Relevant bibliographies by topics / Cancer cachexia, metabolism, pyruvate

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Academic literature on the topic 'Cancer cachexia, metabolism, pyruvate'

Author: Grafiati
Published: 14 March 2023

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Journal articles on the topic "Cancer cachexia, metabolism, pyruvate"

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Khamoui, Andy V., Dorota Tokmina-Roszyk, Harry B. Rossiter, Gregg B. Fields, and Nishant P. Visavadiya. "Hepatic proteome analysis reveals altered mitochondrial metabolism and suppressed acyl-CoA synthetase-1 in colon-26 tumor-induced cachexia." Physiological Genomics 52, no. 5 (May 1, 2020): 203–16. http://dx.doi.org/10.1152/physiolgenomics.00124.2019.

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Cachexia is a life-threatening complication of cancer traditionally characterized by weight loss and muscle dysfunction. Cachexia, however, is a systemic disease that also involves remodeling of nonmuscle organs. The liver exerts major control over systemic metabolism, yet its role in cancer cachexia is not well understood. To advance the understanding of how the liver contributes to cancer cachexia, we used quantitative proteomics and bioinformatics to identify hepatic pathways and cellular processes dysregulated in mice with moderate and severe colon-26 tumor-induced cachexia; ~300 differentially expressed proteins identified during the induction of moderate cachexia were also differentially regulated in the transition to severe cachexia. KEGG pathway enrichment revealed representation by oxidative phosphorylation, indicating altered hepatic mitochondrial function as a common feature across cachexia severity. Glycogen catabolism was also observed in cachexic livers along with decreased pyruvate dehydrogenase protein X component (Pdhx), increased lactate dehydrogenase A chain (Ldha), and increased lactate transporter Mct1. Together this suggests altered lactate metabolism and transport in cachexic livers, which may contribute to energetically inefficient interorgan lactate cycling. Acyl-CoA synthetase-1 (ACSL1), known for activating long-chain fatty acids, was decreased in moderate and severe cachexia based on LC-MS/MS analysis and immunoblotting. ACSL1 showed strong linear relationships with percent body weight change and muscle fiber size (R2 = 0.73–0.76, P < 0.01). Mitochondrial coupling efficiency, which is compromised in cachexic livers to potentially increase energy expenditure and weight loss, also showed a linear relationship with ACSL1. Findings suggest altered mitochondrial and substrate metabolism of the liver in cancer cachexia, and possible hepatic targets for intervention.
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Mannelli, Michele, Tania Gamberi, Francesca Magherini, and Tania Fiaschi. "A Metabolic Change towards Fermentation Drives Cancer Cachexia in Myotubes." Biomedicines 9, no. 6 (June 20, 2021): 698. http://dx.doi.org/10.3390/biomedicines9060698.

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Cachexia is a disorder associated with several pathologies, including cancer. In this paper, we describe how cachexia is induced in myotubes by a metabolic shift towards fermentation, and the block of this metabolic modification prevents the onset of the cachectic phenotype. Cachectic myotubes, obtained by the treatment with conditioned medium from murine colon carcinoma cells CT26, show increased glucose uptake, decreased oxygen consumption, altered mitochondria, and increased lactate production. Interestingly, the block of glycolysis by 2-deoxy-glucose or lactate dehydrogenase inhibition by oxamate prevents the induction of cachexia, thus suggesting that this metabolic change is greatly involved in cachexia activation. The treatment with 2-deoxy-glucose or oxamate induces positive effects also in mitochondria, where mitochondrial membrane potential and pyruvate dehydrogenase activity became similar to control myotubes. Moreover, in myotubes treated with interleukin-6, cachectic phenotype is associated with a fermentative metabolism, and the inhibition of lactate dehydrogenase by oxamate prevents cachectic features. The same results have been achieved by treating myotubes with conditioned media from human colon HCT116 and human pancreatic MIAPaCa-2 cancer cell lines, thus showing that what has been observed with murine-conditioned media is a wide phenomenon. These findings demonstrate that cachexia induction in myotubes is linked with a metabolic shift towards fermentation, and inhibition of lactate formation impedes cachexia and highlights lactate dehydrogenase as a possible new tool for counteracting the onset of this pathology.
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Archid, Solass, Tempfer, Königsrainer, Adolph, Reymond, and Wilson. "Cachexia Anorexia Syndrome and Associated Metabolic Dysfunction in Peritoneal Metastasis." International Journal of Molecular Sciences 20, no. 21 (October 31, 2019): 5444. http://dx.doi.org/10.3390/ijms20215444.

