Journal articles: 'Amino acid metabolism'

1

Chandel, Navdeep S. "Amino Acid Metabolism." Cold Spring Harbor Perspectives in Biology 13, no. 4 (April 2021): a040584. http://dx.doi.org/10.1101/cshperspect.a040584.

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KNOWLES, R. G. "Amino Acid Metabolism." Biochemical Society Transactions 14, no. 5 (October 1, 1986): 988–89. http://dx.doi.org/10.1042/bst0140988b.

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Broquist, Harry P. "Amino Acid Metabolism." Nutrition Reviews 34, no. 10 (April 27, 2009): 289–93. http://dx.doi.org/10.1111/j.1753-4887.1976.tb05672.x.

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Lee, Jeremy S. "Amino acid metabolism." Biochemical Education 14, no. 3 (July 1986): 148. http://dx.doi.org/10.1016/0307-4412(86)90187-1.

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Kasperek, George J. "Amino acid metabolism." National Strength & Conditioning Association Journal 10, no. 6 (1988): 23. http://dx.doi.org/10.1519/0744-0049(1988)010<0023:aam>2.3.co;2.

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Reggiani, R., and A. Bertani. "Anaerobic Amino Acid Metabolism." Russian Journal of Plant Physiology 50, no. 6 (November 2003): 733–36. http://dx.doi.org/10.1023/b:rupp.0000003270.33010.22.

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Hjelm, M., and J. Seakins. "Modelling amino acid metabolism." Amino Acids 3, no. 1 (1992): 1–23. http://dx.doi.org/10.1007/bf00806006.

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Muhammad, Nefertiti, Hyun Min Lee, and Jiyeon Kim. "Oncology Therapeutics Targeting the Metabolism of Amino Acids." Cells 9, no. 8 (August 15, 2020): 1904. http://dx.doi.org/10.3390/cells9081904.

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Amino acid metabolism promotes cancer cell proliferation and survival by supporting building block synthesis, producing reducing agents to mitigate oxidative stress, and generating immunosuppressive metabolites for immune evasion. Malignant cells rewire amino acid metabolism to maximize their access to nutrients. Amino acid transporter expression is upregulated to acquire amino acids from the extracellular environment. Under nutrient depleted conditions, macropinocytosis can be activated where proteins from the extracellular environment are engulfed and degraded into the constituent amino acids. The demand for non-essential amino acids (NEAAs) can be met through de novo synthesis pathways. Cancer cells can alter various signaling pathways to boost amino acid usage for the generation of nucleotides, reactive oxygen species (ROS) scavenging molecules, and oncometabolites. The importance of amino acid metabolism in cancer proliferation makes it a potential target for therapeutic intervention, including via small molecules and antibodies. In this review, we will delineate the targets related to amino acid metabolism and promising therapeutic approaches.

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S, Anwar. "Analysis of Arabidopsis amino acid metabolism in response to Heterodera schachtii infection." Pakistan Journal of Nematology 36, no. 2 (July 1, 2018): 131–50. http://dx.doi.org/10.18681/pjn.v36.i02.p131-150.

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Puran, M., L. Dorland, J. B. C. de Klerk, F. J. Van Sprang, and S. K. Wadman. "Disorders of Amino Acid Metabolism." Scandinavian Journal of Clinical and Laboratory Investigation 48 (1988): 75–77. http://dx.doi.org/10.3109/00365518809168514.

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Smith, Paul F. "AMINO ACID METABOLISM OF PPLO*." Annals of the New York Academy of Sciences 79, no. 10 (December 15, 2006): 543–50. http://dx.doi.org/10.1111/j.1749-6632.1960.tb42721.x.

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Puran, M., L. Dorland, J. B. C. de Klerk, F. J. Van Sprang, and S. K. Wadman. "Disorders of Amino Acid Metabolism." Scandinavian Journal of Clinical and Laboratory Investigation 48, sup190 (January 1988): 75–77. http://dx.doi.org/10.1080/00365518809168514.

