Cited by 150Biochemical Acid Research StudiesMetabolism, Diabetes, and CancerMitochondrial Function and Pathology

The DOI matches its Crossref record; 97 of the 97 references it cites were found in a registry or an index.

Anaplerotic roles of pyruvate carboxylase in mammalian tissues

Open access

Jitrapakdee, S., Vidal-Puig, A., Wallace, J. C.·2006·Cellular and Molecular Life Sciences

DOI 10.1007/s00018-005-5410-yPMC PMC11136034

Open this paper in CoChat — free account

Abstract

Pyruvate carboxylase (PC) catalyzes the ATP-dependent carboxylation of pyruvate to oxaloacetate. PC serves an anaplerotic role for the tricarboxylic acid cycle, when intermediates are removed for different biosynthetic purposes. In liver and kidney, PC provides oxaloacetate for gluconeogenesis. In adipocytes PC is involved in de novo fatty acid synthesis and glyceroneogenesis, and is regulated by the peroxisome proliferator-activated receptor-gamma, suggesting that PC is involved in the metabolic switch controlling fuel partitioning toward lipogenesis. In islets, PC is necessary for glucose-induced insulin secretion by providing oxaloacetate to form malate that participates in the 'pyruvate/malate cycle' to shuttle 3C or 4C between mitochondria and cytoplasm. Hyperglycemia and hyperlipidemia impair this cycle and affect glucose-stimulated insulin release. In astrocytes, PC is important for de novo synthesis of glutamate, an important excitatory neurotransmitter supplied to neurons. Transcriptional studies of the PC gene pinpoint some transcription factors that determine tissue-specific expression.

Integrity signals

Registry

Crossref · 10.1007/s00018-005-5410-y

Cites

97 of 97 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Brown Adipose Tissue: Function and Physiological Significance
CANNON, B., & NEDERGAARD, J. (2004) · Physiological Reviews · doi:10.1152/physrev.00015.2003 · Cited by 6,433
Insulin signalling and the regulation of glucose and lipid metabolism
Saltiel, A. R., & Kahn, C. R. (2001) · Nature · doi:10.1038/414799a · Cited by 5,326
Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244
Transcriptional regulation by the phosphorylation-dependent factor CREB
Mayr, B., & Montminy, M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35085068 · Cited by 2,587
CREB regulates hepatic gluconeogenesis through the coactivator PGC-1
Herzig, S., Long, F., Jhala, U. S., Hedrick, S., Quinn, R., Bauer, A., Rudolph, D., Schutz, G., Yoon, C., Puigserver, P., et al. (2001) · Nature · doi:10.1038/35093131 · Cited by 1,440
Molecular Regulation of Adipogenesis
Rosen, E. D., & Spiegelman, B. M. (2000) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.16.1.145 · Cited by 1,310
Fatty acid-induced β cell apoptosis: A link between obesity and diabetes
Shimabukuro, M., Zhou, Y.-T., Levi, M., & Unger, R. H. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2498 · Cited by 1,142
Glucose induces closure of single potassium channels in isolated rat pancreatic β-cells
Ashcroft, F. M., Harrison, D. E., & Ashcroft, S. J. H. (1984) · Nature · doi:10.1038/312446a0 · Cited by 1,113
Biochemistry and physiology of brain ammonia.
Cooper, A. J. L., & Plum, F. (1987) · Physiological Reviews · doi:10.1152/physrev.1987.67.2.440 · Cited by 841
Minireview: Secondary β-Cell Failure in Type 2 Diabetes—A Convergence of Glucotoxicity and Lipotoxicity
Poitout, V., & Robertson, R. P. (2002) · Endocrinology · doi:10.1210/endo.143.2.8623 · Cited by 743

