Relevant bibliographies by topics / Pyruvate

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Pyruvate'

Author: Grafiati
Published: 4 June 2021
Last updated: 14 March 2023

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Journal articles on the topic "Pyruvate"

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Mallet, Robert T., Jie Sun, E. Marty Knott, Arti B. Sharma, and Albert H. Olivencia-Yurvati. "Metabolic Cardioprotection by Pyruvate: Recent Progress." Experimental Biology and Medicine 230, no. 7 (July 2005): 435–43. http://dx.doi.org/10.1177/153537020523000701.

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Pyruvate, a natural metabolic fuel and antioxidant in myocardium and other tissues, exerts a variety of cardioprotective actions when provided at supraphysiological concentrations. Pyruvate increases cardiac contractile performance and myocardial energy state, bolsters endogenous antioxidant systems, and protects myocardium from ischemia-reperfusion injury and oxidant stress. This article reviews and discusses basic and clinically oriented research conducted over the last several years that has yielded fundamental information on pyruvate's inotropic and cardioprotective mechanisms. Particular attention is placed on pyruvate's enhancement of sarcoplasmic reticular Ca2+ transport, its antioxidant properties, and its ability to mitigate reversible and irreversible myocardial injury. These research efforts are establishing the essential foundation for clinical application of pyruvate therapy in numerous settings including cardiopulmonary bypass surgery, cardiopulmonary resuscitation, myocardial stunning, and cardiac failure.
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Mallet, Robert T., Albert H. Olivencia-Yurvati, and Rolf Bünger. "Pyruvate enhancement of cardiac performance: Cellular mechanisms and clinical application." Experimental Biology and Medicine 243, no. 2 (November 20, 2017): 198–210. http://dx.doi.org/10.1177/1535370217743919.

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Cardiac contractile function is adenosine-5'-triphosphate (ATP)-intensive, and the myocardium’s high demand for oxygen and energy substrates leaves it acutely vulnerable to interruptions in its blood supply. The myriad cardioprotective properties of the natural intermediary metabolite pyruvate make it a potentially powerful intervention against the complex injury cascade ignited by myocardial ischemia–reperfusion. A readily oxidized metabolic substrate, pyruvate augments myocardial free energy of ATP hydrolysis to a greater extent than the physiological fuels glucose, lactate and fatty acids, particularly when it is provided at supra-physiological plasma concentrations. Pyruvate also exerts antioxidant effects by detoxifying reactive oxygen and nitrogen intermediates, and by increasing nicotinamide adenine dinucleotide phosphate reduced form (NADPH) production to maintain glutathione redox state. These enhancements of free energy and antioxidant defenses combine to augment sarcoplasmic reticular Ca2+ release and re-uptake central to cardiac mechanical performance and to restore β-adrenergic signaling of ischemically stunned myocardium. By minimizing Ca2+ mismanagement and oxidative stress, pyruvate suppresses inflammation in post-ischemic myocardium. Thus, pyruvate administration stabilized cardiac performance, augmented free energy of ATP hydrolysis and glutathione redox systems, and/or quelled inflammation in a porcine model of cardiopulmonary bypass, a canine model of cardiac arrest–resuscitation, and a caprine model of hypovolemia and hindlimb ischemia–reperfusion. Pyruvate’s myriad benefits in preclinical models provide the mechanistic framework for its clinical application as metabolic support for myocardium at risk. Phase one trials have demonstrated pyruvate’s safety and efficacy for intravenous resuscitation for septic shock, intracoronary infusion for heart failure and as a component of cardioplegia for cardiopulmonary bypass. The favorable outcomes of these trials, which argue for expanded, phase three investigations of pyruvate therapy, mirror findings in isolated, perfused hearts, underscoring the pivotal role of preclinical research in identifying clinical interventions for cardiovascular diseases. Impact statement This article reviews pyruvate’s cardioprotective properties as an energy-yielding metabolic fuel, antioxidant and anti-inflammatory agent in mammalian myocardium. Preclinical research has shown these properties make pyruvate a powerful intervention to curb the complex injury cascade ignited by ischemia and reperfusion. In ischemically stunned isolated hearts and in large mammal models of cardiopulmonary bypass, cardiac arrest–resuscitation and hypovolemia, intracoronary pyruvate supports recovery of myocardial contractile function, intracellular Ca2+ homeostasis and free energy of ATP hydrolysis, and its antioxidant actions restore β-adrenergic signaling and suppress inflammation. The first clinical trials of pyruvate for cardiopulmonary bypass, fluid resuscitation and intracoronary intervention for congestive heart failure have been reported. Receiver operating characteristic analyses show remarkable concordance between pyruvate’s beneficial functional and metabolic effects in isolated, perfused hearts and in patients recovering from cardiopulmonary bypass in which they received pyruvate- vs. L-lactate-fortified cardioplegia. This research exemplifies the translation of mechanism-oriented preclinical studies to clinical application and outcomes.
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Abysalamah, Hazzar M. "Sodium Pyruvate Alters the Immune Response to Influenza A Virus Infection in Macrophages." Journal of Immunology 200, no. 1_Supplement (May 1, 2018): 108.21. http://dx.doi.org/10.4049/jimmunol.200.supp.108.21.