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: Patients with peritoneal metastasis (PM) of gastrointestinal and gynecological origin present with a nutritional deficit characterized by increased resting energy expenditure (REE), loss of muscle mass, and protein catabolism. Progression of peritoneal metastasis, as with other advanced malignancies, is associated with cancer cachexia anorexia syndrome (CAS), involving poor appetite (anorexia), involuntary weight loss, and chronic inflammation. Eventual causes of mortality include dysfunctional metabolism and energy store exhaustion. Etiology of CAS in PM patients is multifactorial including tumor growth, host response, cytokine release, systemic inflammation, proteolysis, lipolysis, malignant small bowel obstruction, ascites, and gastrointestinal side effects of drug therapy (chemotherapy, opioids). Metabolic changes of CAS in PM relate more to a systemic inflammatory response than an adaptation to starvation. Metabolic reprogramming is required for cancer cells shed into the peritoneal cavity to resist anoikis (i.e., programmed cell death). Profound changes in hexokinase metabolism are needed to compensate ineffective oxidative phosphorylation in mitochondria. During the development of PM, hypoxia inducible factor-1α (HIF-1α) plays a key role in activating both aerobic and anaerobic glycolysis, increasing the uptake of glucose, lipid, and glutamine into cancer cells. HIF-1α upregulates hexokinase II, phosphoglycerate kinase 1 (PGK1), pyruvate dehydrogenase kinase (PDK), pyruvate kinase muscle isoenzyme 2 (PKM2), lactate dehydrogenase (LDH) and glucose transporters (GLUT) and promotes cytoplasmic glycolysis. HIF-1α also stimulates the utilization of glutamine and fatty acids as alternative energy substrates. Cancer cells in the peritoneal cavity interact with cancer-associated fibroblasts and adipocytes to meet metabolic demands and incorporate autophagy products for growth. Therapy of CAS in PM is challenging. Optimal nutritional intake alone including total parenteral nutrition is unable to reverse CAS. Pressurized intraperitoneal aerosol chemotherapy (PIPAC) stabilized nutritional status in a significant proportion of PM patients. Agents targeting the mechanisms of CAS are under development.
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Michalak, Krzysztof Piotr, Agnieszka Maćkowska-Kędziora, Bogusław Sobolewski, and Piotr Woźniak. "Key Roles of Glutamine Pathways in Reprogramming the Cancer Metabolism." Oxidative Medicine and Cellular Longevity 2015 (2015): 1–14. http://dx.doi.org/10.1155/2015/964321.

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Glutamine (GLN) is commonly known as an important metabolite used for the growth of cancer cells but the effects of its intake in cancer patients are still not clear. However, GLN is the main substrate for DNA and fatty acid synthesis. On the other hand, it reduces the oxidative stress by glutathione synthesis stimulation, stops the process of cancer cachexia, and nourishes the immunological system and the intestine epithelium, as well. The current paper deals with possible positive effects of GLN supplementation and conditions that should be fulfilled to obtain these effects. The analysis of GLN metabolism suggests that the separation of GLN and carbohydrates in the diet can minimize simultaneous supply of ATP (from glucose) and NADPH2(from glutamine) to cancer cells. It should support to a larger extent the organism to fight against the cancer rather than the cancer cells. GLN cannot be considered the effective source of ATP for cancers with the impaired oxidative phosphorylation and pyruvate dehydrogenase inhibition. GLN intake restores decreased levels of glutathione in the case of chemotherapy and radiotherapy; thus, it facilitates regeneration processes of the intestine epithelium and immunological system.
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Sharma, Raj Kumar, Santosh Kumar Bharti, Balaji Krishnamachary, Yelena Mironchik, Paul Winnard, Marie-France Penet, and Zaver M. Bhujwalla. "Abstract 6353: Metabolic changes in the spleen and pancreas induced by PDAC xenografts with or without glutamine transporter downregulation." Cancer Research 82, no. 12_Supplement (June 15, 2022): 6353. http://dx.doi.org/10.1158/1538-7445.am2022-6353.

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Abstract Introduction: Our ongoing studies are focused on characterizing metabolic changes induced in the organs of mice with cachexia-inducing Pa04C human pancreatic cancer xenografts. Because pancreatic cancer cells are glutamine dependent [1], we downregulated the glutamine transporter SLC1A5 in Pa04C cells to determine if metabolic changes induced in the spleen and pancreas by Pa04C tumors were normalized when SLC1A5 was downregulated in these tumors. Metabolic patterns were characterized using high-resolution quantitative 1H magnetic resonance spectroscopy (MRS) of spleen and pancreas tissue obtained from normal mice and mice with Pa04C tumors and mice with Pa04C tumors with SLC1A5 downregulated. Method: Patient derived cachexia-inducing Pa04C pancreatic cancer cells were lentivirally transduced to express shRNA to stably downregulate SLC1A5. Mice were euthanized once tumors were ~500 mm3, the spleen and pancreas were excised and snap frozen. Snap frozen spleen (normal n= 5, Pa04C n= 11, Pa04C_SLC1A5 n= 10) and pancreas (normal n= 4, Pa04C n= 16, Pa04C_SLC1A5 n= 10) tissue samples were pulverized for dual phase extraction. The aqueous phase was used for 1H MRS analysis. Topspin 3.5 software was used for data processing and analyses. Results and Discussion: Significant downregulation of SLC1A5 mRNA and protein was confirmed in Pa04C_SLC1A5 cells and tumors. SLC1A5 downregulation resulted in significant growth delay and attenuation of weight loss. A comparison of normal mice vs empty vector/wild type tumor (EV/WT) bearing mice identified significant changes in succinate, aspartate and fumarate in the spleen, lactate, acetate, pyruvate, methionine, asparagine, creatine, choline phosphocholine, uracil, histidine and phenylalanine in the pancreas, with leucine, isoleucine, valine, alanine, glutamate, glutamine, glutathione, glycerophosphocholine, glycine, glucose and tyrosine commonly altered in the spleen and pancreas. A comparison of normal vs Pa04C_ SLC1A5 tumor bearing mice identified similar metabolic changes in the spleen and pancreas but these were reduced. Fumarate did not change in the spleen, and of the metabolic changes common to spleen and pancreas, glutamine did not change when tumor SLC1A5 was downregulated. Metabolite changes induced only in the pancreas were also similar to normal vs EV/WT with the exception of a change in glutamine with SLC1A5 downregulation and no change in lactate. Our data highlight the profound metabolic changes in spleen and pancreas metabolism that occur with growth of a cachexia-inducing pancreatic cancer xenograft, and the impact on these metabolic patterns as a result of downregulating the glutamine transporter in these cancer cells. The metabolic patterns identified in the spleen and pancreas may provide novel targets to reduce the morbidity from cachexia. Reference: 1. Son J et al, Nature. 2013;496(7443):101-5. Citation Format: Raj Kumar Sharma, Santosh Kumar Bharti, Balaji Krishnamachary, Yelena Mironchik, Paul Winnard Jr., Marie-France Penet, Zaver M. Bhujwalla. Metabolic changes in the spleen and pancreas induced by PDAC xenografts with or without glutamine transporter downregulation [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2022; 2022 Apr 8-13. Philadelphia (PA): AACR; Cancer Res 2022;82(12_Suppl):Abstract nr 6353.
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Muranaka, Hayato, Natalie Moshayedi, Andrew Eugene Hendifar, Arsen Osipov, Veronica Placencio-Hickok, Aleksandr Stotland, Sarah Parker, Jennifer Van Eyk, Neil Bhowmick, and Jun Gong. "Plasma metabolomics to predict chemotherapy (CTX) response in advanced pancreatic cancer (PC) patients (pts) on enteral feeding for cachexia." Journal of Clinical Oncology 40, no. 4_suppl (February 1, 2022): 600. http://dx.doi.org/10.1200/jco.2022.40.4_suppl.600.