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Fürst, P. "Amino acid metabolism in uremia." Journal of the American College of Nutrition 8, no. 4 (August 1989): 310–23. http://dx.doi.org/10.1080/07315724.1989.10720307.

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Walker, John, and John Barrett. "Parasite sulphur amino acid metabolism." International Journal for Parasitology 27, no. 8 (August 1997): 883–97. http://dx.doi.org/10.1016/s0020-7519(97)00039-8.

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Hanigan, Mark D., Brian J. Bequette, Les A. Crompton, and James France. "Modeling mammary amino acid metabolism." Livestock Production Science 70, no. 1-2 (July 2001): 63–78. http://dx.doi.org/10.1016/s0301-6226(01)00198-1.

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Neis, Evelien P. J. G., S. Sabrkhany, I. Hundscheid, D. Schellekens, K. Lenaerts, S. W. Olde Damink, E. E. Blaak, C. H. C. Dejong, and Sander S. Rensen. "Human splanchnic amino-acid metabolism." Amino Acids 49, no. 1 (October 6, 2016): 161–72. http://dx.doi.org/10.1007/s00726-016-2344-7.

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Kung, Limin, and Lyle M. Rode. "Amino acid metabolism in ruminants." Animal Feed Science and Technology 59, no. 1-3 (June 1996): 167–72. http://dx.doi.org/10.1016/0377-8401(95)00897-7.

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Yoo, Hee-Chan, and Jung-Min Han. "Amino Acid Metabolism in Cancer Drug Resistance." Cells 11, no. 1 (January 2, 2022): 140. http://dx.doi.org/10.3390/cells11010140.

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Despite the numerous investigations on resistance mechanisms, drug resistance in cancer therapies still limits favorable outcomes in cancer patients. The complexities of the inherent characteristics of tumors, such as tumor heterogeneity and the complicated interaction within the tumor microenvironment, still hinder efforts to overcome drug resistance in cancer cells, requiring innovative approaches. In this review, we describe recent studies offering evidence for the essential roles of amino acid metabolism in driving drug resistance in cancer cells. Amino acids support cancer cells in counteracting therapies by maintaining redox homeostasis, sustaining biosynthetic processes, regulating epigenetic modification, and providing metabolic intermediates for energy generation. In addition, amino acid metabolism impacts anticancer immune responses, creating an immunosuppressive or immunoeffective microenvironment. A comprehensive understanding of amino acid metabolism as it relates to therapeutic resistance mechanisms will improve anticancer therapeutic strategies.

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Krishnan, Aarti, and Dominique Soldati-Favre. "Amino Acid Metabolism in Apicomplexan Parasites." Metabolites 11, no. 2 (January 20, 2021): 61. http://dx.doi.org/10.3390/metabo11020061.

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Obligate intracellular pathogens have coevolved with their host, leading to clever strategies to access nutrients, to combat the host’s immune response, and to establish a safe niche for intracellular replication. The host, on the other hand, has also developed ways to restrict the replication of invaders by limiting access to nutrients required for pathogen survival. In this review, we describe the recent advancements in both computational methods and high-throughput –omics techniques that have been used to study and interrogate metabolic functions in the context of intracellular parasitism. Specifically, we cover the current knowledge on the presence of amino acid biosynthesis and uptake within the Apicomplexa phylum, focusing on human-infecting pathogens: Toxoplasma gondii and Plasmodium falciparum. Given the complex multi-host lifecycle of these pathogens, we hypothesize that amino acids are made, rather than acquired, depending on the host niche. We summarize the stage specificities of enzymes revealed through transcriptomics data, the relevance of amino acids for parasite pathogenesis in vivo, and the role of their transporters. Targeting one or more of these pathways may lead to a deeper understanding of the specific contributions of biosynthesis versus acquisition of amino acids and to design better intervention strategies against the apicomplexan parasites.

