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Journal articles on the topic 'Alpha-ketoglutarate'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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1

Le Boucher, Jacques, Biol Eng, Colette Coudray-Lucas, et al. "Enteral administration of ornithine alpha-ketoglutarate or arginine alpha-ketoglutarate." Critical Care Medicine 25, no. 2 (1997): 293–98. http://dx.doi.org/10.1097/00003246-199702000-00017.

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2

Hou, Yongqing. "Alpha-Ketoglutarate and intestinal function." Frontiers in Bioscience 16, no. 1 (2011): 1186. http://dx.doi.org/10.2741/3783.

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3

REX SHEU, KWAN-FU, and JOHN P. BLASS. "The alpha-Ketoglutarate Dehydrogenase Complex." Annals of the New York Academy of Sciences 893, no. 1 OXIDATIVE/ENE (1999): 61–78. http://dx.doi.org/10.1111/j.1749-6632.1999.tb07818.x.

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4

Gougoux, A., P. Vinay, and M. Duplain. "Maleate-induced stimulation of glutamine metabolism in the intact dog kidney." American Journal of Physiology-Renal Physiology 248, no. 4 (1985): F585—F593. http://dx.doi.org/10.1152/ajprenal.1985.248.4.f585.

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Studies were performed in anesthetized normal dogs to evaluate the effects of maleate on renal metabolism. Intravenous administration of maleate (50 mg/kg) markedly increased urinary excretion of glutamine, glutamate, alpha-ketoglutarate, alanine, lactate, pyruvate, and citrate. Despite a fourfold rise in renal cortical concentration of alpha-ketoglutarate, glutamine utilization expressed per 100 ml glomerular filtration rate almost doubled following maleate administration, whereas total ammonia production increased threefold, most of this ammonia being diverted into the renal vein. The renal

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5

Wu, Nan, Mingyao Yang, Uma Gaur, Huailiang Xu, Yongfang Yao, and Diyan Li. "Alpha-Ketoglutarate: Physiological Functions and Applications." Biomolecules & Therapeutics 24, no. 1 (2016): 1–8. http://dx.doi.org/10.4062/biomolther.2015.078.

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6

Tian, Qiyu, Xiangdong Liu, and Min Du. "Alpha-ketoglutarate for adipose tissue rejuvenation." Aging 12, no. 14 (2020): 13845–46. http://dx.doi.org/10.18632/aging.103853.

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7

Uzgare, Arti, Kavalukas Sandra, Qiang Zhang, Luc Cynober, and Adrian Barbul. "Ornithine alpha ketoglutarate enhances wound healing." Journal of the American College of Surgeons 209, no. 3 (2009): S72. http://dx.doi.org/10.1016/j.jamcollsurg.2009.06.174.

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8

Simpson, D. P., N. McSherry, E. Scarbrough, and K. Zweifel. "Substrate responses to acid-base alterations in dog renal proximal tubules." American Journal of Physiology-Renal Physiology 262, no. 6 (1992): F1039—F1046. http://dx.doi.org/10.1152/ajprenal.1992.262.6.f1039.

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Proximal tubules from dog kidney were incubated for 2-6 min with low concentrations of pyruvate, glutamine, and malate. When initial medium citrate was between 0 and 0.5 mM and alpha-ketoglutarate was between 0 and 0.1 mM, concentrations of these two substrates in tubules and media after incubation were lower with 10 than with 40 mM HCO3-. Malate levels in tubules and media changed in the opposite direction. CO2 formation from labeled citrate or alpha-ketoglutarate was greater at low than at high HCO3-. In tubules treated with digitonin to disrupt the cell membrane, differences in citrate and

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9

Cynober, L. "Metabolic interaction between ornithine and alpha-ketoglutarate as a basis for the action of ornithine alpha-ketoglutarate." Clinical Nutrition 12, no. 1 (1993): 54–56. http://dx.doi.org/10.1016/0261-5614(93)90150-3.