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600 Background: We evaluated the potential of plasma metabolites as predictors of response to CTX in a prospective cohort of pts who received enteral feeding for cachexia and advanced PC. Methods: The PANCAX-1 (NCT02400398) prospective trial enrolled 31 cachectic advanced PC pts to receive jejunal tube peptide-based diet for 12 weeks (wks) who were planned for palliative CTX. Out of 16 evaluable pts, 62.5% receiving enteral feeding met the primary endpoint of weight stability at 12 wks. As part of an exploratory analysis of the PANCAX-1 trial, serial blood samples were collected at 3 predefined timepoints over 12 wks of enteral feeding. Up to 219 plasma metabolites were analyzed by mass spectrometry and high-performance liquid chromatography. Analytes were compared by relative area under the curve (AUC) and differences evaluated by two-sample t-tests. The mean AUC was used in pts with metabolites measured from > 1 timepoint of collection. Pts were stratified by stable disease (SD), partial response (PR), or progressive disease (PD) as best overall response to standard CTX. Results: Of 31 pts with advanced PC prospectively enrolled for enteral feeding, there were 55 blood samples collected from 28 pts available for plasma metabolomics. 20/28 (71%) pts received first-line CTX, the majority of whom (90%) received gemcitabine-based CTX. There were 2 PRs (7%) and 10 with SD (36%) as best response to CTX. Overall, there were statistically significant differences in levels of intermediates involved in multiple metabolic pathways including glycolysis, the tricarboxylic acid (TCA) cycle, fatty acid synthesis, and nucleoside synthesis in pts with PR/SD vs. PD to CTX (all p < 0.05). When stratified by CTX regimen, PD to 5-fluorouracil-based CTX (e.g., FOLFIRINOX) was associated with decreased levels of essential amino acids (AAs, L-leucine, L-methionine, L-tryptophan) and non-essential AAs (L-arginine, L-serine, L-tyrosine, all p < 0.05). For gemcitabine-based CTX (e.g., gemcitabine/nab-paclitaxel), PD was associated with increased levels of intermediates of glycolysis (pyruvate), TCA cycle (L-glutamate), nucleoside synthesis (xanthine), and bile acid metabolism (taurocholic acid, all p < 0.05). Conclusions: We are the first to demonstrate the feasibility of plasma metabolomics in a prospective cohort of advanced PC pts on enteral feeding as their primary source of nutrition. Metabolic signatures unique to FOLFIRINOX or gemcitabine/nab-paclitaxel may be predictive of response and warrant further study.
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Dalal, Shalini. "Lipid metabolism in cancer cachexia." Annals of Palliative Medicine 8, no. 1 (January 2019): 13–23. http://dx.doi.org/10.21037/apm.2018.10.01.

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Mulligan, HD, SA Beck, and MJ Tisdale. "Lipid metabolism in cancer cachexia." British Journal of Cancer 66, no. 1 (July 1992): 57–61. http://dx.doi.org/10.1038/bjc.1992.216.

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Penna, Fabio, Riccardo Ballarò, Marc Beltrá, Serena De Lucia, and Paola Costelli. "Modulating Metabolism to Improve Cancer-Induced Muscle Wasting." Oxidative Medicine and Cellular Longevity 2018 (2018): 1–11. http://dx.doi.org/10.1155/2018/7153610.