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Kazmierczak, Steven C. "Diseases of Metabolism (Disorders of Amino Acid Metabolism)." Analytical Chemistry 65, no. 12 (June 15, 1993): 401–4. http://dx.doi.org/10.1021/ac00060a606.

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Van Winkle, Lon J. "A Summary of Amino Acid Metabolism Based on Amino Acid Structure." Biochemical Education 13, no. 1 (January 1985): 25–26. http://dx.doi.org/10.1016/0307-4412(85)90123-2.

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22

Bender, David A. "The metabolism of “surplus” amino acids." British Journal of Nutrition 108, S2 (August 2012): S113—S121. http://dx.doi.org/10.1017/s0007114512002292.

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For an adult in N balance, apart from small amounts of amino acids required for the synthesis of neurotransmitters, hormones, etc, an amount of amino acids almost equal to that absorbed from the diet can be considered to be “surplus” in that it will be catabolized. The higher diet-induced thermogenesis from protein than from carbohydrate or fat has generally been assumed to be due to increased protein synthesis, which is ATP expensive. To this must be added the ATP cost of protein catabolism through the ubiquitin-proteasome pathway. Amino acid catabolism will add to thermogenesis. Deamination results in net ATP formation except when serine and threonine deaminases are used, but there is the energy cost of synthesizing glutamine in extra-hepatic tissues. The synthesis of urea has a net cost of only 1·5 × ATP when the ATP yield from fumarate metabolism is offset against the ATP cost of the urea cycle, but this offset is thermogenic. In fasting and on a low carbohydrate diet as much of the amino acid carbon as possible will be used for gluconeogenesis – an ATP-expensive, and hence thermogenic, process. Complete oxidation of most amino acid carbon skeletons also involves a number of thermogenic steps in which ATP (or GTP) or reduced coenzymes are utilized. There are no such thermogenic steps in the metabolism of pyruvate, acetyl CoA or acetoacetate, but for amino acids that are metabolized by way of the citric acid cycle intermediates there is thermogenesis ranging from 1 up to 7 × ATP equivalent per mol.

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Zhang, Hanyuan, Youxiu Zhu, Peng Xu, Zixia Zhao, Jianxin Feng, Biyin Wu, Yanliang Jiang, Chuanju Dong, and Jian Xu. "Multi-Omics Data Reveal Amino Acids Related Genes in the Common Carp Cyprinus carpio." Fishes 7, no. 5 (August 29, 2022): 225. http://dx.doi.org/10.3390/fishes7050225.

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Amino acids have important physiological effects on fish growth and development and are essential nutrition for humans. Flavor-related amino acids, such as glutamic acid and glycine, could have a significant effect on the taste of fish flesh. However, studies on the genetic mechanisms of amino acid metabolism in common carp (Cyprinus carpio) are still limited. This study identified divergent patterns on the genomic, transcriptomic and epigenomic levels in two groups of common carp with different amino acid contents. After genome-wide association analysis, a total of 62 genes was found to be associated with glycine, proline and tyrosine content. Transcriptome analysis of essential amino acids, branched-chain amino acids and flavor-related amino acids were performed using brain, liver and muscle tissues, resulting in 1643 differentially expressed genes (DEGs). Whole-genome bisulfite sequencing identified 3108 genes with differentially methylated promoters (DMPs). After the enrichment analysis, a series of pathways associated with amino acid metabolism, including growth regulation, lipid metabolism and the citrate cycle, was revealed. Integrated studies showed a strong correlation between DEGs and DMPs for amino acid contents in brain and muscle tissues. These multi-omics data revealed candidate genes and pathways related to amino acid metabolism in C. carpio.

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Heinemann, Björn, and Tatjana M. Hildebrandt. "The role of amino acid metabolism in signaling and metabolic adaptation to stress-induced energy deficiency in plants." Journal of Experimental Botany 72, no. 13 (May 16, 2021): 4634–45. http://dx.doi.org/10.1093/jxb/erab182.