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Abstract Pyruvate is the end product of glycolysis. It can either be transported into the mitochondria for use in the TCA cycle or be used to regenerate NAD+ during aerobic glycolysis. We recently discovered that addition of sodium pyruvate to the culture medium during infection of macrophages with influenza A virus affects the production of cytokines involved in immune signaling. The purpose of the present study was to determine whether sodium pyruvate’s role in energy production in the macrophages may alter the immune response to the infection. While infection of macrophages with influenza A virus resulted in high levels of cytokines (IL-6, IL-1β, and TNF-α) in the absence of sodium pyruvate, the addition of sodium pyruvate significantly impaired cytokine production. Furthermore, sodium pyruvate did not affect virus growth, suggesting the effect of sodium pyruvate is on the immune response produced by the macrophages and not the viability of the virus.
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Reel, Jessica M., and Christopher R. Lupfer. "Sodium Pyruvate Ameliorates Influenza a Virus Infection In Vivo." Microbiology Research 12, no. 2 (March 26, 2021): 258–67. http://dx.doi.org/10.3390/microbiolres12020018.

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Influenza A virus (IAV) causes seasonal epidemics annually and pandemics every few decades. Most antiviral treatments used for IAV are only effective if administered during the first 48 h of infection and antiviral resistance is possible. Therapies that can be initiated later during IAV infection and that are less likely to elicit resistance will significantly improve treatment options. Pyruvate, a key metabolite, and an end product of glycolysis, has been studied for many uses, including its anti-inflammatory capabilities. Sodium pyruvate was recently shown by us to decrease inflammasome activation during IAV infection. Here, we investigated sodium pyruvate’s effects on IAV in vivo. We found that nebulizing mice with sodium pyruvate decreased morbidity and weight loss during infection. Additionally, treated mice consumed more chow during infection, indicating improved symptoms. There were notable improvements in pro-inflammatory cytokine production (IL-1β) and lower virus titers on day 7 post-infection in mice treated with sodium pyruvate compared to control animals. As pyruvate acts on the host immune response and metabolic pathways and not directly on the virus, our data demonstrate that sodium pyruvate is a promising treatment option that is safe, effective, and unlikely to elicit antiviral resistance.
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&NA;. "Pyruvate." Reactions Weekly &NA;, no. 376 (November 1991): 7–8. http://dx.doi.org/10.2165/00128415-199103760-00042.

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Vassault, Anne. "Pyruvate." EMC - Biologie Médicale 1, no. 3 (January 2006): 1–3. http://dx.doi.org/10.1016/s2211-9698(06)76497-4.

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Priestman, David A., Karen A. Orfali, and Mary C. Sugden. "Pyruvate inhibition of pyruvate dehydrogenase kinase." FEBS Letters 393, no. 2-3 (September 16, 1996): 174–78. http://dx.doi.org/10.1016/0014-5793(96)00877-0.

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Hasona, Adnan, Youngnyun Kim, F. G. Healy, L. O. Ingram, and K. T. Shanmugam. "Pyruvate Formate Lyase and Acetate Kinase Are Essential for Anaerobic Growth of Escherichia coli on Xylose." Journal of Bacteriology 186, no. 22 (November 15, 2004): 7593–600. http://dx.doi.org/10.1128/jb.186.22.7593-7600.2004.

