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Relevant bibliographies by topics / Pyruvate mitochondrial

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Academic literature on the topic 'Pyruvate mitochondrial'

Author: Grafiati

Published: 18 May 2024

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Journal articles on the topic "Pyruvate mitochondrial"

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HILDYARD, John C. W., and Andrew P. HALESTRAP. "Identification of the mitochondrial pyruvate carrier in Saccharomyces cerevisiae." Biochemical Journal 374, no. 3 (September 15, 2003): 607–11. http://dx.doi.org/10.1042/bj20030995.

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Mitochondrial pyruvate transport is fundamental for metabolism and mediated by a specific inhibitable carrier. We have identified the yeast mitochondrial pyruvate carrier by measuring inhibitor-sensitive pyruvate uptake into mitochondria from 18 different Saccharomyces cerevisiae mutants, each lacking an unattributed member of the mitochondrial carrier family (MCF). Only mitochondria from the YIL006w deletion mutant exhibited no inhibitor-sensitive pyruvate transport, but otherwise behaved normally. YIL006w encodes a 41.9 kDa MCF member with homologous proteins present in both the human and mouse genomes.

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Tang, Bor Luen. "Targeting the Mitochondrial Pyruvate Carrier for Neuroprotection." Brain Sciences 9, no. 9 (September 18, 2019): 238. http://dx.doi.org/10.3390/brainsci9090238.

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The mitochondrial pyruvate carriers mediate pyruvate import into the mitochondria, which is key to the sustenance of the tricarboxylic cycle and oxidative phosphorylation. However, inhibition of mitochondria pyruvate carrier-mediated pyruvate transport was recently shown to be beneficial in experimental models of neurotoxicity pertaining to the context of Parkinson’s disease, and is also protective against excitotoxic neuronal death. These findings attested to the metabolic adaptability of neurons resulting from MPC inhibition, a phenomenon that has also been shown in other tissue types. In this short review, I discuss the mechanism and potential feasibility of mitochondrial pyruvate carrier inhibition as a neuroprotective strategy in neuronal injury and neurodegenerative diseases.

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Zangari, Joséphine, Francesco Petrelli, Benoît Maillot, and Jean-Claude Martinou. "The Multifaceted Pyruvate Metabolism: Role of the Mitochondrial Pyruvate Carrier." Biomolecules 10, no. 7 (July 17, 2020): 1068. http://dx.doi.org/10.3390/biom10071068.

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Pyruvate, the end product of glycolysis, plays a major role in cell metabolism. Produced in the cytosol, it is oxidized in the mitochondria where it fuels the citric acid cycle and boosts oxidative phosphorylation. Its sole entry point into mitochondria is through the recently identified mitochondrial pyruvate carrier (MPC). In this review, we report the latest findings on the physiology of the MPC and we discuss how a dysfunctional MPC can lead to diverse pathologies, including neurodegenerative diseases, metabolic disorders, and cancer.

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Reiter, Russel, Ramaswamy Sharma, Sergio Rosales-Corral, Walter Manucha, Luiz Gustavo de Almeida Chuffa, and Debora Aparecida Pires de Campos Zuccari. "Melatonin and Pathological Cell Interactions: Mitochondrial Glucose Processing in Cancer Cells." International Journal of Molecular Sciences 22, no. 22 (November 19, 2021): 12494. http://dx.doi.org/10.3390/ijms222212494.

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Melatonin is synthesized in the pineal gland at night. Since melatonin is produced in the mitochondria of all other cells in a non-circadian manner, the amount synthesized by the pineal gland is less than 5% of the total. Melatonin produced in mitochondria influences glucose metabolism in all cells. Many pathological cells adopt aerobic glycolysis (Warburg effect) in which pyruvate is excluded from the mitochondria and remains in the cytosol where it is metabolized to lactate. The entrance of pyruvate into the mitochondria of healthy cells allows it to be irreversibly decarboxylated by pyruvate dehydrogenase (PDH) to acetyl coenzyme A (acetyl-CoA). The exclusion of pyruvate from the mitochondria in pathological cells prevents the generation of acetyl-CoA from pyruvate. This is relevant to mitochondrial melatonin production, as acetyl-CoA is a required co-substrate/co-factor for melatonin synthesis. When PDH is inhibited during aerobic glycolysis or during intracellular hypoxia, the deficiency of acetyl-CoA likely prevents mitochondrial melatonin synthesis. When cells experiencing aerobic glycolysis or hypoxia with a diminished level of acetyl-CoA are supplemented with melatonin or receive it from another endogenous source (pineal-derived), pathological cells convert to a more normal phenotype and support the transport of pyruvate into the mitochondria, thereby re-establishing a healthier mitochondrial metabolic physiology.