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Abstract The adaptation of plant metabolism to stress-induced energy deficiency involves profound changes in amino acid metabolism. Anabolic reactions are suppressed, whereas respiratory pathways that use amino acids as alternative substrates are activated. This review highlights recent progress in unraveling the stress-induced amino acid oxidation pathways, their regulation, and the role of amino acids as signaling molecules. We present an updated map of the degradation pathways for lysine and the branched-chain amino acids. The regulation of amino acid metabolism during energy deprivation, including the coordinated induction of several catabolic pathways, is mediated by the balance between TOR and SnRK signaling. Recent findings indicate that some amino acids might act as nutrient signals in TOR activation and thus promote a shift from catabolic to anabolic pathways. The metabolism of the sulfur-containing amino acid cysteine is highly interconnected with TOR and SnRK signaling. Mechanistic details have recently been elucidated for cysteine signaling during the abscisic acid-dependent drought response. Local cysteine synthesis triggers abscisic acid production and, in addition, cysteine degradation produces the gaseous messenger hydrogen sulfide, which promotes stomatal closure via protein persulfidation. Amino acid signaling in plants is still an emerging topic with potential for fundamental discoveries.

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Graf, Anastasia, Lidia Trofimova, Alexander Ksenofontov, Lyudmila Baratova, and Victoria Bunik. "Hypoxic Adaptation of Mitochondrial Metabolism in Rat Cerebellum Decreases in Pregnancy." Cells 9, no. 1 (January 7, 2020): 139. http://dx.doi.org/10.3390/cells9010139.

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Function of brain amino acids as neurotransmitters or their precursors implies changes in the amino acid levels and/or metabolism in response to physiological and environmental challenges. Modelling such challenges by pregnancy and/or hypoxia, we characterize the amino acid pool in the rat cerebellum, quantifying the levels and correlations of 15 amino acids and activity of 2-oxoglutarate dehydrogenase complex (OGDHC). The parameters are systemic indicators of metabolism because OGDHC limits the flux through mitochondrial TCA cycle, where amino acids are degraded and their precursors synthesized. Compared to non-pregnant state, pregnancy increases the cerebellar content of glutamate and tryptophan, decreasing interdependence between the quantified components of amino acid metabolism. In response to hypoxia, the dependence of cerebellar amino acid pool on OGDHC and the average levels of arginine, glutamate, lysine, methionine, serine, phenylalanine, and tryptophan increase in non-pregnant rats only. This is accompanied by a higher hypoxic resistance of the non-pregnant vs. pregnant rats, pointing to adaptive significance of the hypoxia-induced changes in the cerebellar amino acid metabolism. These adaptive mechanisms are not effective in the pregnancy-changed metabolic network. Thus, the cerebellar amino acid levels and OGDHC activity provide sensitive markers of the physiology-dependent organization of metabolic network and its stress adaptations.

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Pogorelova, T. N., V. O. Gunko, V. V. Avrutskaya, L. V. Kaushanskaya, and O. A. Durnitsyna. "Impairments of placental amino acid metabolism in fetal growth restriction." Biomeditsinskaya Khimiya 63, no. 3 (2017): 266–71. http://dx.doi.org/10.18097/pbmc20176303266.

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The content of the amino acids in the placenta during physiological pregnancy and fetal growth restriction (FGR) has been investigated my means of the method of ion-exchange chromatography. It has been found that in FGR the placental amino acid pool is characterized by a decreased content of arginine, proline, alanine, serine, cysteine, methionine, tryptophan, leucine, threonine, tyrosine, phenylalanine, glutamine and an increased content of dicarboxylic amino acids, lysine, histidine and glycine. These changes are accompanied by altered activity of some enzymes of amino acid metabolism, and the degree of these changes correlates with the level of corresponding amino acids.