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ABSTRACT During anaerobic growth of bacteria, organic intermediates of metabolism, such as pyruvate or its derivatives, serve as electron acceptors to maintain the overall redox balance. Under these conditions, the ATP needed for cell growth is derived from substrate-level phosphorylation. In Escherichia coli, conversion of glucose to pyruvate yields 2 net ATPs, while metabolism of a pentose, such as xylose, to pyruvate only yields 0.67 net ATP per xylose due to the need for one (each) ATP for xylose transport and xylulose phosphorylation. During fermentative growth, E. coli produces equimolar amounts of acetate and ethanol from two pyruvates, and these reactions generate one additional ATP from two pyruvates (one hexose equivalent) while still maintaining the overall redox balance. Conversion of xylose to acetate and ethanol increases the net ATP yield from 0.67 to 1.5 per xylose. An E. coli pfl mutant lacking pyruvate formate lyase cannot convert pyruvate to acetyl coenzyme A, the required precursor for acetate and ethanol production, and could not produce this additional ATP. E. coli pfl mutants failed to grow under anaerobic conditions in xylose minimal medium without any negative effect on their survival or aerobic growth. An ackA mutant, lacking the ability to generate ATP from acetyl phosphate, also failed to grow in xylose minimal medium under anaerobic conditions, confirming the need for the ATP produced by acetate kinase for anaerobic growth on xylose. Since arabinose transport by AraE, the low-affinity, high-capacity, arabinose/H+ symport, conserves the ATP expended in pentose transport by the ABC transporter, both pfl and ackA mutants grew anaerobically with arabinose. AraE-based xylose transport, achieved after constitutively expressing araE, also supported the growth of the pfl mutant in xylose minimal medium. These results suggest that a net ATP yield of 0.67 per pentose is only enough to provide for maintenance energy but not enough to support growth of E. coli in minimal medium. Thus, pyruvate formate lyase and acetate kinase are essential for anaerobic growth of E. coli on xylose due to energetic constraints.
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El-Harairy, Ahmed, Mennatallah Shaheen, Jun Li, Yuzhou Wu, Minghao Li, and Yanlong Gu. "Synthesis of α-indolylacrylates as potential anticancer agents using a Brønsted acid ionic liquid catalyst and the butyl acetate solvent." RSC Advances 10, no. 23 (2020): 13507–16. http://dx.doi.org/10.1039/d0ra00990c.

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4lNew α-indolylacrylate derivatives were synthesized by reaction of 2-substituted indoles with various pyruvates using a Brønsted acid ionic liquid catalyst in butyl acetate solvent. This is the first application of pyruvate compounds for the synthesis of indolylacrylates.
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Max-Audit, Isabelle. "Pyruvate kinase." EMC - Biologie Médicale 1, no. 3 (January 2006): 1–4. http://dx.doi.org/10.1016/s2211-9698(06)76498-6.

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Dissertations / Theses on the topic "Pyruvate"

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Debebe, Tewodros, Monika Krüger, Klaus Huse, Johannes Kacza, Katja Mühlberg, Brigitte König, and Gerd Birkenmeier. "Ethyl pyruvate." Universitätsbibliothek Leipzig, 2016. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-212525.

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The microbiota has a strong influence on health and disease in humans. A causative shift favoring pathobionts is strongly linked to diseases. Therefore, anti-microbial agents selectively targeting potential pathogens as well as their biofilms are urgently demanded. Here we demonstrate the impact of ethyl pyruvate, so far known as ROS scavenger and antiinflammatory agent, on planktonic microbes and biofilms. Ethyl pyruvate combats preferably the growth of pathobionts belonging to bacteria and fungi independent of the genera and prevailing drug resistance. Surprisingly, this anti-microbial agent preserves symbionts like Lactobacillus species. Moreover, ethyl pyruvate prevents the formation of biofilms and promotes matured biofilms dissolution. This potentially new anti-microbial and anti-biofilm agent could have a tremendous positive impact on human, veterinary medicine and technical industry as well.
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Blalock, LeeAnn Talarico. "Expression of pyruvate decarboxylase in a Gram positive host Sarcina ventriculi pyruvate decarboxylase versus other known pyruvate decarboxylases /." [Gainesville, Fla.] : University of Florida, 2003. http://purl.fcla.edu/fcla/etd/UFE0002366.