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Muscle wasting is one of the main features of cancer cachexia, a multifactorial syndrome frequently occurring in oncologic patients. The onset of cachexia is associated with reduced tolerance and response to antineoplastic treatments, eventually leading to clinical conditions that are not compatible with survival. Among the mechanisms underlying cachexia, protein and energy dysmetabolism play a major role. In this regard, several potential treatments have been proposed, mainly on the basis of promising results obtained in preclinical models. However, at present, no treatment yet reached validation to be used in the clinical practice, although several drugs are currently tested in clinical trials for their ability to improve muscle metabolism in cancer patients. Along this line, the results obtained in both experimental and clinical studies clearly show that cachexia can be effectively approached by a multidirectional strategy targeting nutrition, inflammation, catabolism, and inactivity at the same time. In the present study, approaches aimed to modulate muscle metabolism in cachexia will be reviewed.
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Dave, Dhwani T., and Bhoomika M. Patel. "Mitochondrial Metabolism in Cancer Cachexia: Novel Drug Target." Current Drug Metabolism 20, no. 14 (February 25, 2020): 1141–53. http://dx.doi.org/10.2174/1389200220666190816162658.

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Background: Cancer cachexia is a metabolic syndrome prevalent in the majority of the advanced cancers and is associated with complications such as anorexia, early satiety, weakness, anaemia, and edema, thereby reducing performance and impairing quality of life. Skeletal muscle wasting is a characteristic feature of cancer-cachexia and mitochondria is responsible for regulating total protein turnover in skeletal muscle tissue. Methods: We carried out exhaustive search for cancer cachexia and role of mitochondria in the same in various databases. All the relevant articles were gathered and the pertinent information was extracted out and compiled which was further structured into different sub-sections. Results: Various findings on the mitochondrial alterations in connection to its disturbed normal physiology in various models of cancer-cachexia have been recently reported, suggesting a significant role of the organelle in the pathogenesis of the complications involved in the disorder. It has also been reported that reduced mitochondrial oxidative capacity is due to reduced mitochondrial biogenesis as well as altered balance between fusion and fission protein activities. Moreover, autophagy in mitochondria (termed as mitophagy) is reported to play an important role in cancer cachexia. Conclusions: The present review aims to put forth the changes occurring in mitochondria and hence explore possible targets which can be exploited in cancer-induced cachexia for treatment of such a debilitating condition.
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Dissertations / Theses on the topic "Cancer cachexia, metabolism, pyruvate"

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Michele, Mannelli. "A metabolic change towards fermentation drives cancer cachexia in myotubes." Doctoral thesis, Università di Siena, 2022. http://hdl.handle.net/11365/1211634.

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The findings reported in this thesis hihlight the pivotal role of a metabolic change towards fermentation in the induction of cancer cachexia in myotubes treated with the conditioned medium of CT26 murine colon carcinoma cell line. Particularly, cachectic myotubes manifest a reduced oxygen consumption, increased lactate production and several mitochondrial alterations including a decreased activity of PDH. Our results reveal that PDH activity restoration, achieved by glycolysis or lactic fermentation inhibition was able to prevent cancer cachexia induction and previously observed metabolic alterations. This could be due to an increased availability of pyruvate within mitochondria. In agreement, pyruvate supplementation was able to prevent cancer cachexia induction and previously observed metabolic alterations, triggering a PDH activity restoration. Thus, pyruvate supplementation could represent a new tool to counteract cancer cachexia induction and development.
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Winter, Aaron. "Protein metabolism and insulin resistance in non-small cell lung cancer cachexia." Thesis, McGill University, 2011. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=97084.

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Cancer cachexia is characterized by weight loss and insulin resistance. Previous work has shown blunted protein anabolism in insulin resistant conditions. This study tested whether hyperaminoacidemia with hyperinsulinemia elicits blunted whole-body protein anabolism in cachectic non-small cell lung cancer (NSCLC). Whole-body [13C]leucine and [3H]glucose kinetics were assessed in 8 NSCLC patients and 10 age and weight-matched controls during a euglycemic, hyperinsulinemic, clamp with isoaminoacidemia (Iso-AA), followed by hyperaminoacidemia (Hyper-AA). Glucose utilization increased from Iso-AA to Hyper-AA but was lower in NSCLC patients. During Iso-AA, protein breakdown decreased and synthesis was unchanged resulting in positive net balance that was lower in NSCLC patients. During Hyper-AA, synthesis increased but breakdown was unchanged resulting in increased net balance in both groups. In summary, weight-losing NSCLC patients demonstrate insulin resistance of whole-body glucose and protein metabolism. Physiologic hyperaminoacidemia normalized their anabolic response to that of controls and did not impair insulin sensitivity of glucose.
La perte de poids et la résistance à l'insuline caractérisent la cachexie due au cancer. Un anabolisme protéique amoindri a été démontré dans des conditions d'insulino-résistance. Cette étude a évalué si l'hyperaminoacidemie et l'hyperinsulinemie résultent en un défaut de l'anabolisme protéique corporel dans la cachexie due au cancer du poumon « non à petites cellules » (NSCLC). La cinétique des protéines ([13C]leucine) et du [3H]glucose corporels ont été évalués chez 8 patients avec NSCLC et 10 hommes en santé, d'âge et de poids similaires, à l'aide du clamp hyperinsulinique, euglycémique, isoaminoacidémique (Iso-AA), suivi d'une hyperaminoacidémie (Hyper-AA). L'utilisation du glucose a augmenté entre Iso-AA et Hyper-AA, mais il était plus bas chez les patients NSCLC. Pendant Iso-AA, la dégradation des protéines a diminué et la synthèse n'a pas changé, résultant en une balance positive moindre chez les NSCLC. En Hyper-AA, la synthèse a augmenté, mais la dégradation n'a pas changé, ce qui a augmenté davantage la balance positive, dans les deux groupes. En résumé, les patients NSCLC perdant du poids ont démontré une résistance du métabolisme glucidique et protéique à l'insuline. L'hyperaminoacidémie a normalisé leur réponse anabolique à celle des contrôles sans affecter la sensibilité du glucose à l'insuline.
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Tian, Min. "Dys-regulated Metabolism and Cardiac Dysfunction in A Mouse Model of Cancer Cachexia." The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1297196325.

