Xingyou Wang, Payal Chirania, Madhulika Gupta, John R. Ossyra, Richard J. Giannone, et al. "Horizontal transfer of a pathway for coumarate catabolism unexpectedly inhibits purine nucleotide biosynthesis." Molecular Microbiology 112, no. 6 (October 2019): 1784–97. http://dx.doi.org/10.1111/mmi.14393.

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Möllhoff, T., S. Sukehiro, M. Hendrickx, H. Van Belle, and W. Flameng. "Effects of Hypothermic Ischemia on Purine Catabolism in Canine, Primate, and Human Myocardium." Thoracic and Cardiovascular Surgeon 39, no. 04 (August 1991): 187–92. http://dx.doi.org/10.1055/s-2007-1022706.

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Kather, H. "Beta-adrenergic stimulation of adenine nucleotide catabolism and purine release in human adipocytes." Journal of Clinical Investigation 85, no. 1 (January 1, 1990): 106–14. http://dx.doi.org/10.1172/jci114399.

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