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Moyes, C. D., L. T. Buck, P. W. Hochachka, and R. K. Suarez. "Oxidative properties of carp red and white muscle." Journal of Experimental Biology 143, no. 1 (May 1, 1989): 321–31. http://dx.doi.org/10.1242/jeb.143.1.321.

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Substrate preferences of isolated mitochondria and maximal enzyme activities were used to assess the oxidative capacities of red muscle (RM) and white muscle (WM) of carp (Cyprinus carpio). A 14-fold higher activity of citrate synthase (CS) in RM reflects the higher mitochondrial density in this tissue. RM mitochondria oxidize pyruvate and fatty acyl carnitines (8:O, 12:O, 16:O) at similarly high rates. WM mitochondria oxidize these fatty acyl carnitines at 35–70% the rate of pyruvate, depending on chain length. WM has only half the carnitine palmitoyl transferase/CS ratio of RM, but similar ratios of beta-hydroxyacyl CoA dehydrogenase/CS. Ketone bodies are poor substrates for mitochondria from both tissues. In both tissues mitochondrial alpha-glycerophosphate oxidation was minimal, and alpha-glycerophosphate dehydrogenase was present at low activities, suggesting the alpha-glycerophosphate shuttle is of minor significance in maintaining cytosolic redox balance in either tissue. The mitochondrial oxidation rates of other substrates relative to pyruvate are as follows: alpha-ketoglutarate 90% (RM and WM); glutamate 45% (WM) and 70% (RM); proline 20% (WM) and 45% (RM). Oxidation of neutral amino acids (serine, glycine, alanine, beta-alanine) was not consistently detectable. These data suggest that RM and WM differ in mitochondrial properties as well as mitochondrial abundance. Whereas RM mitochondria appear to be able to utilize a wide range of metabolic fuels (fatty acids, pyruvate, amino acids but not ketone bodies), WM mitochondria appear to be specialized to use pyruvate.

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Simard, Chloé, Andréa Lebel, Eric Pierre Allain, Mohamed Touaibia, Etienne Hebert-Chatelain, and Nicolas Pichaud. "Metabolic Characterization and Consequences of Mitochondrial Pyruvate Carrier Deficiency in Drosophila melanogaster." Metabolites 10, no. 9 (September 6, 2020): 363. http://dx.doi.org/10.3390/metabo10090363.

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In insect, pyruvate is generally the predominant oxidative substrate for mitochondria. This metabolite is transported inside mitochondria via the mitochondrial pyruvate carrier (MPC), but whether and how this transporter controls mitochondrial oxidative capacities in insects is still relatively unknown. Here, we characterize the importance of pyruvate transport as a metabolic control point for mitochondrial substrate oxidation in two genotypes of an insect model, Drosophila melanogaster, differently expressing MPC1, an essential protein for the MPC function. We evaluated the kinetics of pyruvate oxidation, mitochondrial oxygen consumption, metabolic profile, activities of metabolic enzymes, and climbing abilities of wild-type (WT) flies and flies harboring a deficiency in MPC1 (MPC1def). We hypothesized that MPC1 deficiency would cause a metabolic reprogramming that would favor the oxidation of alternative substrates. Our results show that the MPC1def flies display significantly reduced climbing capacity, pyruvate-induced oxygen consumption, and enzymatic activities of pyruvate kinase, alanine aminotransferase, and citrate synthase. Moreover, increased proline oxidation capacity was detected in MPC1def flies, which was associated with generally lower levels of several metabolites, and particularly those involved in amino acid catabolism such as ornithine, citrulline, and arginosuccinate. This study therefore reveals the flexibility of mitochondrial substrate oxidation allowing Drosophila to maintain cellular homeostasis.

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VALENTI, Daniela, Lidia de BARI, Anna ATLANTE, and Salvatore PASSARELLA. "l-Lactate transport into rat heart mitochondria and reconstruction of the l-lactate/pyruvate shuttle." Biochemical Journal 364, no. 1 (May 8, 2002): 101–4. http://dx.doi.org/10.1042/bj3640101.