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Kooshan, Zeinab. "Nanoparticle assisted small molecule delivery to target prostate cancer metabolism." Thesis, Queensland University of Technology, 2022. https://eprints.qut.edu.au/228736/1/Zeinab_Kooshan_Thesis.pdf.

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Prostate cancer is the second most diagnosed and cause of cancer-related death in Australian men. Resistance to treatment and non-specificity of the drugs is a major bottleneck for prostate cancer. Recently, nano-formulated drugs are being developed for targeted drug delivery into the cancer cells. Prostate cancer cells use aerobic glycolysis promoted by the pyruvate dehydrogenase kinase-1 (PDK1) gene for energy production. We targeted PDK1 using nano-formulations selective for prostate cancer cells and tested these using in vitro and in vivo models. Nano-conjugated Radicicol was identified as most promising drug and potential useful co-therapy agent with inhibitory effect on tumour development.
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Marco-Rius, Irene. "Preserving hyperpolarised nuclear spin order to study cancer metabolism." Thesis, University of Cambridge, 2014. https://www.repository.cam.ac.uk/handle/1810/245345.

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Monitoring the early responses of tumours to treatment is a crucial element in guiding therapy and increasing patient survival. To achieve this, we are using magnetic resonance imaging (MRI), which can provide detailed physiological information with relatively high temporal and spatial resolution. In combination with the dynamic nuclear polarisation (DNP) technique, high signal-to-noise is obtained, resulting in a powerful tool for in vivo 13C metabolic imaging. However, detection of hyperpolarised substrates is limited to a few seconds due to the exponential decay of the polarisation with the longitudinal relaxation time constant T1. This work aimed to improve the combination of hyperpolarisation and metabolic NMR/ MRI by extending the observation timescale of the technique. Working with quantum mechanical properties of the detected substrates, long lifetimes might be accessible by using the nuclear singlet configuration of two coupled nuclei. The singlet state is immune to intramolecular dipole-dipole relaxation processes, which is one of the main sources of signal decay in MRI. In favourable situations, the singlet relaxation time constant can be much longer than T1, so transfer of the polarisation into the singlet state may allow one to extend the usable time period of the nuclear hyperpolarisation. Here we studied the relaxation of hyperpolarised metabolites, including those found in the TCA cycle, and examined the possibility of extending their observation timescale by storing the polarisation in the long-lived singlet state. The polarisation remains in this state until it is eventually required for imaging. We also investigate how one may track polarised metabolites after injection into a subject due to the transfer of polarisation to the solvent by Overhauser cross-relaxation, so that the 13C polarisation remains untouched until imaging is required. In this way we should be able to interrogate slower metabolic processes than have been examined hitherto using hyperpolarised 13C MRS, and better understand metabolic changes induced in tumours by treatment.
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Schäfer, Michaela [Verfasser], and Stephan [Akademischer Betreuer] Herzig. "Tumor-borne mediators trigger heart atrophy and alter cardiac metabolism in cancer cachexia / Michaela Schäfer ; Betreuer: Stephan Herzig." Heidelberg : Universitätsbibliothek Heidelberg, 2015. http://d-nb.info/1180607945/34.

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Mehrfar, Parisa. "Biological markers of weight loss and muscle protein metabolism in early non-small cell lung cancer." Thesis, McGill University, 2008. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=116069.

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The loss of muscle mass leading to cachexia is rarely identified in early lung cancer. Fasting blood and muscle biopsy were collected in 59 non-small cell lung cancer (NSCLC) and 16 non-cancer patients, at the beginning of thoracic surgery. Serum C-reactive protein (CRP), and IL-6 were higher in NSCLC. In weight-losing NSCLC, food intake and serum albumin were lower, CRP, and TNF-alpha were higher. Although the expression of genes of the ubiquitin-proteasome system was not different, ubiquitinated-protein levels were lower and negatively correlated with ph-FOX01 in weight-losing patients. This would suggest lower muscle proteolytic rates in the early stages of NSCLC. Ph-FOXO1 also related to the degree of weight loss and stage of NSCLC. These data suggest that in early stages of the disease, weight and muscle loss could be mainly due to reduced food intake, rather than accelerated proteolysis, which reinforces the potential for successful dietary interventions to prevent or delay the onset of cachexia.
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Wojtkowiak, Jonathan W., Heather C. Cornnell, Shingo Matsumoto, Keita Saito, Yoichi Takakusagi, Prasanta Dutta, Munju Kim, et al. "Pyruvate sensitizes pancreatic tumors to hypoxia-activated prodrug TH-302." BioMed Central, 2016. http://hdl.handle.net/10150/610264.