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Walker, Dianne. "Bacillus stearothermophilus pyruvate kinase." Thesis, University of Bristol, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.335572.

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Wexler, Isaiah David. "Disorders of pyruvate metabolism." Case Western Reserve University School of Graduate Studies / OhioLINK, 1995. http://rave.ohiolink.edu/etdc/view?acc_num=case1057937741.

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Peng, YI. "Pyruvate formate lyase and pyruvate formate lyase activating enzyme spectroscopic characteristics, interaction and mechanism /." Diss., Connect to online resource - MSU authorized users, 2008.

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Johnson, Sam. "Insulin regulation of pyruvate dehydrogenase." Thesis, University of Bristol, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.390644.

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Burthier, Jean Michel. "Les déficits en pyruvate déshydrogénase." Paris 5, 1990. http://www.theses.fr/1990PA05P176.

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Cassady, Alan Ian. "Pyruvate carboxylase : a molecular biological study /." Title page, contents and summary only, 1987. http://web4.library.adelaide.edu.au/theses/09PH/09phc343.pdf.

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Chen, Yiyuan. "Regulation studies on human pyruvate kinases." Thesis, University of Edinburgh, 2018. http://hdl.handle.net/1842/33175.

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Human pyruvate kinase performs the last step in glucose glycolysis in all cells and organisms and can be a key regulator of glycolytic flux. Pyruvate produced by PYK is transported into the mitochondria to fuel the TCA cycle, which enables the production of ATP; the main energy source of the cell. Human PYK contains four isoforms: M1 (found in muscle, heart and brain), M2 (in foetal cells and tumours), L (liver), and R (red blood cells) PYK. M2PYK plays a crucial role in tumour cell proliferation; by down-regulating metabolic flux, upstream metabolites can be used for protein and DNA synthesis. Reprogramming the metabolism of fast proliferating cells is called the 'Warburg effect'. The biological relevance of the different isoform activities is also discussed. For example RPYK in red blood cells is exposed to slowly altering metabolite concentrations, especially after intestinal absorption in plasma and RBCs uptake some of the metabolites. This thesis describes biochemical and biophysical studies of human M1PYK, M2PYK, LPYK, and RPYK. PYK is allosterically regulated by a range of metabolites. A comparative enzyme kinetics study of the four isoforms was performed to examine the mechanisms of activation and inhibition of these small molecule regulators, including all 20 amino acids and the thyroid hormone T3. The redox state of the environment was also found to be an important regulator of PYK activity. All four PYK isoforms were successfully expressed and purified. Interestingly, only M2PYK and RPYK were strongly regulated by amino acids and metabolites. We also found that the redox state regulates the activity of all four PYK isoforms as well as the sensitivity of M2PYK in response to natural regulators. These studies also confirmed the dissociation of tetrameric PYK into inactive monomers as an important mechanism of regulation, particularly for M2PYK activity. Nuclear magnetic resonance (NMR) and Small-angle X-ray scattering (SAXS) studies were performed to investigate the conformational behaviour of PYK isoforms in solution and to compare the effects of ligand binding. NMR data of all four isoforms reveal a conserved binding mechanism between isoforms and specific amino acids. SAXS data of all four isoforms demonstrate that ligands affect tetramerisation of PYK isoforms.
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Robinson, Andrew James Cave. "Pyruvate kinase & glycolysis in potato." Thesis, University of Cambridge, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.335799.

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Books on the topic "Pyruvate"

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B, Keech D., and Wallace J. C, eds. Pyruvate carboxylase. Boca Raton, Fla: CRC Press, 1985.

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Yazdanpanah, Mehrdad. Pyruvate improves myocardial functional recovery after ischemia and reperfusion. Ottawa: National Library of Canada, 1998.

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Dykshoorn, Philip. Identification of an upstream activating sequence of the yeast pyruvate kinase gene (PYK). Ottawa: National Library of Canada, 1990.