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Rivera, S., J. Azcón-Bieto, F. J. López-Soriano, M. Miralpeix, and J. M. Argilés. "Amino acid metabolism in tumour-bearing mice." Biochemical Journal 249, no. 2 (January 15, 1988): 443–49. http://dx.doi.org/10.1042/bj2490443.

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Mice bearing the Lewis lung carcinoma showed a high tumour glutaminase activity and significantly higher concentrations of most amino acids than in both the liver and the skeletal muscle of the host. Tumour tissue slices showed a marked preference for glutamine, especially for oxidation of its skeleton to CO2. It is proposed that the metabolism of this particular carcinoma is focused on amino acid degradation, glutamine being its preferred substrate.

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Layman, Donald K. "Role of Leucine in Protein Metabolism During Exercise and Recovery." Canadian Journal of Applied Physiology 27, no. 6 (December 1, 2002): 646–62. http://dx.doi.org/10.1139/h02-038.

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Exercise produces changes in protein and amino acid metabolism. These changes include degradation of the branched-chain amino acids, production of alanine and glutamine, and changes in protein turnover. One of the amino acid most affected by exercise is the branched-chain amino acid leucine. Recently, there has been an increased understanding of the role of leucine in metabolic regulations and remarkable new findings about the role of leucine in intracellular signaling. Leucine appears to exert a synergistic role with insulin as a regulatory factor in the insulin/phosphatidylinositol-3 kinase (PI3-K) signal cascade. Insulin serves to activate the signal pathway, while leucine is essential to enhance or amplify the signal for protein synthesis at the level of peptide initiation. Studies feeding amino acids or leucine soon after exercise suggest that post-exercise consumption of amino acids stimulates recovery of muscle protein synthesis via translation regulations. This review focuses on the unique roles of leucine in amino acid metabolism in skeletal muscle during and after exercise. Key words: branched-chain amino acids, insulin, protein synthesis, skeletal muscle

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Devignes, Claire-Sophie, Geert Carmeliet, and Steve Stegen. "Amino acid metabolism in skeletal cells." Bone Reports 17 (December 2022): 101620. http://dx.doi.org/10.1016/j.bonr.2022.101620.

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Pratelli, Réjane, and Guillaume Pilot. "Altered Amino Acid Metabolism inGlutamine Dumper1Plants." Plant Signaling & Behavior 2, no. 3 (May 2007): 182–84. http://dx.doi.org/10.4161/psb.2.3.3972.

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Tobias, Deirdre K., Samia Mora, Subodh Verma, and Patrick R. Lawler. "Altered branched chain amino acid metabolism." Current Opinion in Cardiology 33, no. 5 (September 2018): 558–64. http://dx.doi.org/10.1097/hco.0000000000000552.

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Watts, R. W. E. "Congenital Abnormalities of Amino-acid Metabolism." Developmental Medicine & Child Neurology 4, no. 4 (November 12, 2008): 405–17. http://dx.doi.org/10.1111/j.1469-8749.1962.tb03196.x.

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Devlin, J. T., I. Brodsky, A. Scrimgeour, S. Fuller, and D. M. Bier. "Amino acid metabolism after intense exercise." American Journal of Physiology-Endocrinology and Metabolism 258, no. 2 (February 1, 1990): E249—E255. http://dx.doi.org/10.1152/ajpendo.1990.258.2.e249.