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BACKGROUND: Hypoxic niches in solid tumors harbor therapy-resistant cells. Hypoxia-activated prodrugs (HAPs) have been designed to overcome this resistance and, to date, have begun to show clinical efficacy. However, clinical HAPs activity could be improved. In this study, we sought to identify non-pharmacological methods to acutely exacerbate tumor hypoxia to increase TH-302 activity in pancreatic ductal adenocarcinoma (PDAC) tumor models. RESULTS: Three human PDAC cell lines with varying sensitivity to TH-302 (Hs766t > MiaPaCa-2 > SU.86.86) were used to establish PDAC xenograft models. PDAC cells were metabolically profiled in vitro and in vivo using the Seahorse XF system and hyperpolarized 13C pyruvate MRI, respectively, in addition to quantitative immunohistochemistry. The effect of exogenous pyruvate on tumor oxygenation was determined using electroparamagnetic resonance (EPR) oxygen imaging. Hs766t and MiaPaCa-2 cells exhibited a glycolytic phenotype in comparison to TH-302 resistant line SU.86.86. Supporting this observation is a higher lactate/pyruvate ratio in Hs766t and MiaPaCa xenografts as observed during hyperpolarized pyruvate MRI studies in vivo. Coincidentally, response to exogenous pyruvate both in vitro (Seahorse oxygen consumption) and in vivo (EPR oxygen imaging) was greatest in Hs766t and MiaPaCa models, possibly due to a higher mitochondrial reserve capacity. Changes in oxygen consumption and in vivo hypoxic status to pyruvate were limited in the SU.86.86 model. Combination therapy of pyruvate plus TH-302 in vivo significantly decreased tumor growth and increased survival in the MiaPaCa model and improved survival in Hs766t tumors. CONCLUSIONS: Using metabolic profiling, functional imaging, and computational modeling, we show improved TH-302 activity by transiently increasing tumor hypoxia metabolically with exogenous pyruvate. Additionally, this work identified a set of biomarkers that may be used clinically to predict which tumors will be most responsive to pyruvate + TH-302 combination therapy. The results of this study support the concept that acute increases in tumor hypoxia can be beneficial for improving the clinical efficacy of HAPs and can positively impact the future treatment of PDAC and other cancers.
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Martin, Agnès. "Role of the glucocorticoid pathway in skeletal muscle wasting and hepatic metabolism rewiring during cancer cachexia in ApcMin/+ mice – Functional implication of myostatin gene invalidation." Thesis, Lyon, 2020. http://www.theses.fr/2020LYSES034.

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La cachexie affecte environ la moitié des patients atteints d’un cancer et est caractérisée par une perte progressive de la masse corporelle résultant principalement d’une perte de masse musculaire squelettique. Cette perte de masse musculaire squelettique associée à une perte de force musculaire contribue fortement à réduire la qualité de vie des patients, l’efficacité des traitements et à terme, la survie des patients. Plusieurs facteurs sont connus pour être impliqués dans la régulation de la masse musculaire. Parmi eux, les glucocorticoïdes sont des hormones stéroïdiennes sécrétées sous le contrôle de l’axe hypothalamo-hypophysaire qui sont connues pour induire l’atrophie musculaire mais aussi pour avoir une action systémique via l’activation ou l’expression de gènes dans plusieurs tissus. Nous faisons l’hypothèse que la voie des glucocorticoïdes pourrait être activée pendant la cachexie associée au cancer dans les souris ApcMin/+, un model murin de cancer intestinal. Nous rapportons ici que l’activation du catabolisme musculaire était associée à une reprogrammation complète du métabolisme du foie. En outre, nous montrons une activation de l’axe hypothalamo-hypophysaire associée à une augmentation du niveau en corticostérone (le glucocorticoïde principal chez les rongeurs) dans le sérum, le muscle quadriceps et le foie des souris à un stade avancé de la cachexie associée au cancer. La signature transcriptionnelle dans le muscle quadriceps et le foie des souris à un stade avancé de la cachexie associée au cancer reflète celle observée dans des souris traitées avec de la dexaméthasone, un analogue des glucocorticoïdes. Il est important de souligner que l’inhibition de la cachexie associée au cancer par l’inactivation du gène de la myostatine dans les souris ApcMin/+ a restauré les niveaux en corticostérone et abolit la reprogrammation génique dans le muscle squelettique et le foie. Ensemble, ces données indiquent que les glucocorticoïdes induisent un programme transcriptionnel pour réguler de façon coordonnée la perte de masse musculaire et le remaniement du métabolisme hépatique. L’inhibition de cette réponse par l’invalidation du gène de la myostatine souligne l’existence d’un dialogue moléculaire entre le muscle squelettique et le foie
Cachexia affects about half of cancer patients and is characterized by a progressive body mass loss mainly resulting from skeletal muscle depletion. This loss of skeletal muscle mass together with a decrease in muscle force strongly contribute to reduce cancer patient quality of life, treatment efficiency and ultimately patient survival. Many factors are known to be involved in the regulation of skeletal muscle homeostasis. Among them, glucocorticoids are steroid hormones secreted under the control of the hypothalamic-pituitary axis that have been well described to promote skeletal muscle atrophy but also to exert systemic actions through activation or repression of gene expression in many tissues. We hypothesized that the glucocorticoid pathway could be activated during cancer cachexia in ApcMin/+ mice, a mouse model of intestinal cancer. Here, we reported that activation of skeletal muscle catabolism was associated with a complete reprogramming of liver metabolism. Moreover, we showed an activation of the hypothalamus-pituitary axis that was associated with an increase in the level of corticosterone (the main glucocorticoid in rodent) in serum, quadriceps muscle and liver of advanced cancer cachectic mice. The transcriptional signature in quadriceps muscle and liver of advanced cancer cachectic mice significantly mirrored that observed in mice treated with dexamethasone, an analog glucocorticoid. Importantly, the inhibition of cancer cachexia by myostatin gene invalidation in ApcMin/+ mice restored corticosterone levels and abolished skeletal muscle and liver gene reprogramming. Together, these data indicate that glucocorticoids drive a transcriptional program to coordinately regulate skeletal muscle mass loss and hepatic metabolism rewiring. The inhibition of this response by myostatin gene invalidation highlights the existence of a molecular dialog between skeletal muscle and liver
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Subramaniam, Sugarniya. "Expression, function, and regulation of two key genes involved in prostate cancer metabolism." Thesis, Queensland University of Technology, 2020. https://eprints.qut.edu.au/200151/1/Sugarniya_Subramaniam_Thesis.pdf.