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Lesicki, Andrzej. Fosfofruktokinaza i kinaza pirogronianowa w tkankach skorupiaków i owadów. 3rd ed. Poznań: Wydawn. Nauk. Uniwersytetu im. Adama Mickiewicza, 1993.

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Staples, Elizabeth M. The effects of R(+)-lipoic acid supplementation on regulation of human skeletal muscle pyruvate dehydrogenase. St. Catharines, Ont: Brock University, Faculty of Applied Health Science, 2006.

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MacPherson, Laura Lynn. Adaptations of skeletal muscle pyruvate dehydrogenase kinase in response to food-restriction in mitochondrial subpopulations. St. Catharines, Ont: Brock University, Faculty of Applied Health Sciences, 2007.

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International Meeting on the Function of Thiamin Diphosphate Enzymes (1990 Blaubeuren, Germany). Biochemistry and physiology of thiamin diphosphate enzymes: Proceedings of the International Meeting on the Function of Thiamin Diphosphate Enzymes, held in Blaubeuren, October 1990. Weinheim: VCH, 1991.

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Parker, James N., and Philip M. Parker. Pyruvate carboxylase deficiency: A bibliography and dictionary for physicians, patients, and genome researchers [to Internet references]. San Diego, CA: ICON Health Publications, 2007.

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Pyruvate: The natural dietary supplement that increases exercise endurance, promotes fat loss, and regulates blood sugar metabolism. New Canaan, Conn: Keats Pub., 1997.

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Bornemann, Stephen. Studies on pyruvate decarboxylase-catalysed acyloin formation and the effects of surfactants on lipase-catalysedhydrolysis of esters. [s.l.]: typescript, 1992.

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Book chapters on the topic "Pyruvate"

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Cleaves, Henderson James. "Pyruvate." In Encyclopedia of Astrobiology, 2098. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_5134.

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Cleaves, Henderson James. "Pyruvate." In Encyclopedia of Astrobiology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27833-4_5134-1.

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De Meirleir, Linda. "Pyruvate Carboxylase and Pyruvate Dehydrogenase Deficiency." In Physician's Guide to the Diagnosis, Treatment, and Follow-Up of Inherited Metabolic Diseases, 303–11. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-40337-8_19.

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Schomburg, Dietmar, Margit Salzmann, and Dörte Stephan. "Pyruvate oxidase." In Enzyme Handbook, 267–70. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-58051-2_56.

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Schomburg, Dietmar, Margit Salzmann, and Dörte Stephan. "Pyruvate synthase." In Enzyme Handbook, 333–38. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-58051-2_68.

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Schomburg, Dietmar, and Margit Salzmann. "Pyruvate decarboxylase." In Enzyme Handbook 1, 1–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_1.

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Stotz, Elmer. "Pyruvate Metabolism." In Advances in Enzymology - and Related Areas of Molecular Biology, 129–64. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122501.ch5.

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Schomburg, Dietmar, and Dörte Stephan. "Pyruvate kinase." In Enzyme Handbook 13, 799–810. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59176-1_151.

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Schomburg, Dietmar, Margit Salzmann, and Dörte Stephan. "Pyruvate dehydrogenase (NADP+)." In Enzyme Handbook, 223–25. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-58051-2_46.

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Schomburg, Dietmar, Margit Salzmann, and Dörte Stephan. "Pyruvate dehydrogenase (cytochrome)." In Enzyme Handbook, 251–54. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-58051-2_53.

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Conference papers on the topic "Pyruvate"

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Bamberger, A., M. Szibor, F. N. Gellerich, T. Doenst, and M. Schwarzer. "Contractile Function Is Regulated by Regulation of Pyruvate Supply." In 50th Annual Meeting of the German Society for Thoracic and Cardiovascular Surgery (DGTHG). Georg Thieme Verlag KG, 2021. http://dx.doi.org/10.1055/s-0041-1725676.

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Zayou, Fouzia, Chintan Chheda, Adrian Lim, Omer H. Elmadbouh, Stephen J. Pandol, and Mouad Edderkaoui. "Abstract 2403: Pyruvate dehydrogenase mediates chemo-resistance in pancreatic cancer." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-2403.