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10

Donati, L., M. Signorini, and S. Grappolini. "Ornithine alpha-ketoglutarate administration in burn injury." Clinical Nutrition 12, no. 1 (1993): 70–71. http://dx.doi.org/10.1016/0261-5614(93)90159-2.

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11

Chistyakova, E. Yu, S. V. Okovitiy, V. N. Yuskovec, D. S. Lisitskii, and A. B. Verveda. "Actoprotective Activity of Dimethylaminoethanol Compounds Combined with Intermediates of the Citric Acid Cycle." Journal Biomed 17, no. 2 (2021): 58–70. http://dx.doi.org/10.33647/2074-5982-17-2-58-70.

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The article presents the results of evaluation of actoprotective activity of combined dimethylaminoethanol compounds containing intermediates of the citric acid cycle (L-malate, α-ketoglutarate, succinate and fumarate). The effect of long-term intragastric administration of pharmacological agents for 4 weeks at a dose of 75 mg/kg on the static, dynamic endurance, motor coordination and body weight gain of “trained” laboratory animals was assessed in comparison with reference actoprotector ethylthiobenzimidazole (25 mg/kg, intragastrically). It was found that the most promising substances for f

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12

Trivedi, B., and R. L. Tannen. "Effect of respiratory acidosis on intracellular pH of the proximal tubule." American Journal of Physiology-Renal Physiology 250, no. 6 (1986): F1039—F1045. http://dx.doi.org/10.1152/ajprenal.1986.250.6.f1039.

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In contrast to chronic metabolic acidosis, chronic respiratory acidosis does not result in an adaptation in either renal ammonia or glucose production. To examine the possibility that this might be explained by a difference in proximal tubule intracellular pH, the response of two pH-sensitive metabolites, citrate and alpha-ketoglutarate, were assessed. Metabolic acidosis of 3 days duration, induced by drinking 1.5% NH4Cl, significantly reduced urinary citrate excretion (172 to 15 mumol/day) and renal cortical citrate (1.33 to 0.88 mumol/g) and alpha-ketoglutarate (0.90 to 0.46 mumol/g) concent

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13

Lylyk, M. P., M. M. Bayliak, H. V. Shmihel, J. M. Storey, K. B. Storey, and V. I. Lushchak. "Effects of alpha-ketoglutarate on lifespan and functional aging of Drosophila melanogaster flies." Ukrainian Biochemical Journal 90, no. 6 (2018): 49–61. http://dx.doi.org/10.15407/ubj90.06.049.

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14

Seol, W., and A. J. Shatkin. "Escherichia coli kgtP encodes an alpha-ketoglutarate transporter." Proceedings of the National Academy of Sciences 88, no. 9 (1991): 3802–6. http://dx.doi.org/10.1073/pnas.88.9.3802.

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15

Repetto, B., and A. Tzagoloff. "Structure and regulation of KGD1, the structural gene for yeast alpha-ketoglutarate dehydrogenase." Molecular and Cellular Biology 9, no. 6 (1989): 2695–705. http://dx.doi.org/10.1128/mcb.9.6.2695.

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Nuclear respiratory-defective mutants of Saccharomyces cerevisiae have been screened for lesions in the mitochondrial alpha-ketoglutarate dehydrogenase complex. Strains assigned to complementation group G70 were ascertained to be deficient in enzyme activity due to mutations in the KGD1 gene coding for the alpha-ketoglutarate dehydrogenase component of the complex. The KGD1 gene has been cloned by transformation of a representative kgd1 mutant, C225/U1, with a recombinant plasmid library of wild-type yeast nuclear DNA. Transformants containing the gene on a multicopy plasmid had three- to four

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16

Repetto, B., and A. Tzagoloff. "Structure and regulation of KGD1, the structural gene for yeast alpha-ketoglutarate dehydrogenase." Molecular and Cellular Biology 9, no. 6 (1989): 2695–705. http://dx.doi.org/10.1128/mcb.9.6.2695-2705.1989.