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We studied postexercise amino acid metabolism, in the whole body and across the forearm. Seven volunteers were infused with L-[alpha-15N]lysine and L-[1-13C]-leucine twice [one time during 3 h after cycle exercise (75% VO2max), and one time in the resting state]. Whole body protein breakdown was estimated from dilution of L-[alpha-15N]lysine and L-[1-13C]ketoisocaproic acid (KIC) enrichments in plasma. Leucine oxidation was calculated from 13CO2 enrichments in expired air. Whole body protein breakdown was not increased above resting levels during the recovery period. Leucine oxidation was decreased after exercise (postexercise 13 +/- 2.3 vs. resting 19 +/- 3.2 mumol.kg-1.h-1; P less than 0.02), while nonoxidative leucine disposal was increased (115 +/- 6.1 vs. 103 +/- 5.6 micrograms.kg-1.min-1; P less than 0.02). After exercise, forearm net lysine balance was unchanged (87 +/- 25 vs. 93 +/- 28 nmol.100 ml-1.min-1), but there were decreases in forearm muscle protein degradation (219 +/- 51 vs. 356 +/- 85 nmol.100 ml-1.min-1; P less than 0.05) and synthesis (132 +/- 41 vs. 255 +/- 69 nmol.100 ml-1.min-1; P less than 0.01). In conclusion, after exercise 1) whole body protein degradation is not increased, 2) leucine disposal is directed away from oxidative and toward nonoxidative pathways, 3) forearm protein synthesis is decreased. Postexercise increases in whole body protein synthesis occur in tissues other than nonexercised muscle.

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34

Courtney-Martin, Glenda, Ronald O. Ball, and Paul B. Pencharz. "Sulfur amino acid metabolism and requirements." Nutrition Reviews 70, no. 3 (February 24, 2012): 170–75. http://dx.doi.org/10.1111/j.1753-4887.2011.00466.x.

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35

Holm, Eggert, Oliver Sedlaczek, and Eva Grips. "Amino acid metabolism in liver disease." Current Opinion in Clinical Nutrition and Metabolic Care 2, no. 1 (January 1999): 47–53. http://dx.doi.org/10.1097/00075197-199901000-00009.

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36

Tischler, Marc E. "Amino Acid Metabolism. David A. Bender." Quarterly Review of Biology 61, no. 4 (December 1986): 532–33. http://dx.doi.org/10.1086/415160.

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37

KLEINBERGER, G. "Amino acid metabolism in liver disease." Clinical Nutrition 4 (1985): 67–87. http://dx.doi.org/10.1016/s0261-5614(85)80009-1.

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Yudkoff, Marc, Yevgeny Daikhin, Ilana Nissim, and Itzhak Nissim. "Acidosis and astrocyte amino acid metabolism." Neurochemistry International 36, no. 4-5 (April 2000): 329–39. http://dx.doi.org/10.1016/s0197-0186(99)00141-2.

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Imura, Kenji, and Akira Okada. "Amino Acid Metabolism in Pediatric Patients." Nutrition 14, no. 1 (January 1998): 143–48. http://dx.doi.org/10.1016/s0899-9007(97)00230-x.

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Gough, N. R. "Coupling Lipid and Amino Acid Metabolism." Science Signaling 5, no. 213 (February 28, 2012): ec65-ec65. http://dx.doi.org/10.1126/scisignal.2003000.

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van der Schoor, Sophie. "Intestinal amino acid metabolism in neonates." Tijdschrift voor kindergeneeskunde 72, no. 2 (April 2004): 102–3. http://dx.doi.org/10.1007/bf03061492.

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Yudkoff, Marc, Yevgeny Daikhin, Ilana Nissim, Adam Lazarow, and Itzhak Nissim. "Brain amino acid metabolism and ketosis." Journal of Neuroscience Research 66, no. 2 (October 15, 2001): 272–81. http://dx.doi.org/10.1002/jnr.1221.

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Hattori, Ayuna, and Takahiro Ito. "Amino acid metabolism in myeloid leukemia." Experimental Hematology 43, no. 9 (September 2015): S66. http://dx.doi.org/10.1016/j.exphem.2015.06.136.

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DeFronzo, Ralph A. "Introduction: Protein and amino acid metabolism." Diabetes / Metabolism Reviews 4, no. 8 (December 1988): 749. http://dx.doi.org/10.1002/dmr.5610040804.