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Scott, Iain, Dharendra Thapa, Paramesha Bugga, Bellina Mushala, Janet Manning, Michael Stoner, Brenda McMahon, et al. "BS3 GCN5L1 promotes diastolic dysfunction by inhibiting cardiac pyruvate oxidation." In British Cardiovascular Society Annual Conference, ‘100 years of Cardiology’, 6–8 June 2022. BMJ Publishing Group Ltd and British Cardiovascular Society, 2022. http://dx.doi.org/10.1136/heartjnl-2022-bcs.183.

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Kay, Emily, Lisa Neilson, Claudia Boldrini, Juan Hernandez-Fernaud, Enio Gjerga, David Sumpton, Sandeep Dhayade, et al. "Abstract B76: Pyruvate dehydrogenase: A key to epigenetic regulation in CAFs." In Abstracts: AACR Special Conference on Advances in Ovarian Cancer Research; September 13-16, 2019; Atlanta, GA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1557-3265.ovca19-b76.

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Damerau, Alexandra, Marieluise Kirchner, Moritz Pfeiffenberger, Lisa Ehlers, Ha Nguyen Duc Do, Philipp Mertins, Benjamin Bartek, et al. "Pyruvate dehydrogenase kinases as a potential novel target to treat osteoarthritis." In Jahreskongress DVO OSTEOLOGIE 2022. Georg Thieme Verlag, 2022. http://dx.doi.org/10.1055/s-0042-1755919.

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Yahui, He, Li Yan, He Hongwu, and Yuan Junlin. "A New Optimized Spectrophotometric Assay for the Measurement of Pyruvate Dehydrogenase's Activity." In 2007 1st International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2007. http://dx.doi.org/10.1109/icbbe.2007.110.

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Rai, N., T. Novoyatleva, N. Weissmann, H. A. Ghofrani, R. T. Schermuly, and W. Seeger. "Role of Pyruvate Kinase 2 Muscle (PKM2) Oligomerization in Pulmonary Arterial Hypertension." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a5278.

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Maskevich, Sergei A., Ivan P. Chernikevich, Gennedy A. Gachko, Leonid N. Kivach, and Nataliya D. Strekal. "Study of pyruvate decarboxylase and thiamine kinase from brewer's yeast by SERS." In Laser Spectroscopy of Biomolecules: 4th International Conference on Laser Applications in Life Sciences, edited by Jouko E. Korppi-Tommola. SPIE, 1993. http://dx.doi.org/10.1117/12.146134.

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O'Neill, Wendi, Tereza Golias, Martin Benej, and Nicholas Denko. "Abstract 5467: Phosphoproteomic analysis of pyruvate dehydrogenase in response to environmental stress." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-5467.

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Birch, Jodie, and Joao Passos. "The mitochondrial pyruvate carrier: a role in senescence and the ageing lung?" In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.oa4439.

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Reports on the topic "Pyruvate"

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Corscadden, Louise, and Anjali Singh. Metabolism And Measurable Metabolic Parameters. ConductScience, December 2022. http://dx.doi.org/10.55157/me20221213.

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Metabolism is the sum of chemical reactions involved in sustaining the life of organisms.[1] It constantly provides your body with the energy to perform essential functions. The process is categorized into two groups:[2] Catabolism: It’s the process of breaking down molecules to obtain energy. For example, converting glucose to pyruvate by cellular respiration. Anabolism: It’s the process of synthesis of compounds required to run the metabolic process of the organisms. For example, carbohydrates, proteins, lipids, and nucleic acids.[2] Metabolism is affected by a range of factors, such as age, sex, muscle mass, body size, and physical activity affect metabolism or BMR (the basal metabolic rate). By definition, BMR is the minimum amount of calories your body requires to function at rest.[2] Now, you have a rough idea about the concept. But, you might wonder why you need to study it. What and how metabolic parameters are measured to determine the metabolism of the organism? Find the answer to all these questions in this article.
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Or, Etti, David Galbraith, and Anne Fennell. Exploring mechanisms involved in grape bud dormancy: Large-scale analysis of expression reprogramming following controlled dormancy induction and dormancy release. United States Department of Agriculture, December 2002. http://dx.doi.org/10.32747/2002.7587232.bard.