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Nuclear respiratory-defective mutants of Saccharomyces cerevisiae have been screened for lesions in the mitochondrial alpha-ketoglutarate dehydrogenase complex. Strains assigned to complementation group G70 were ascertained to be deficient in enzyme activity due to mutations in the KGD1 gene coding for the alpha-ketoglutarate dehydrogenase component of the complex. The KGD1 gene has been cloned by transformation of a representative kgd1 mutant, C225/U1, with a recombinant plasmid library of wild-type yeast nuclear DNA. Transformants containing the gene on a multicopy plasmid had three- to four

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17

Cynober, L., C. Coudray-Lucas, J. P. de Bandt, et al. "Action of ornithine alpha-ketoglutarate, ornithine hydrochloride, and calcium alpha-ketoglutarate on plasma amino acid and hormonal patterns in healthy subjects." Journal of the American College of Nutrition 9, no. 1 (1990): 2–12. http://dx.doi.org/10.1080/07315724.1990.10720343.

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18

Lewandowski, E. D., L. A. Damico, L. T. White, and X. Yu. "Cardiac responses to induced lactate oxidation: NMR analysis of metabolic equilibria." American Journal of Physiology-Heart and Circulatory Physiology 269, no. 1 (1995): H160—H168. http://dx.doi.org/10.1152/ajpheart.1995.269.1.h160.

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The role of lactate as a source of pyruvate oxidation in supporting cardiac work, energetics, and formation of oxidative metabolites was examined in normal myocardium. 13C- and 31P-nuclear magnetic resonance (NMR) spectra were acquired from isolated rabbit hearts supplied 2.5 mM [3-13C]lactate or [3-13C]pyruvate with or without stimulation of pyruvate dehydrogenase (PDH) by dichloroacetate (DCA). Similar workloads determined by rate-pressure products were noted with pyruvate (21,700 +/- 2,400; mean +/- SE) and lactate (18,970 +/- 1,510). Oxygen consumption was similar in all four groups with m

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19

He, Liuqin, Zhiqi Xu, Kang Yao, et al. "The Physiological Basis and Nutritional Function of Alpha-ketoglutarate." Current Protein & Peptide Science 16, no. 7 (2015): 576–81. http://dx.doi.org/10.2174/1389203716666150630140157.

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20

Bonnefont, Jean-Paul, Dominique Chretien, Pierre Rustin, et al. "Alpha-ketoglutarate dehydrogenase deficiency presenting as congenital lactic acidosis." Journal of Pediatrics 121, no. 2 (1992): 255–58. http://dx.doi.org/10.1016/s0022-3476(05)81199-0.

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21

Fukumori, F., and R. P. Hausinger. "Purification and characterization of 2,4-dichlorophenoxyacetate/alpha-ketoglutarate dioxygenase." Journal of Biological Chemistry 268, no. 32 (1993): 24311–17. http://dx.doi.org/10.1016/s0021-9258(20)80527-4.

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22

Kristensen, N. B., H. Jungvid, J. A. Fernandez, and S. G. Pierzynowski. "Absorption and metabolism of alpha-ketoglutarate in growing pigs." Journal of Animal Physiology and Animal Nutrition 86, no. 7-8 (2002): 239–45. http://dx.doi.org/10.1046/j.1439-0396.2002.00380.x.

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23

Liu, Shaojuan, Liuqin He, and Kang Yao. "The Antioxidative Function of Alpha-Ketoglutarate and Its Applications." BioMed Research International 2018 (2018): 1–6. http://dx.doi.org/10.1155/2018/3408467.

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Alpha-ketoglutarate (AKG) is a crucial intermediate of the Krebs cycle and plays a critical role in multiple metabolic processes in animals and humans. Of note, AKG contributes to the oxidation of nutrients (i.e., amino acids, glucose, fatty acids) and then provides energy for cell processes. As a precursor of glutamate and glutamine, AKG acts as an antioxidant agent as it directly reacts with hydrogen peroxide with formation of succinate, water, and carbon dioxide; meanwhile, it discharges plenty of ATP by oxidative decarboxylation. Recent studies also show that AKG has alleviative effect on

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24

Donati, L., M. Signorini, L. S. Weilemann, et al. "Nutritional effects of ornithine alpha ketoglutarate in burn patients." Clinical Nutrition 11 (January 1992): 25–26. http://dx.doi.org/10.1016/0261-5614(92)90157-l.