Show all 97 references

Sorted by citations

Glutamine blockade induces divergent metabolic programs to overcome tumor immune evasion
Leone, R. D., Zhao, L., Englert, J. M., Sun, I.-M., Oh, M.-H., Sun, I.-H., Arwood, M. L., Bettencourt, I. A., Patel, C. H., Wen, J., et al. (2019) · Science · doi:10.1126/science.aav2588 · Cited by 1,169
Lactate: the ugly duckling of energy metabolism
Rabinowitz, J. D., & Enerbäck, S. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0243-4 · Cited by 1,140
Glutamine reliance in cell metabolism
Yoo, H. C., Yu, Y. C., Sung, Y., & Han, J. M. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-00504-8 · Cited by 1,021
Reprogramming of the Circadian Clock by Nutritional Challenge
Eckel‐Mahan, K. L., Patel, V. R., de Mateo, S., Orozco-Solís, R., Ceglia, N., Sahar, S., Dilag-Penilla, S. A., Dyar, K. A., Baldi, P., & Sassone‐Corsi, P. (2013) · Cell · doi:10.1016/j.cell.2013.11.034 · Cited by 737
Induction of metastasis, cancer stem cell phenotype, and oncogenic metabolism in cancer cells by ionizing radiation
Lee, S. Y., Jeong, E. K., Ju, M. K., Jeon, H. M., Kim, M. Y., Kim, C. H., Park, H. G., Han, S. I., & Kang, H. S. (2017) · Molecular Cancer · doi:10.1186/s12943-016-0577-4 · Cited by 592
Gluconeogenesis in dairy cows: The secret of making sweet milk from sour dough
Aschenbach, J. R., Kristensen, N. B., Donkin, S. S., Hammon, H. M., & Penner, G. B. (2010) · IUBMB Life · doi:10.1002/iub.400 · Cited by 529
Structure and function of biotin-dependent carboxylases
Tong, L. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1096-0 · Cited by 492
Nrf2–MafG heterodimers contribute globally to antioxidant and metabolic networks
Hirotsu, Y., Katsuoka, F., Funayama, R., Nagashima, T., Nishida, Y., Nakayama, K., Engel, J. D., & Yamamoto, M. P. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks827 · Cited by 431
Effective breast cancer combination therapy targeting BACH1 and mitochondrial metabolism
Lee, J., Yesilkanal, A. E., Wynne, J. P., Frankenberger, C. A., Liu, J., Yan, J., Elbaz, M., Rabe, D. C., Rustandy, F. D., Tiwari, P., et al. (2019) · Nature · doi:10.1038/s41586-019-1005-x · Cited by 381
Ketogenic Diet for Obesity: Friend or Foe?
Paoli, A. (2014) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph110202092 · Cited by 380
Metabolic adaptation in hypoxia and cancer
Paredes, F., Williams, H. C., & Martín, A. S. (2021) · Cancer Letters · doi:10.1016/j.canlet.2020.12.020 · Cited by 276
Ketosis, ketogenic diet and food intake control: a complex relationship
Paoli, A., Bosco, G., Camporesi, E. M., & Mangar, D. (2015) · Frontiers in Psychology · doi:10.3389/fpsyg.2015.00027 · Cited by 270
Regulation of Tumor Progression by Programmed Necrosis
Lee, S. Y., Ju, M. K., Jeon, H. M., Jeong, E. K., Lee, Y. J., Kim, C. H., Park, H. G., Han, S. I., & Kang, H. S. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/3537471 · Cited by 238
Ketogenic Diet in Neuromuscular and Neurodegenerative Diseases
Paoli, A., Bianco, A., Damiani, E., & Bosco, G. (2014) · BioMed Research International · doi:10.1155/2014/474296 · Cited by 221
Transcription factors and coactivators controlling nutrient and hormonal regulation of hepatic gluconeogenesis
Jitrapakdee, S. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.10.001 · Cited by 202
Self-citation
Wnt/Snail Signaling Regulates Cytochrome c Oxidase and Glucose Metabolism
Lee, S. Y., Jeon, H. M., Ju, M. K., Kim, C. H., Yoon, G., Han, S. I., Park, H. G., & Kang, H. S. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-0006 · Cited by 197