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In vitro reconstruction of the l-lactate/pyruvate shuttle has been performed, which allows NADH oxidation outside rat heart mitochondria. Such a shuttle occurs due to the combined action of the novel mitochondrial l-lactate/pyruvate antiporter, which differs from the monocarboxylate carrier, and the mitochondrial l-lactate dehydrogenase. The rate of l-lactate/pyruvate antiport proved to regulate the shuttle in vitro.

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Fernandez-Caggiano, Mariana, and Philip Eaton. "Heart failure—emerging roles for the mitochondrial pyruvate carrier." Cell Death & Differentiation 28, no. 4 (January 20, 2021): 1149–58. http://dx.doi.org/10.1038/s41418-020-00729-0.

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AbstractThe mitochondrial pyruvate carrier (MPC) is the entry point for the glycolytic end-product pyruvate to the mitochondria. MPC activity, which is controlled by its abundance and post-translational regulation, determines whether pyruvate is oxidised in the mitochondria or metabolised in the cytosol. MPC serves as a crucial metabolic branch point that determines the fate of pyruvate in the cell, enabling metabolic adaptations during health, such as exercise, or as a result of disease. Decreased MPC expression in several cancers limits the mitochondrial oxidation of pyruvate and contributes to lactate accumulation in the cytosol, highlighting its role as a contributing, causal mediator of the Warburg effect. Pyruvate is handled similarly in the failing heart where a large proportion of it is reduced to lactate in the cytosol instead of being fully oxidised in the mitochondria. Several recent studies have found that the MPC abundance was also reduced in failing human and mouse hearts that were characterised by maladaptive hypertrophic growth, emulating the anabolic scenario observed in some cancer cells. In this review we discuss the evidence implicating the MPC as an important, perhaps causal, mediator of heart failure progression.

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Diers, Anne R., Katarzyna A. Broniowska, Ching-Fang Chang, and Neil Hogg. "Pyruvate fuels mitochondrial respiration and proliferation of breast cancer cells: effect of monocarboxylate transporter inhibition." Biochemical Journal 444, no. 3 (May 29, 2012): 561–71. http://dx.doi.org/10.1042/bj20120294.

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Recent studies have highlighted the fact that cancer cells have an altered metabolic phenotype, and this metabolic reprogramming is required to drive the biosynthesis pathways necessary for rapid replication and proliferation. Specifically, the importance of citric acid cycle-generated intermediates in the regulation of cancer cell proliferation has been recently appreciated. One function of MCTs (monocarboxylate transporters) is to transport the citric acid cycle substrate pyruvate across the plasma membrane and into mitochondria, and inhibition of MCTs has been proposed as a therapeutic strategy to target metabolic pathways in cancer. In the present paper, we examined the effect of different metabolic substrates (glucose and pyruvate) on mitochondrial function and proliferation in breast cancer cells. We demonstrated that cancer cells proliferate more rapidly in the presence of exogenous pyruvate when compared with lactate. Pyruvate supplementation fuelled mitochondrial oxygen consumption and the reserve respiratory capacity, and this increase in mitochondrial function correlated with proliferative potential. In addition, inhibition of cellular pyruvate uptake using the MCT inhibitor α-cyano-4-hydroxycinnamic acid impaired mitochondrial respiration and decreased cell growth. These data demonstrate the importance of mitochondrial metabolism in proliferative responses and highlight a novel mechanism of action for MCT inhibitors through suppression of pyruvate-fuelled mitochondrial respiration.

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Li, Min, Shuang Zhou, Chaoyang Chen, Lingyun Ma, Daohuang Luo, Xin Tian, Xiu Dong, Ying Zhou, Yanling Yang, and Yimin Cui. "Therapeutic potential of pyruvate therapy for patients with mitochondrial diseases: a systematic review." Therapeutic Advances in Endocrinology and Metabolism 11 (January 2020): 204201882093824. http://dx.doi.org/10.1177/2042018820938240.