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25

Rhoads, Timothy W., and Rozalyn M. Anderson. "Alpha-Ketoglutarate, the Metabolite that Regulates Aging in Mice." Cell Metabolism 32, no. 3 (2020): 323–25. http://dx.doi.org/10.1016/j.cmet.2020.08.009.

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26

Yang, D., S. F. Previs, C. A. Fernandez, et al. "Noninvasive probing of citric acid cycle intermediates in primate liver with phenylacetylglutamine." American Journal of Physiology-Endocrinology and Metabolism 270, no. 5 (1996): E882—E889. http://dx.doi.org/10.1152/ajpendo.1996.270.5.e882.

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In human and primate liver, phenylacetate and glutamine form phenylacetylglutamine, which is excreted in urine. Probing noninvasively the labeling pattern of liver citric acid cycle intermediates with phenylacetylglutamine assumes that the labeling pattern of its glutamine moiety reflects that of liver alpha-ketoglutarate. To validate this probe, we infused monkeys with [U-13C3]lactate, [3-13C]lactate, [1, 2-13C2]acetate, [2-13C]acetate, [U-13C3]glycerol, or 2-[3-13C]ketoisocaproate and compared the labeling patterns of urinary phenylacetyl-glutamine with those of glutamate and glutamine in li

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27

Seol, Wongi, and Aaron J. Shatkin. "Site-directed mutants of Escherichia coli .alpha.-ketoglutarate permease (KgtP)." Biochemistry 31, no. 13 (1992): 3550–54. http://dx.doi.org/10.1021/bi00128a032.

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28

Der Garabedian, P. Arsene. "Candida .delta.-aminovalerate:.alpha.-ketoglutarate aminotransferase: purification and enzymologic properties." Biochemistry 25, no. 19 (1986): 5507–12. http://dx.doi.org/10.1021/bi00367a024.

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29

Omede, Ameh, Delvac Oceandy, Mamas Mamas, et al. "177 The Alpha-ketoglutarate Receptor GPR99 Regulates Pathological Cardiac Hypertrophy." Heart 100, Suppl 3 (2014): A100.1—A100. http://dx.doi.org/10.1136/heartjnl-2014-306118.177.

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30

Dabek, M., D. Kruszewska, R. Filip, et al. "alpha-Ketoglutarate (AKG) absorption from pig intestine and plasma pharmacokinetics." Journal of Animal Physiology and Animal Nutrition 89, no. 11-12 (2005): 419–26. http://dx.doi.org/10.1111/j.1439-0396.2005.00566.x.

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31

Riedel, Eberhard, Michael Nündel, and Hannelore Hampl. "α-Ketoglutarate Application in Hemodialysis Patients Improves Amino Acid Metabolism." Nephron 74, no. 2 (1996): 261–65. http://dx.doi.org/10.1159/000189319.

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32

Repetto, B., and A. Tzagoloff. "In vivo assembly of yeast mitochondrial alpha-ketoglutarate dehydrogenase complex." Molecular and Cellular Biology 11, no. 8 (1991): 3931–39. http://dx.doi.org/10.1128/mcb.11.8.3931.

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The assembly of alpha-ketoglutarate dehydrogenase complex (KGDC) has been studied in wild-type Saccharomyces cerevisiae and in respiratory-deficient strains (pet) with mutations in KGD1 and KGD2, the structural genes for alpha-ketoglutarate dehydrogenase (KE1) and dihydrolipoyl transsuccinylase (KE2) components, respectively. Mutants unable to express KE1 or KE2 form partial complexes similar to those reported in earlier studies on the resolution and reconstitution of bacterial and mammalian KGDC. Thus mutants lacking KE1 assemble a high-molecular-weight subcomplex consisting of a KE2 core par

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33

Tretter, Laszlo, and Vera Adam-Vizi. "Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress." Philosophical Transactions of the Royal Society B: Biological Sciences 360, no. 1464 (2005): 2335–45. http://dx.doi.org/10.1098/rstb.2005.1764.