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Miyamoto, Tetsuya, Masumi Katane, Yasuaki Saitoh, Masae Sekine, and Hiroshi Homma. "Cystathionine β-lyase is involved in d-amino acid metabolism." Biochemical Journal 475, no. 8 (April 23, 2018): 1397–410. http://dx.doi.org/10.1042/bcj20180039.

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Non-canonical d-amino acids play important roles in bacteria including control of peptidoglycan metabolism and biofilm disassembly. Bacteria appear to produce non-canonical d-amino acids to adapt to various environmental changes, and understanding the biosynthetic pathways is important. We identified novel amino acid racemases possessing the ability to produce non-canonical d-amino acids in Escherichia coli and Bacillus subtilis in our previous study, whereas the biosynthetic pathways of these d-amino acids still remain unclear. In the present study, we demonstrated that two cystathionine β-lyases (MetC and MalY) from E. coli produce non-canonical d-amino acids including non-proteinogenic amino acids. Furthermore, MetC displayed d- and l-serine (Ser) dehydratase activity. We characterised amino acid racemase, Ser dehydratase and cysteine lyase activities, and all were higher for MetC. Interestingly, all three activities were at a comparable level for MetC, although optimal conditions for each reaction were distinct. These results indicate that MetC and MalY are multifunctional enzymes involved in l-methionine metabolism and the production of d-amino acids, as well as d- and l-Ser metabolism. To our knowledge, this is the first evidence that cystathionine β-lyase is a multifunctional enzyme with three different activities.

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Jones, Courtney L., Brett M. Stevens, Angelo D'Alessandro, Julia Reisz, Rachel Culp-Hill, Travis Nemkov, Shanshan Pei, et al. "Inhibition of Amino Acid Metabolism Selectively Targets Human Leukemia Stem Cells." Blood 132, Supplement 1 (November 29, 2018): 1521. http://dx.doi.org/10.1182/blood-2018-99-111965.