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Background: Mitochondrial disease is a term used to describe a set of heterogeneous genetic diseases caused by impaired structure or function of mitochondria. Pyruvate therapy for mitochondrial disease is promising from a clinical point of view. Methods: According to PRISMA guidelines, the following databases were searched to identify studies regarding pyruvate therapy for mitochondrial disease: PubMed, EMBASE, Cochrane Library, and Clinicaltrials. The search was up to April 2019. The endpoints were specific biomarkers (plasma level of lactate, plasma level of pyruvate, L/P ratio) and clinical rating scales [Japanese mitochondrial disease-rating scale (JMDRS), Newcastle Mitochondrial Disease Adult Scale (NMDAS), and others]. Two researchers independently screened articles, extracted data, and assessed the quality of the studies. Results: A total of six studies were included. Considerable differences were noted between studies in terms of study design, patient information, and outcome measures. The collected evidence may indicate an effective potential of pyruvate therapy on the improvement of mitochondrial disease. The majority of the common adverse events of pyruvate therapy were diarrhea and short irritation of the stomach. Conclusion: Pyruvate therapy with no serious adverse events may be a potential therapeutic candidate for patients with incurable mitochondrial diseases, such as Leigh syndrome. However, recent evidence taken from case series and case reports, and theoretical supports of basic research are not sufficient. The use of global registries to collect patient data and more adaptive trial designs with larger numbers of participants are necessary to clarify the efficacy of pyruvate therapy.

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Dissertations / Theses on the topic "Pyruvate mitochondrial"

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Hildyard, John Carl Westgarth. "Identification of the mitochondrial pyruvate carrier." Thesis, University of Bristol, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.410146.

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McGow, Donna. "Cloning and characterisation of the plant pyruvate dehydrogenase complex components." Thesis, University of Glasgow, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.248232.

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Collins, Yvonne. "Regulation of pyruvate dehydrogenase kinase 2 by mitochondrial reactive oxygen species." Thesis, University of Cambridge, 2015. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708470.

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Nemani, Neeharika. "Molecular Determinant of Mitochondrial Shape Change." Diss., Temple University Libraries, 2018. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/511170.

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Biomedical Sciences
Ph.D.
Mitochondria shape cytosolic Ca2+ (cCa2+) transients. Ca2+ entry into the mitochondria is driven by the highly negative mitochondrial membrane potential and through a highly selective channel, the Mitochondrial Calcium Uniporter (MCU). Mitochondrial Ca2+ (mCa2+) is utilized by the matrix dehydrogenases for maintaining cellular bioenergetics. The TCA cycle-derived NADH and FADH2 are mCa2+ dependent thus, feed into the electron transport chain (ETC) to generate ATP. Either loss of mCa2+ or metabolite uptake by the mitochondria results in a bioenergetic crisis and mitochondrial dysfunction. Reciprocally, sudden elevation of cCa2+ under conditions of stroke or ischemia/reperfusion injury (I/R) drives excessive mCa2+ overload that in turn leads to the opening of a large channel, the mitochondrial permeability transition pore (PTP) that triggers necrotic cell death. Thus, Ca2+ and metabolite equilibrium is essential to maintain a healthy mitochondrial pool. Our laboratory has previously showed that loss of mCa2+ uptake leads to decreased ATP generation and cell survival through autophagy. Although metabolite scarcity also results in similar reduction in ATP generation, the molecular mechanisms by which metabolites control mitochondrial ion homeostasis remain elusive. Deprivation of glucose or supplementation of mitochondrial pyruvate carrier (MPC) transport blocker UK5099 and or carnitine-dependent fatty acid blocker etomoxir triggered an increase in the expression of MICU1, a regulator of the mitochondrial calcium uniporter (MCU) but not the MCU core subunit. Consistently, either RNAi-mediated deletion of MPC isoforms or dominant negative human mutant MPC1 R97W showed significant induction of MICU1 protein abundance and inhibition of MCU-mediated mCa2+ uptake. Moreover, TCA cycle substrate-dependent MICU1 expression is under the control of EGR1 transcriptional regulation. Reciprocally, the MICU1 dependent inhibition of mCa2+ uptake exhibited lower NADH production and oxygen consumption and ATP production. The reduction of mitochondrial pyruvate by MPC knockdown is linked to higher production of mitochondrial ROS and elevated autophagy markers. These studies reveal an unexpected regulation of MCU-mediated mCa2+ flux machinery involving major TCA cycle substrate availability and possibly MICU1 to control cellular switch between glycolysis and oxidative phosphorylation. While mCa2+ is required for energy generation, sustained elevation of mCa2+ results in mitochondrial swelling and necrotic death. Hence, it was thought that preventing mCa2+ overload can be protective under conditions of elevated cCa2+. Contrary to this, mice knocked-out for MCU, that demonstrated no mCa2+ uptake and hence no mitochondrial swelling, however failed protect cells from I/R- mediated cell death. MCU-/- animals showed a similar infarct size comparable to that of control animals, suggesting that prevention of MCU-mediated mCa2+ overload alone is not sufficient to protect cells from Ca2+ -induced necrosis. The absence of mCa2+ entry revealed an elevation in the upstream cCa2+ transients in hepatocytes from MCUDHEP. Ultra-structural analysis of liver sections from MCU-/- (MCUDHEP) and MCUfl/fl animals revealed stark contrast in the shape of mitochondria: MCUfl/fl liver sections showed long and filamentous mitochondria (spaghetti-like) while MCUDHEP mitochondria were short and circular (donut-like). Furthermore, challenging MCUfl/fl and MCUDHEP hepatocytes with ionomycin caused a marked increase in cCa2+ and a simultaneous change in mitochondrial shape (from spaghetti to donut), a phenomenon we termed mitochondrial shape transition (MiST) that was independent of mitochondrial swelling. The cCa2+-mediated MiST is induced by an evolutionarily conserved mitochondrial surface EF-hand domain containing Miro1. Glutamate and Ca2+ -stress driven cCa2+ mobilization cause MiST in neurons that is suppressed by expression of Miro1 EF1 mutants. Miro1-dependent MiST is essential for autophagosome formation that is attenuated in cells harboring Miro1 EF1 mutants. Remarkably, loss of cCa2+ sensitization by Miro1 prevented MiST and mitigated autophagy. These results demonstrate that an interplay of ions and metabolites function in concert to regulate mitochondrial shape that in turn dictates the diverse mitochondrial processes from ATP generation to determining mechanisms of cell death.
Temple University--Theses