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Metabolic deregulation is an emergent hallmark of prostate cancer and studies show that altered patterns of metabolic pathways involved in the development of malignancy. A large genetic association on microRNA (miRNA) related genetic variations recently identified single nucleotide polymorphisms (SNPs) in two key metabolic genes. This thesis analysed the role of metabolic genes and functional validation of SNPs and associated miRNAs involved in the regulation of these genes as a mediator of prostate cancer aetiology. The findings from this study suggest that studies of miRNAs and their interactions with SNPs could provide valuable insights into the complicated mechanisms of prostate cancer risk and identify suitable molecular pathways for targeted therapy.
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Books on the topic "Cancer cachexia, metabolism, pyruvate"

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Pisters, Peter W. T., and Murray F. Brennan. Protein and Amino Acid Metabolism in Cancer Cachexia. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-22346-8.

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T, Pisters Peter W., and Brennan Murray F, eds. Protein and amino acid metabolism in cancer cachexia. New York: Springer, 1996.

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Pisters, Peter W. T., 1960- and Brennan Murray F, eds. Protein and amino acid metabolism in cancer cachexia. New York: Chapman & Hall, 1996.

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F, Bozzetti, Dionigi R, Moore Francis D. 1913-, and Fürst P, eds. Nutrition in cancer and trauma sepsis: Proceedings of the 6th Congress of the European Society of Parenteral and Enteral Nutrition (ESPEN), Milan, October 1-3, 1984. Basel ; New York: Karger, 1985.

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Pisters, Peter W. T., and Murray F. Brennan. Protein and Amino Acid Metabolism in Cancer Cachexia. Springer London, Limited, 2013.

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Pisters, Peter W. T. Protein and Amino Acid Metabolism in Cancer Cachexia. Springer, 2013.

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Pisters, Peter W. T., and Murray F. Brennan. Protein and Amino Acid Metabolism in Cancer Cachexia (Medical Intelligence Unit). Landes Bioscience, 1995.

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Book chapters on the topic "Cancer cachexia, metabolism, pyruvate"

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Bode, Barrie P., Craig Fischer, Steven Abcouwer, Masafumi Wasa, and Wiley W. Souba. "Glutamine and Cancer Cachexia." In Protein and Amino Acid Metabolism in Cancer Cachexia, 139–70. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-22346-8_11.

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Billingsley, Kevin G., and H. Richard Alexander. "Cytokines in Cancer Cachexia." In Protein and Amino Acid Metabolism in Cancer Cachexia, 51–72. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-22346-8_4.

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Harrison, Lawrence E. "Animal Models of Cancer Cachexia." In Protein and Amino Acid Metabolism in Cancer Cachexia, 1–19. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-22346-8_1.

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Hochwald, Steven, and Martin Heslin. "Plasma Amino Acid Concentrations in Cancer Cachexia." In Protein and Amino Acid Metabolism in Cancer Cachexia, 73–82. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-22346-8_5.

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Newman, Elliot, and Steven Hochwald. "Regional Amino Acid Studies in Cancer Cachexia." In Protein and Amino Acid Metabolism in Cancer Cachexia, 93–111. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-22346-8_7.

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Pisters, Peter W. T., and Murray F. Brennan. "Enteral Nutrition in Cancer." In Protein and Amino Acid Metabolism in Cancer Cachexia, 133–38. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-22346-8_10.

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Pisters, Peter W. T., and Murray F. Brennan. "Total Parenteral Nutrition in Cancer." In Protein and Amino Acid Metabolism in Cancer Cachexia, 123–32. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-22346-8_9.

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Berman, Russell S. "Whole Body Amino Acid Studies in Cancer Cachexia." In Protein and Amino Acid Metabolism in Cancer Cachexia, 113–21. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-22346-8_8.

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Gomes-Marcondes, Maria Cristina Cintra, and Emilianne Miguel Salomão. "Combining Exercise with Glutamine Supplementation in Cancer-Cachexia Metabolism." In Glutamine in Clinical Nutrition, 487–98. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1932-1_37.