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The timing of dormancy induction and release is very important to the economic production of table grape. Advances in manipulation of dormancy induction and dormancy release are dependent on the establishment of a comprehensive understanding of biological mechanisms involved in bud dormancy. To gain insight into these mechanisms we initiated the research that had two main objectives: A. Analyzing the expression profiles of large subsets of genes, following controlled dormancy induction and dormancy release, and assessing the role of known metabolic pathways, known regulatory genes and novel sequences involved in these processes B. Comparing expression profiles following the perception of various artificial as well as natural signals known to induce dormancy release, and searching for gene showing similar expression patterns, as candidates for further study of pathways having potential to play a central role in dormancy release. We first created targeted EST collections from V. vinifera and V. riparia mature buds. Clones were randomly selected from cDNA libraries prepared following controlled dormancy release and controlled dormancy induction and from respective controls. The entire collection (7920 vinifera and 1194 riparia clones) was sequenced and subjected to bioinformatics analysis, including clustering, annotations and GO classifications. PCR products from the entire collection were used for printing of cDNA microarrays. Bud tissue in general, and the dormant bud in particular, are under-represented within the grape EST database. Accordingly, 59% of the our vinifera EST collection, composed of 5516 unigenes, are not included within the current Vitis TIGR collection and about 22% of these transcripts bear no resemblance to any known plant transcript, corroborating the current need for our targeted EST collection and the bud specific cDNA array. Analysis of the V. riparia sequences yielded 814 unigenes, of which 140 are unique (keilin et al., manuscript, Appendix B). Results from computational expression profiling of the vinifera collection suggest that oxidative stress, calcium signaling, intracellular vesicle trafficking and anaerobic mode of carbohydrate metabolism play a role in the regulation and execution of grape-bud dormancy release. A comprehensive analysis confirmed the induction of transcription from several calcium–signaling related genes following HC treatment, and detected an inhibiting effect of calcium channel blocker and calcium chelator on HC-induced and chilling-induced bud break. It also detected the existence of HC-induced and calcium dependent protein phosphorylation activity. These data suggest, for the first time, that calcium signaling is involved in the mechanism of dormancy release (Pang et al., in preparation). We compared the effects of heat shock (HS) to those detected in buds following HC application and found that HS lead to earlier and higher bud break. We also demonstrated similar temporary reduction in catalase expression and temporary induction of ascorbate peroxidase, glutathione reductase, thioredoxin and glutathione S transferase expression following both treatments. These findings further support the assumption that temporary oxidative stress is part of the mechanism leading to bud break. The temporary induction of sucrose syntase, pyruvate decarboxylase and alcohol dehydrogenase indicate that temporary respiratory stress is developed and suggest that mitochondrial function may be of central importance for that mechanism. These finding, suggesting triggering of identical mechanisms by HS and HC, justified the comparison of expression profiles of HC and HS treated buds, as a tool for the identification of pathways with a central role in dormancy release (Halaly et al., in preparation). RNA samples from buds treated with HS, HC and water were hybridized with the cDNA arrays in an interconnected loop design. Differentially expressed genes from the were selected using R-language package from Bioconductor project called LIMMA and clones showing a significant change following both HS and HC treatments, compared to control, were selected for further analysis. A total of 1541 clones show significant induction, of which 37% have no hit or unknown function and the rest represent 661 genes with identified function. Similarly, out of 1452 clones showing significant reduction, only 53% of the clones have identified function and they represent 573 genes. The 661 induced genes are involved in 445 different molecular functions. About 90% of those functions were classified to 20 categories based on careful survey of the literature. Among other things, it appears that carbohydrate metabolism and mitochondrial function may be of central importance in the mechanism of dormancy release and studies in this direction are ongoing. Analysis of the reduced function is ongoing (Appendix A). A second set of hybridizations was carried out with RNA samples from buds exposed to short photoperiod, leading to induction of bud dormancy, and long photoperiod treatment, as control. Analysis indicated that 42 genes were significant difference between LD and SD and 11 of these were unique.
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(Pyruvate decarboxylase: A key enzyme for alcohol production). Office of Scientific and Technical Information (OSTI), January 1989. http://dx.doi.org/10.2172/5454091.

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