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Oonthonpan, Lalita. "Two human Mitochondrial Pyruvate Carrier mutations reveal distinct mechanisms of molecular pathogenesis." Diss., University of Iowa, 2019. https://ir.uiowa.edu/etd/7006.

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The Mitochondrial Pyruvate Carrier (MPC) occupies a central metabolic node by transporting cytosolic pyruvate into the mitochondrial matrix, thereby linking glycolysis with mitochondrial metabolism. Two reported human MPC1 mutations cause developmental abnormalities, neurological problems, metabolic deficits, and for one patient, early death. We aimed to understand biochemical mechanisms by which the human patient c.C289T and c.T236A MPC1 alleles disrupt MPC function. MPC1 c.C289T encodes two protein variants, a mis-spliced, truncation mutant (A58G) and full-length point mutant (R97W). MPC1 c.T236A encodes a full-length point mutant (L79H). Using human patient fibroblasts and complementation of CRISPR-deleted, MPC1 null mouse C2C12 cells, we investigated how MPC1 mutations cause MPC deficiency. Truncated MPC1 A58G protein was intrinsically unstable and failed to form MPC complexes. The MPC1 R97W protein was less stable but when overexpressed formed complexes with MPC2 that retained pyruvate transport activity. Conversely, MPC1 L79H protein formed stable complexes with MPC2, but these complexes failed to transport pyruvate. These findings inform MPC structure-function relationships and delineate three distinct biochemical pathologies resulting from human patient MPC1 mutations and inform fundamental MPC structure-function relationships. These results also demonstrate an efficient molecular genetic system using the mouse C2C12 cell line to mechanistically investigate human inborn errors in pyruvate metabolism.

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Thelen, Jay J. "Purification, characterization and molecular analysis of the mitochondrial pyruvate dehydrogenase complex from maize /." free to MU campus, to others for purchase, 1998. http://wwwlib.umi.com/cr/mo/fullcit?p9901296.

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Ghosh, Kakoli. "Molecular characterisation and expression of the E1#alpha# gene of the mitochondrial pyruvate dehydrogenase complex from potato." Thesis, University of Oxford, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.297938.

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Baggetto, Loris Gilbert. "Déviations métaboliques et génomiques mitochondriales dans les cellules tumorales glycolytiques AS30-D et Ehrlich : voie de l'acétoïne." Lyon 1, 1991. http://www.theses.fr/1991LYO10014.