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Alpha-ketoglutarate dehydrogenase (α-KGDH) is a highly regulated enzyme, which could determine the metabolic flux through the Krebs cycle. It catalyses the conversion of α-ketoglutarate to succinyl-CoA and produces NADH directly providing electrons for the respiratory chain. α-KGDH is sensitive to reactive oxygen species (ROS) and inhibition of this enzyme could be critical in the metabolic deficiency induced by oxidative stress. Aconitase in the Krebs cycle is more vulnerable than α-KGDH to ROS but as long as α-KGDH is functional NADH generation in the Krebs cycle is maintained. NADH supply t

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34

Rosenbeiger, P., M. R. Tatara, N. Sierant-Rożmiej, et al. "Antiosteopenic effect of alpha-ketoglutarate (AKG) administration in female turkeys." Bone 48 (May 2011): S225. http://dx.doi.org/10.1016/j.bone.2011.03.527.

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35

Xiao, Dingfu, Liming Zeng, Kang Yao, Xiangfeng Kong, Guoyao Wu, and Yulong Yin. "The glutamine-alpha-ketoglutarate (AKG) metabolism and its nutritional implications." Amino Acids 48, no. 9 (2016): 2067–80. http://dx.doi.org/10.1007/s00726-016-2254-8.

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36

Sultana, Shaheen, Sushma Talegaonkar, Dhruv Kumar Nishad, Gaurav Mittal, F. J. Ahmad, and Aseem Bhatnagar. "Alpha ketoglutarate nanoparticles: A potentially effective treatment for cyanide poisoning." European Journal of Pharmaceutics and Biopharmaceutics 126 (May 2018): 221–32. http://dx.doi.org/10.1016/j.ejpb.2017.06.017.

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37

Roth-Merten, A., J. Karner, S. Winkler, L. Valentini, K. Schaupp, and E. Roth. "Influence of alpha-ketoglutarate infusion on glutamate and glutamine metabolism." Clinical Nutrition 9, no. 1 (1990): 46–47. http://dx.doi.org/10.1016/0261-5614(90)90081-3.

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38

Xu, Feng, Jin Wang, and Guo-Ping Zhao. "Alpha-ketoglutarate protects Streptomyces coelicolor from visible light-induced phototoxicity." Biochemistry and Biophysics Reports 9 (March 2017): 22–28. http://dx.doi.org/10.1016/j.bbrep.2016.11.002.

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39

Repetto, B., and A. Tzagoloff. "In vivo assembly of yeast mitochondrial alpha-ketoglutarate dehydrogenase complex." Molecular and Cellular Biology 11, no. 8 (1991): 3931–39. http://dx.doi.org/10.1128/mcb.11.8.3931-3939.1991.

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The assembly of alpha-ketoglutarate dehydrogenase complex (KGDC) has been studied in wild-type Saccharomyces cerevisiae and in respiratory-deficient strains (pet) with mutations in KGD1 and KGD2, the structural genes for alpha-ketoglutarate dehydrogenase (KE1) and dihydrolipoyl transsuccinylase (KE2) components, respectively. Mutants unable to express KE1 or KE2 form partial complexes similar to those reported in earlier studies on the resolution and reconstitution of bacterial and mammalian KGDC. Thus mutants lacking KE1 assemble a high-molecular-weight subcomplex consisting of a KE2 core par

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40

Repetto, B., and A. Tzagoloff. "Structure and regulation of KGD2, the structural gene for yeast dihydrolipoyl transsuccinylase." Molecular and Cellular Biology 10, no. 8 (1990): 4221–32. http://dx.doi.org/10.1128/mcb.10.8.4221.