Carnitine, mitochondrial function and therapy
Zammit, V. A., Ramsay, R. R., Bonomini, M., & Arduini, A. (2009) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2009.04.024 · Cited by 149
Targeting Pyruvate Carboxylase Reduces Gluconeogenesis and Adiposity and Improves Insulin Resistance
Kumashiro, N., Beddow, S. A., Vatner, D. F., Majumdar, S. K., Cantley, J. L., Guebre‐Egziabher, F., Fat, I., Guigni, B. A., Jurczak, M. J., Birkenfeld, A. L., et al. (2013) · Diabetes · doi:10.2337/db12-1311 · Cited by 157
Rosmarinus officinalis polyphenols produce anti-depressant like effect through monoaminergic and cholinergic functions modulation
Sasaki, K., Omri, A. E., Kondo, S., Han, J., & Isoda, H. (2012) · Behavioural Brain Research · doi:10.1016/j.bbr.2012.10.010 · Cited by 152
Domain Architecture of Pyruvate Carboxylase, a Biotin-Dependent Multifunctional Enzyme
Maurice, M. S., Reinhardt, L. A., Surinya, K. H., Attwood, P. V., Wallace, J. C., Cleland, W. W., & Rayment, I. (2007) · Science · doi:10.1126/science.1144504 · Cited by 151
Self-citation
The Role of TCA Cycle Anaplerosis in Ketosis and Fatty Liver in Periparturient Dairy Cows
White, H. M. (2015) · Animals · doi:10.3390/ani5030384 · Cited by 148
Compensatory Responses to Pyruvate Carboxylase Suppression in Islet β-Cells
Jensen, M. V., Joseph, J. W., Ilkayeva, O., Burgess, S. C., Lu, D., Ronnebaum, S. M., Odegaard, M. L., Becker, T. C., Sherry, A. D., & Newgard, C. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604350200 · Cited by 144
Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction
Xiang, S., & Tong, L. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1393 · Cited by 139
The Flavonoid Kaempferol Ameliorates Streptozotocin-Induced Diabetes by Suppressing Hepatic Glucose Production
Alkhalidy, H., Moore, W., Wang, Y., Luo, J., McMillan, R. P., Wei, Z., Zhou, K., & Liu, D. (2018) · Molecules · doi:10.3390/molecules23092338 · Cited by 142
Small-Molecule Fluorescent Probes for Binding- and Activity-Based Sensing of Redox-Active Biological Metals
Grover, K., Koblova, A., Pezacki, A. T., Chang, C. J., & New, E. J. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00819 · Cited by 129
Pyruvate carboxylase and cancer progression
Kiesel, V. A., Sheeley, M. P., Coleman, M. F., Kulkoyluoglu‐Cotul, E., Donkin, S. S., Hursting, S. D., Wendt, M. K., & Teegarden, D. (2021) · Cancer & Metabolism · doi:10.1186/s40170-021-00256-7 · Cited by 131
Mitochondrial dysfunctions in cancer: Genetic defects and oncogenic signaling impinging on TCA cycle activity
Desideri, E., Vegliante, R., & Ciriolo, M. R. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.02.023 · Cited by 116
Impact of mitochondrial calcium on the coupling of metabolism to insulin secretion in the pancreatic β-cell
Wiederkehr, A., & Wollheim, C. B. (2008) · Cell Calcium · doi:10.1016/j.ceca.2007.11.004 · Cited by 102
Nutrition and Acne: Therapeutic Potential of Ketogenic Diets
Paoli, A., Grimaldi, K. A., Toniolo, L., Canato, M., Bianco, A., & Fratter, A. (2012) · Skin Pharmacology and Physiology · doi:10.1159/000336404 · Cited by 100
Impaired anaplerosis and insulin secretion in insulinoma cells caused by small interfering RNA-mediated suppression of pyruvate carboxylase.
Hasan, N. M., Longacre, M. J., Stoker, S. W., Boonsaen, T., Jitrapakdee, S., Kendrick, M. A., Wallace, J. C., & MacDonald, M. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804170200 · Cited by 88
Self-citation
Roles of pyruvate carboxylase in human diseases: from diabetes to cancers and infection