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Le pyruvate est rapidement decarboxyle par les mitochondries des tumeurs d'ehrlich pour former de l'acetoine qui, si ajoutee aux mitochondries, est rapidement utilisee pour former de petites quantites d'ethanol et de citrate. Elle a aussi ete detectee dans les mitochondries as 30-d mais pas dans celles du foie de rat controle. Elle resulte de la condensation d'acetaldehyde active et d'acetaldehyde par le complexe pyruvate deshydrogenase tumoral (pdh). Elle controle le metabolisme du pyruvate par l'inhibition competitive du complexe pdh, ainsi que l'oxydation du succinate qu'elle inhibe. La forte accumulation de cholesterol dans les membranes mitochondriales entraine une diminution de la fuite passive des protons. Cette derniere, avec la presence insolite d'isozymes de la creatine kinase et la presence d'une hexokinase liee a la membrane externe de la mitochondrie alimentant la glycolyse a partir d'atp mitochondrial, contribuent a distribuer efficacement les molecules energetiques pour les besoins cellulaires comme la division. Une anomalie de la restriction de l'adn mitochondrial as 30-d accompagne ce metabolisme deviant: un des deux sites de restriction par l'enzyme xba i a disparu. Les molecules normales et mutees coexistent avec une heteroplasmie d'environ 50%

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Singh, Geetanjali. "Analysis of genetic mutations using a recombinant model of the mammalian pyruvate dehydrogenase complex." Thesis, Thesis restricted. Connect to e-thesis to view abstract, 2008. http://theses.gla.ac.uk/214/.

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Thesis (Ph.D.) - University of Glasgow, 2008.
Ph.D. thesis submitted to the Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, 2008. Includes bibliographical references. Print version also available.

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Phelps, Anne. "Structural and functional studies on two mitochondrial proteins : the pyruvate dehydrogenase complex and the phosphate carrier." Thesis, University of Glasgow, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.305594.

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Books on the topic "Pyruvate mitochondrial"

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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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Keogh, Adrian Colin. Anti-mitochondrial antigen on human biliary epithelial cells [: A study of membrane expression of dihydrolipoamide acetyltransferase sub unit of pyruvate dehydrogenase on human biliary epithelial cells]. Birmingham: University of Birmingham, 2001.

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Sherwood, Dennis, and Paul Dalby. The bioenergetics of living cells. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780198782957.003.0024.

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Living systems create order, and appear to break the Second Law. This chapter explains, and resolves, this apparent paradox, drawing on the concept of coupled reactions (as introduced in Chapters 13 and 16), as mediated by ‘energy currencies’ such as ATP and NADH. The chapter then examines the key energy-capturing systems in biological systems – glycolysis and the citric acid cycle, and also photosynthesis. Topics covered include how energy is captured in the conversion of glucose to pyruvate, the mitochondrial membrane, respiration, electron transport, ATP synthase, chloroplasts and thylakoids, photosystems I and II, and the light-independent reactions of photosynthesis.

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Book chapters on the topic "Pyruvate mitochondrial"

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Marsac, C., D. François, F. Fouque, and C. Benelli. "Pyruvate Dehydrogenase Deficiencies." In Mitochondrial Diseases, 173–84. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59884-5_13.

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Gray, Lawrence R., Alix A. J. Rouault, Lalita Oonthonpan, Adam J. Rauckhorst, Julien A. Sebag, and Eric B. Taylor. "Measuring Mitochondrial Pyruvate Oxidation." In Neuromethods, 321–38. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6890-9_16.

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Miernyk, Jan A., Barbara J. Rapp, Nancy R. David, and Douglas D. Randall. "Higher Plant Mitochondrial Pyruvate Dehydrogenase Complexes." In Plant Mitochondria, 189–97. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4899-3517-5_31.

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DeBrosse, Suzanne D., and Douglas S. Kerr. "Pyruvate Dehydrogenase Complex Deficiencies." In Mitochondrial Disorders Caused by Nuclear Genes, 301–17. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-3722-2_19.

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Miernyk, Jan A., and Douglas D. Randall. "Some Properties of Plant Mitochondrial Pyruvate Dehydrogenase Kinases." In Plant Mitochondria, 223–26. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4899-3517-5_38.

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Hansford, Richard G., Rafael Moreno-Sánchez, and James Staddon. "Regulation of Respiration and Pyruvate Dehydrogenase in Isolated Cardiac Myocytes and Hepatocytes." In Integration of Mitochondrial Function, 235–44. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2551-0_21.