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Yeast mutants assigned to the pet complementation group G104 were found to lack alpha-ketoglutarate dehydrogenase activity as a result of mutations in the dihydrolipoyl transsuccinylase (KE2) component of the complex. The nuclear gene KGD2, coding for yeast KE2, was cloned by transformation of E250/U6, a G104 mutant, with a yeast genomic library. Analysis of the KGD2 sequence revealed an open reading frame encoding a protein with a molecular weight of 52,375 and 42% identities to the KE2 component of Escherichia coli alpha-ketoglutarate dehydrogenase complex. Disruption of the chromosomal copy

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41

Repetto, B., and A. Tzagoloff. "Structure and regulation of KGD2, the structural gene for yeast dihydrolipoyl transsuccinylase." Molecular and Cellular Biology 10, no. 8 (1990): 4221–32. http://dx.doi.org/10.1128/mcb.10.8.4221-4232.1990.

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Yeast mutants assigned to the pet complementation group G104 were found to lack alpha-ketoglutarate dehydrogenase activity as a result of mutations in the dihydrolipoyl transsuccinylase (KE2) component of the complex. The nuclear gene KGD2, coding for yeast KE2, was cloned by transformation of E250/U6, a G104 mutant, with a yeast genomic library. Analysis of the KGD2 sequence revealed an open reading frame encoding a protein with a molecular weight of 52,375 and 42% identities to the KE2 component of Escherichia coli alpha-ketoglutarate dehydrogenase complex. Disruption of the chromosomal copy

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42

Oh, H. Y., G. Z. Fadda, M. Smogorzewski, H. H. Liou, and S. G. Massry. "Phosphate depletion impairs leucine-induced insulin secretion." Journal of the American Society of Nephrology 5, no. 5 (1994): 1259–65. http://dx.doi.org/10.1681/asn.v551259.

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Phosphate depletion (PD) in vivo causes a sundry of abnormalities in pancreatic islets including a rise in cytosolic calcium, low ATP content, reduced Ca2+ ATPase and Na(+)-K+ ATPase activity, and impaired insulin secretion in response to glucose or potassium. L-Leucine is a strong secretagogue that triggers insulin secretion by deamination to alpha-ketoisocaproic acid (KIC) and the subsequent metabolism of the latter to ATP and by the activation of glutamate dehydrogenase (GLDH), which acts on glutamate to generate alpha-ketoglutarate, the metabolism of which results in ATP production. The ge

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43

Gleadle, Jonathan M., and Annette Mazzone. "Remote ischaemic preconditioning: closer to the mechanism?" F1000Research 5 (December 13, 2016): 2846. http://dx.doi.org/10.12688/f1000research.9633.1.

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Brief periods of ischaemia followed by reperfusion of one tissue such as skeletal muscle can confer subsequent protection against ischaemia-induced injury in other organs such as the heart. Substantial evidence of this effect has been accrued in experimental animal models. However, the translation of this phenomenon to its use as a therapy in ischaemic disease has been largely disappointing without clear evidence of benefit in humans. Recently, innovative experimental observations have suggested that remote ischaemic preconditioning (RIPC) may be largely mediated through hypoxic inhibition of

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44

Simpson, D. P. "Dissociation of acid-base effects on substrate accumulation and on delta pH in dog mitochondria." American Journal of Physiology-Renal Physiology 254, no. 6 (1988): F863—F870. http://dx.doi.org/10.1152/ajprenal.1988.254.6.f863.