Lao-On, U., Attwood, P. V., & Jitrapakdee, S. (2018) · Journal of Molecular Medicine · doi:10.1007/s00109-018-1622-0 · Cited by 85
Self-citation
Regulation of the structure and activity of pyruvate carboxylase by acetyl CoA
Adina-Zada, A., Zeczycki, T. N., & Attwood, P. V. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.11.015 · Cited by 84
Roles of Pyruvate, NADH, and Mitochondrial Complex I in Redox Balance and Imbalance inβCell Function and Dysfunction
Luo, X., Li, R., & Yan, L. (2015) · Journal of Diabetes Research · doi:10.1155/2015/512618 · Cited by 81
H2S-induced S-sulfhydration of pyruvate carboxylase contributes to gluconeogenesis in liver cells
Ju, Y., Untereiner, A. A., Wu, L., & Yang, G. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.08.003 · Cited by 76
MicroRNAs and oncogenic transcriptional regulatory networks controlling metabolic reprogramming in cancers
Pinweha, P., Rattanapornsompong, K., Charoensawan, V., & Jitrapakdee, S. (2016) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2016.05.005 · Cited by 75
Self-citation
Comprehensive and quantitative proteome profiling of the mouse liver and plasma
Lai, K. K. Y., Kolippakkam, D. N., & Beretta, L. (2008) · Hepatology · doi:10.1002/hep.22123 · Cited by 69
Dynamic Acetylation of Phosphoenolpyruvate Carboxykinase Toggles Enzyme Activity between Gluconeogenic and Anaplerotic Reactions
Latorre‐Muro, P., Baeza, J., Armstrong, E. A., Hurtado‐Guerrero, R., Corzana, F., Wu, L. E., Sinclair, D. A., López‐Buesa, P., Carrodeguas, J. A., & Denu, J. M. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.07.031 · Cited by 68
Oncogenic Metabolism Acts as a Prerequisite Step for Induction of Cancer Metastasis and Cancer Stem Cell Phenotype
Lee, S. Y., Ju, M. K., Jeon, H. M., Lee, Y. J., Kim, C. H., Park, H. G., Han, S. I., & Kang, H. S. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1027453 · Cited by 69
Plasma and urine metabolic fingerprinting of type 1 diabetic children
Balderas, C., Rupérez, F. J., Ibáñez, E., Señorans, J., Guerrero-Fernández, J., Casado, I. G., Gracia‐Bouthelier, R., Garcı́a, A., & Barbas, C. (2013) · Electrophoresis · doi:10.1002/elps.201300062 · Cited by 67
A Symmetrical Tetramer for S. aureus Pyruvate Carboxylase in Complex with Coenzyme A
Yu, L. P. C., Xiang, S., Lasso, G., Gil‐Carton, D., Valle, M., & Tong, L. (2009) · Structure · doi:10.1016/j.str.2009.04.008 · Cited by 65
CO2 – Intrinsic Product, Essential Substrate, and Regulatory Trigger of Microbial and Mammalian Production Processes
Blombach, B., & Takors, R. (2015) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2015.00108 · Cited by 65
Prohibitin has an important role in adipocyte differentiation
Ande, S. R., Xu, Z., Gu, Y., & Mishra, S. (2011) · International Journal of Obesity · doi:10.1038/ijo.2011.227 · Cited by 66
Glial Dysfunction Causes Age-Related Memory Impairment in Drosophila
Yamazaki, D., Horiuchi, J., Ueno, K., Ueno, T., Saeki, S., Matsuno, M., Naganos, S., Miyashita, T., Hirano, Y., Nishikawa, H., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.09.039 · Cited by 66
Metabolomic and microarray analyses of adipose tissue of dapagliflozin-treated mice, and effects of 3-hydroxybutyrate on induction of adiponectin in adipocytes
Nishitani, S., Fukuhara, A., Shin, J., Okuno, Y., Otsuki, M., & Shimomura, I. (2018) · Scientific Reports · doi:10.1038/s41598-018-27181-y · Cited by 61
Contribution of PGC-1α to Obesity- and Caloric Restriction-Related Physiological Changes in White Adipose Tissue