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Heslin, Martin J. "Insulin to Impact on Protein and Amino Acid Metabolism." In Protein and Amino Acid Metabolism in Cancer Cachexia, 187–99. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-22346-8_13.

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Conference papers on the topic "Cancer cachexia, metabolism, pyruvate"

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Sharma, Raj Kumar, Santosh K. Bharti, Paul T. Winnard, Marie-France Penet, and Zaver M. Bhujwalla. "Abstract 1625: Lung and kidney metabolism altered by cancer-induced cachexia." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-1625.

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Bankson, James A., Christopher M. Walker, Yunyun Chen, Stephen Y. Lai, and John D. Hazle. "Abstract B51: Metabolic imaging with hyperpolarized [1-13C]-pyruvate and DCE-MRI." In Abstracts: AACR Special Conference: Metabolism and Cancer; June 7-10, 2015; Bellevue, WA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1557-3125.metca15-b51.

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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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Prakasam, Gopinath, and Rameshwar N. K. Bamezai. "Abstract B19: LKB1-AMPK axis regulates the switch of Pyruvate Kinase M isoforms to tolerate nutritional stress." In Abstracts: AACR Special Conference: Metabolism and Cancer; June 7-10, 2015; Bellevue, WA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1557-3125.metca15-b19.

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Cerniglia, George, Souvik Dey, Shannon M. Gallagher-Colombo, Natalie Daurio, Stephen Tuttle, Theresa M. Busch, Alexander Lin, et al. "Abstract B05: PI3K/mTOR pathway-dependent regulation of oxygen metabolism via pyruvate dehydrogenase (PDH)-E1alpha phosphorylation." In Abstracts: AACR Special Conference: Targeting the PI3K-mTOR Network in Cancer; September 14-17, 2014; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-8514.pi3k14-b05.

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Kimura, Tetsuo, Priya Bhardwaj, Domenick J. Falcone, Andrew J. Dannenberg, and Kotha Subbaramaiah. "Abstract B36: Pyruvate kinase M2 regulates adipocyte differentiation and the expression of enzymes involved in glucose metabolism." In Abstracts: Thirteenth Annual AACR International Conference on Frontiers in Cancer Prevention Research; September 27 - October 1, 2014; New Orleans, LA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1940-6215.prev-14-b36.

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Chen, Jing, Taro Hitosugi, Jun Fan, Sumin Kang, Ting-Lei Gu, and Titus Boggon. "Abstract 997: Oncogenic tyrosine kinases are localized to mitochondria and regulate cancer metabolism by phosphorylating key components of pyruvate dehydrogenase kinase complex." 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.am2012-997.

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Guda, Maheedhara R., Swapna Asuthkar, Soumen Das, Sudipta Seal, Andrew J. Tsung, and Kiran K. Velpula. "Abstract 1920: miR-211 directly targets pyruvate dehydrogenase kinase 4 to inhibit cellular growth and glucose metabolism in triple negative breast cancer." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1920.

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Moore, Jonathan, Anna Staniszewska, Terence Shaw, Jalanie D'Alessandro, Ben Davis, Alan Surgenor, Lisa Baker, et al. "Abstract B155: VER-246608, a novel pan-isoform ATP competitive inhibitor of pyruvate dehydrogenase kinase, disrupts Warburg metabolism and demonstrates context-dependent cytotoxicity to cancer cells." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Oct 19-23, 2013; Boston, MA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1535-7163.targ-13-b155.

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Angelotti, Austin, Rachel Cole, Amy Webb, Maciej Pietrzak, and Martha Belury. "Diet-induced Gene Expression Changes of Cachectic Muscle, Adipose, and Liver." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/gvbe2596.

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Abstract:
Cancer cachexia is a systemic disease characterized by muscle and adipose loss that cannot be reversed by increasing caloric intake. Our previous research has shown insulin resistance precedes cancer cachexia in the C26 mouse model of cachexia, and a diet high in linoleic acid, the essential omega-6 polyunsaturated fatty acid, attenuates the C26-induced insulin resistance. Therefore, to better understand how dietary linoleic acid is improving insulin sensitivity, we characterized gene expression changes in three major tissues responsible for controlling insulin sensitivity: skeletal muscle, adipose, and liver. To do this male CD2F1 (Charles River, MA) were randomized to semi-purified diet (24% fat by weight) containing fat prominently from lard, or containing fat prominently from safflower oil (a linoleic acid-rich oil). One week after diet randomization, mice were inoculated with colon-26 (C26) adenocarcinoma cells (1.0E6 cells). 13 days after inoculation mice were euthanized and gastrocnemius skeletal muscle, epididymal white adipose tissue, and liver tissue were collected for total transcriptome analysis using poly-A enriched next generation RNA-sequencing. Differentially expressed genes were selected based on p-values < 0.05. There were no detectable differences in body weight or food intake between the two diets in mice with C26 tumors. Between the two diets 12 genes were differentially expressed in the muscle, while 57 genes were differentially expressed in the liver, and 314 genes were differentially expressed in adipose. A linoleic acid enriched diet had little effect on the skeletal muscle transcriptome but induced larger transcriptome changes in liver and adipose. This could suggest dietary linoleic acid increases insulin sensitivity through affecting metabolism in adipose and liver, rather than skeletal muscle. Determining these diet-induced transcriptome changes allows us to better target tissue-specific molecular mechanisms of linoleic acid in future research.
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