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Abstract Outcomes for AML patients remain poor because of the inability to fully eliminate leukemia stem cells (LSCs). We have previously shown that primary human LSCs reside in a unique metabolic condition characterized by a relatively low oxidative state (termed "ROS-low") and increased levels of glutathione (Lagadinou et al. Cell Stem Cell, 2013). Cells in this condition are highly dependent on oxidative phosphorylation (OXPHOS) for survival, in striking contrast to many tumor cells which often rely on glycolysis, suggesting that LSCs are governed by distinct metabolic properties. Therefore, the goal of this project was to identify and target metabolic vulnerabilities of LSCs. To achieve this objective, we used mass spectroscopy to interrogate the metabolome of leukemia stem cells (LSCs) isolated from primary human AML specimens. We observed significant increases in the levels, uptake, and metabolism of amino acids in LSCs compared to bulk AML cells. These data suggest that LSCs may preferentially rely on amino acids for survival. To investigate this hypothesis, we cultured LSCs and bulk leukemia cells isolated from primary leukemia specimens in media lacking amino acids and measured cell viability and colony forming potential. We found that LSCs were uniquely sensitive to amino acid loss. In addition, LSCs formed significantly fewer colonies upon amino acid depletion compared to LSCs cultured in media containing amino acids. To confirm that amino acid depletion was targeting functionally-defined LSCs, we employed engraftment assays in immune incompetent mice. Culturing primary AML cells without amino acids for 24 hours resulted in significantly reduced levels of leukemia cell engraftment. Next, we interrogated whether amino acid depletion impaired normal HSC survival and function by culturing mobilized peripheral blood without amino acids and measuring the frequency of CD34+ cells, colony forming ability, and engraftment into immune deficient mice. HSC frequency, colony forming ability, and engraftment potential were not changed by amino acid depletion. Altogether, these data demonstrate the LSCs are selectively dependent on amino acids for survival. We next determined how amino acids modulate LSC biology by measuring the consequences of amino acid loss on LSC metabolism. We observed that amino acid depletion decreased OXPHOS specifically in LSCs and not in bulk leukemia cells. We have previously shown that BCL-2 inhibition decreases OXPHOS in LSCs (Lagadinou et al. Cell Stem Cell, 2013). Importantly, recent studies have shown that inhibition of BCL-2 using the BCL-2 inhibitor venetoclax in combination with azacitidine has resulted in superior outcomes for AML patients (Dinardo et al. Lancet Oncology, 2018). Furthermore, our preliminary data demonstrates that venetoclax with azacitidine targets LSCs in AML patients. Therefore, we hypothesized that venetoclax with azacitidine may be targeting LSCs by modulating OXPHOS via amino acid metabolism. To test this hypothesis, we isolated LSCs from AML patients undergoing treatment with venetoclax and azacitidine. LSC specimens obtained pre and 24 hours after initiation of therapy were analyzed for changes in OXPHOS, gene expression, and the metabolome. We observed that venetoclax with azacitidine treatment decreased OXPHOS and reduced amino acid levels. In addition, expression of amino acid transporters was down-regulated. Finally, we sought to determine if culturing LSCs in high levels of amino acids before venetoclax and azacitidine treatment could rescue LSC viability and OXHPOS. We found that culturing LSCs with increased levels of amino acids rescued LSCs survival and OXPHOS, demonstrating that venetoclax with azacitidine targets LSCs by decreasing amino acid levels. Taken together, our data indicate that LSCs are selectively reliant on amino acid metabolism to fuel OXPHOS. Furthermore, amino acid metabolism can be targeted in AML patients by venetoclax with azacitidine treatment. These studies are the first to characterize metabolic targeting of LSCs in AML patients. Disclosures Nemkov: Omix Technologies inc: Equity Ownership. Pollyea:Argenx: Consultancy, Membership on an entity's Board of Directors or advisory committees; Karyopharm: Membership on an entity's Board of Directors or advisory committees; AbbVie: Consultancy, Research Funding; Celgene: Membership on an entity's Board of Directors or advisory committees; Agios: Consultancy, Membership on an entity's Board of Directors or advisory committees, Research Funding; Celyad: Consultancy, Membership on an entity's Board of Directors or advisory committees; Gilead: Consultancy; Pfizer: Consultancy, Membership on an entity's Board of Directors or advisory committees, Research Funding; Curis: Membership on an entity's Board of Directors or advisory committees.

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Ferrannini, E., R. A. DeFronzo, R. Gusberg, J. Tepler, R. Jacob, M. Aaron, D. Smith, and E. J. Barrett. "Splanchnic Amino Acid and Glucose Metabolism During Amino Acid Infusion in Dogs." Diabetes 37, no. 2 (February 1, 1988): 237–45. http://dx.doi.org/10.2337/diab.37.2.237.

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P. M., Jakeman. "Amino acid metabolism, branched-chain amino acid feeding and brain monoamine function." Proceedings of the Nutrition Society 57, no. 01 (February 1998): 35–41. http://dx.doi.org/10.1079/pns19980007.

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49

Ferrannini, E., R. A. DeFronzo, R. Gusberg, J. Tepler, R. Jacob, M. Aaron, D. Smith, and E. J. Barrett. "Splanchnic amino acid and glucose metabolism during amino acid infusion in dogs." Diabetes 37, no. 2 (February 1, 1988): 237–45. http://dx.doi.org/10.2337/diabetes.37.2.237.

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Griffith, O. W. "β-Amino Acids: Mammalian Metabolism and Utility as α-Amino Acid Analogues." Annual Review of Biochemistry 55, no. 1 (June 1986): 855–78. http://dx.doi.org/10.1146/annurev.bi.55.070186.004231.

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Journal articles on the topic 'Amino acid metabolism'

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