Kobayashi, M., Deguchi, Y., Nozaki, Y., & Higami, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116025 · Cited by 63
Differential responses of white adipose tissue and brown adipose tissue to caloric restriction in rats
Okita, N., Hayashida, Y., Kojima, Y., Fukushima, M., Yuguchi, K., Mikami, K., Yamauchi, A., Watanabe, K., Noguchi, M., Nakamura, M., et al. (2012) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2012.02.003 · Cited by 57
Phosphoenolpyruvate Carboxylase Identified as a Key Enzyme in Erythrocytic Plasmodium falciparum Carbon Metabolism
Storm, J., Sethia, S., Blackburn, G., Chokkathukalam, A., Watson, D., Breitling, R., Coombs, G., & Müller, S. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1003876 · Cited by 54
Changes in energy metabolism induced by fluoride: Insights from inside the mitochondria
Araújo, T. T., Pereira, H. A. B. S., Dionizio, A. S., Sanchez, C. D. C., Carvalho, T. D. S., Fernandes, M. D. S., & Buzalaf, M. A. R. (2019) · Chemosphere · doi:10.1016/j.chemosphere.2019.124357 · Cited by 53
Influence of dietary conjugated linoleic acids and vitamin E on meat quality, and adipose tissue in rabbits
Corino, C., Fiego, D. P. L., Macchioni, P., Pastorelli, G., Giancamillo, A. D., Domeneghini, C., & Rossi, R. (2006) · Meat Science · doi:10.1016/j.meatsci.2006.10.007 · Cited by 53
Proteomics of human mitochondria
Palmfeldt, J., & Bross, P. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.07.006 · Cited by 55
Metabolic flux model for an anchorage‐dependent MDCK cell line: Characteristic growth phases and minimum substrate consumption flux distribution
Wahl, A., Sidorenko, Y., Dauner, M., Genzel, Y., & Reichl, U. (2008) · Biotechnology and Bioengineering · doi:10.1002/bit.21873 · Cited by 51
Interaction between the Biotin Carboxyl Carrier Domain and the Biotin Carboxylase Domain in Pyruvate Carboxylase from Rhizobium etli
Lietzan, A. D., Menefee, A. L., Zeczycki, T. N., Kumar, S., Attwood, P. V., Wallace, J. C., Cleland, W. W., & Maurice, M. S. (2011) · Biochemistry · doi:10.1021/bi201277j · Cited by 49
Self-citation
Biometals and glycosylation in humans: Congenital disorders of glycosylation shed lights into the crucial role of Golgi manganese homeostasis
Foulquier, F., & Legrand, D. (2020) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2020.129674 · Cited by 48
Inhibitors of Pyruvate Carboxylase~!2009-12-01~!2010-02-01~!2010-04-15~!
Zeczycki, T. N., Maurice, M. S., & Attwood, P. V. (2010) · The Open Enzyme Inhibition Journal · doi:10.2174/1874940201003010008 · Cited by 48
Coupling between d -3-phosphoglycerate dehydrogenase and d -2-hydroxyglutarate dehydrogenase drives bacterial l -serine synthesis
Zhang, W., Zhang, M., Gao, C., Zhang, Y., Ge, Y., Guo, S., Guo, X., Zhou, Z., Liu, Q., Zhang, Y., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1619034114 · Cited by 47
1,25-Dihydroxyvitamin D regulates lipid metabolism and glucose utilization in differentiated 3T3-L1 adipocytes
Larrick, B., Kim, K., Donkin, S. S., & Teegarden, D. (2018) · Nutrition Research · doi:10.1016/j.nutres.2018.07.004 · Cited by 49
Analysis and interpretation of transcriptomic data obtained from extended Warburg effect genes in patients with clear cell renal cell carcinoma
Sanders, E. B., & Diehl, S. (2015) · Oncoscience · doi:10.18632/oncoscience.128 · Cited by 43
Chronic Inhibition of Mitochondrial Dihydrolipoamide Dehydrogenase (DLDH) as an Approach to Managing Diabetic Oxidative Stress
Yang, X., Song, J., & Yan, L. (2019) · Antioxidants · doi:10.3390/antiox8020032 · Cited by 42