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The relationship between the pH gradient (delta pH) and substrate accumulation was examined in mitochondria from dog renal cortex. Mitochondria were incubated in media containing bicarbonate or nonbicarbonate buffers. Mitochondrial delta pH was at equilibrium after 2 min incubation but citrate accumulation in the matrix space was still increasing. With nonbicarbonate buffer in rotenone-inhibited mitochondria, citrate and alpha-ketoglutarate concentrations in the matrix did not vary between pH 7.5 and 7.1; delta pH decreased from 0.62 to 0.52 as medium pH fell. With decreasing bicarbonate conce

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45

Weinberg, J. M., D. N. Buchanan, J. A. Davis, and M. Abarzua. "Metabolic aspects of protection by glycine against hypoxic injury to isolated proximal tubules." Journal of the American Society of Nephrology 1, no. 7 (1991): 949–58. http://dx.doi.org/10.1681/asn.v17949.

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To clarify the roles of butyrate and acylglycine formation in hypoxic proximal tubule cell injury and protection by glycine and to test the contribution of iodoacetate-suppressible metabolism to protection, (1) it was determined whether protection by glycine is fully expressed when glucose, lactate, alanine, and butyrate are replaced by alpha-ketoglutarate as the sole substrate for the tubules, (2) butyrate metabolism and acylglycine formation were directly measured in control and hypoxic preparations, and (3) it was assessed whether injury produced by iodoacetate, a potent inhibitor of glycol

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46

Ali, Rashid, Shaheen Sultana, Sarwat Sultana, Amit Kumar, Aseem Bhatnagar, and Gaurav Mittal. "Sub-Acute Inhalation Toxicity Study of Submicronic Alpha-Ketoglutarate Respiratory Formulation." Toxicology International (Formerly Indian Journal of Toxicology) 23, no. 2 (2016): 127. http://dx.doi.org/10.22506/ti/2016/v23/i2/146687.

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47

Shmihel, Halyna. "Alpha-Ketoglutarate Partially Protects Fruit Fly Drosophila Melanogaster from Ethanol Toxicity." Journal of Vasyl Stefanyk Precarpathian National University 2, no. 1 (2015): 115–21. http://dx.doi.org/10.15330/jpnu.2.1.115-121.

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Alpha-ketoglutarate (AKG) is an important intermediate in Krebs cycle and inmetabolism of amino acids. Recently, it was proposed to apply as a dietary supplement to improveoverall functional state of living organisms. In particular, AKG was supposed to use underexposure of animals and cell cultures to many toxic agents. In this context, this study aimed toelucidate the ability of dietary AKG to reduce toxic effects of ethanol on development of fruit flyDrosophila melanogaster, which is a popular model subject to research many aspects of biology ofhigher eukaryotes. For this aim, the effect of

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48

Lylyk, M. P., M. V. Golovchak, H. V. Shmihel, and M. M. Bayliak. "Influence of Alpha-Ketoglutarate on Drosophila melanogaster Resistance to Different Toxicants." Ukraïnsʹkij žurnal medicini, bìologìï ta sportu 2, no. 4 (2017): 180–84. http://dx.doi.org/10.26693/jmbs02.04.180.

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49

Tell, Grethe S., Livar Frøyland, Margaretha Haugen, et al. "Risk Assessment of "Other Substances" –L-arginine and Arginine Alpha-ketoglutarate." European Journal of Nutrition & Food Safety 9, no. 1 (2018): 33–35. http://dx.doi.org/10.9734/ejnfs/2019/45632.

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50

Zhang, Zhenzhen, Changjiu He, Lu Zhang, et al. "Alpha-ketoglutarate affects murine embryo development through metabolic and epigenetic modulations." Reproduction 158, no. 2 (2019): 125–35. http://dx.doi.org/10.1530/rep-19-0018.

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Abstract:

α-Ketoglutarate (α-KG) is an intermediary metabolite in the tricarboxylic acid (TCA) cycle and functions to inhibit ATPase and maintain the pluripotency of embryonic stem cells (ESCs); however, little is known regarding the effects of α-KG on the development of preimplantation embryos. Herein, we report that α-KG (150 μM) treatment significantly promoted the blastocyst rate, the number of inner cell mass (ICM) cells and foetal growth after embryo transfer. Mechanistic studies revealed two important pathways involved in the α-KG effects on embryo development. First, α-KG modulates mitochondria

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