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Nałęcz, Katarzyna A. "The Mitochondrial Pyruvate Carrier: The Mechanism of Substrate Binding." In Molecular Biology of Mitochondrial Transport Systems, 67–79. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78936-6_6.

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Trijbels, Frans J. M., Wim Ruitenbeek, Marjan Huizing, Udo Wendel, Jan A. M. Smeitink, and Rob C. A. Sengers. "Defects in the mitochondrial energy metabolism outside the respiratory chain and the pyruvate dehydrogenase complex." In Detection of Mitochondrial Diseases, 243–47. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-6111-8_38.

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Zaleski, Jan, Małgorzata Zaleska, and Maria Erecinska. "Possible Role of Membrane-Enzyme Interactions in Activation of Pyruvate Carboxylation and Decarboxylation in Mitochondria." In Integration of Mitochondrial Function, 325–32. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2551-0_29.

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Vary, Thomas C., Wiley W. Souba, and Christopher J. Lynch. "Regulation of Pyruvate and Amino Acid Metabolism." In Mitochondria, 117–50. New York, NY: Springer New York, 2007. http://dx.doi.org/10.1007/978-0-387-69945-5_5.

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Conference papers on the topic "Pyruvate mitochondrial"

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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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Ceribelli, Angela, Natasa Isailovic, Carolina Gorlino, Elena Generali, Maria De Santis, Giacomo Maria Guidelli, Marta Caprioli, Piercarlo Sarzi-Puttini, Minoru Satoh, and Carlo Selmi. "FRI0316 SERUM ANTI-MITOCHONDRIAL ANTIBODIES IN SYSTEMIC SCLEROSIS RECOGNIZE VARIABLE PYRUVATE DEHYDROGENASE COMPLEX ANTIGENS." In Annual European Congress of Rheumatology, EULAR 2019, Madrid, 12–15 June 2019. BMJ Publishing Group Ltd and European League Against Rheumatism, 2019. http://dx.doi.org/10.1136/annrheumdis-2019-eular.6733.

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Le, Ha Xuyen. "MPC1 is an important component of the mitochondrial pyruvate import complex in Arabidopsis thaliana." In ASPB PLANT BIOLOGY 2020. USA: ASPB, 2020. http://dx.doi.org/10.46678/pb.20.1053434.

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Bamberger, A., M. Szibor, F. N. Gellerich, T. Doenst, and M. Schwarzer. "Calcium-Controlled Cytosolic Pyruvate Supply Is Essential to Adjust Mitochondrial OXPHOS to Cardiac Power." In 52nd Annual Meeting of the German Society for Thoracic and Cardiovascular Surgery (DGTHG). Georg Thieme Verlag KG, 2023. http://dx.doi.org/10.1055/s-0043-1761688.

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Cevatemre, B., E. Dere, and E. Ulukaya. "PO-197 A possible link between the mitochondrial gatekeeper pyruvate dehydrogenase enzyme complex and EMT." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.233.

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Bader, David A., Nagireddy Putluri, Sean M. Hartig, and Sean E. McGuire. "Abstract 5431: Androgen receptor regulates the mitochondrial pyruvate carrier to fuel oncometabolism in prostate cancer." 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.am2017-5431.

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Solst, Shane R., Samuel N. Rodman, Melissa A. Fath, Eric B. Taylor, and Douglas R. Spitz. "Abstract 3527: Inhibition of mitochondrial pyruvate transport selectively sensitizes cancer cells to metabolic oxidative stress." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3527.

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Chung, Tae-Wook, Taro Hitosugi, Jun Fan, Xu Wang, Ting-Lei Gu, Johannes L. Roesel, Titus Boggon, et al. "Abstract 1257: Tyrosine phosphorylation of mitochondrial pyruvate dehydrogenase kinase 1 is important for cancer metabolism." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-1257.

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Farook, MR Yasim, D. Gonzalez, M. Sheldon, and J. Cronin. "PO-257 Loss of the mitochondrial pyruvate carrier drives ‘glutamine addiction’, a hallmark of aggressive ovarian cancers." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.289.

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Jaitin, Diego, Leanne Sayles, Tereza Goliazova, Nicholas Denko, and Alejandro Sweet-Cordero. "Abstract 1000: Oncogenic Kras inhibits mitochondrial metabolism by regulating the pyruvate dehydrogenase complex under conditions of nutrient stress." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-1000.

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Reports on the topic "Pyruvate mitochondrial"

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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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Abstract:

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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