1α,25-dihydroxyvitamin D inhibits de novo fatty acid synthesis and lipid accumulation in metastatic breast cancer cells through down-regulation of pyruvate carboxylase
Wilmanski, T. M., Buhman, K. K., Donkin, S. S., Burgess, J. R., & Teegarden, D. (2016) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.11.006 · Cited by 37
Immunocytochemical localization of glucose 6-phosphatase and cytosolic phosphoenolpyruvate carboxykinase in gluconeogenic tissues reveals unsuspected metabolic zonation
Rajas, F., Jourdan‐Pineau, H., Stefanutti, A., Mrad, E. A., Iynedjian, P. B., & Mithieux, G. (2007) · Histochemistry and Cell Biology · doi:10.1007/s00418-006-0263-5 · Cited by 37
Insight into the Carboxyl Transferase Domain Mechanism of Pyruvate Carboxylase from Rhizobium etli
Zeczycki, T. N., Maurice, M. S., Jitrapakdee, S., Wallace, J. C., Attwood, P. V., & Cleland, W. W. (2009) · Biochemistry · doi:10.1021/bi9003759 · Cited by 36
Self-citation
Novel Insights into the Biotin Carboxylase Domain Reactions of Pyruvate Carboxylase from Rhizobium etli
Zeczycki, T. N., Menefee, A. L., Adina-Zada, A., Jitrapakdee, S., Surinya, K. H., Wallace, J. C., Attwood, P. V., Maurice, M. S., & Cleland, W. W. (2011) · Biochemistry · doi:10.1021/bi2012788 · Cited by 35
Self-citation
Geniposide Regulates Glucose-Stimulated Insulin Secretion Possibly through Controlling Glucose Metabolism in INS-1 Cells
Liu, J., Guo, L., Yin, F., Zhang, Y., Liu, Z., & Wang, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078315 · Cited by 35
Suppression of fat deposition in broiler chickens by (-)-hydroxycitric acid supplementation: A proteomics perspective
Peng, M., Han, J. D. J., Li, L., & Ma, H. (2016) · Scientific Reports · doi:10.1038/srep32580 · Cited by 36
Nicotinamide Adenine Dinucleotide: The Redox Sensor in Aging-Related Disorders
Schiuma, G., Lara, D., Clement, J. P., Narducci, M., & Rizzo, R. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0375 · Cited by 34
Differential regulation of bovine pyruvate carboxylase promoters by fatty acids and peroxisome proliferator-activated receptor-α agonist
White, H. M., Koser, S. L., & Donkin, S. S. (2011) · Journal of Dairy Science · doi:10.3168/jds.2010-3960 · Cited by 33
A Substrate-induced Biotin Binding Pocket in the Carboxyltransferase Domain of Pyruvate Carboxylase
Lietzan, A. D., & Maurice, M. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.477828 · Cited by 32
Pyruvate carboxylase promotes thyroid cancer aggressiveness through fatty acid synthesis
Liu, C., Zhou, X., Pan, Y., Liu, Y., & Zhang, Y. (2021) · BMC Cancer · doi:10.1186/s12885-021-08499-9 · Cited by 32
Combining metabolic flux analysis tools and 13C NMR to estimate intracellular fluxes of cultured astrocytes
Teixeira, A. P., Santos, S. S., Carinhas, N., Oliveira, R., & Alves, P. M. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.08.007 · Cited by 32
Pigment Epithelium-Derived Factor (PEDF) Suppresses IL-1β-Mediated c-Jun N-Terminal Kinase (JNK) Activation to Improve Hepatocyte Insulin Signaling
Gattu, A. K., Birkenfeld, A. L., Iwakiri, Y., Jay, S. M., Saltzman, W. M., Doll, J. A., Protiva, P., Samuel, V. T., Crawford, S. E., & Chung, C. (2014) · Endocrinology · doi:10.1210/en.2013-1785 · Cited by 31
Pyruvate Carboxylase Activates the RIG-I-like Receptor-Mediated Antiviral Immune Response by Targeting the MAVS signalosome
Cao, Z., Zhou, Y., Zhu, S., Feng, J. J., Chen, X., Liu, S., Peng, N., Yang, X., Xu, G., & Zhu, Y. (2016) · Scientific Reports · doi:10.1038/srep22002 · Cited by 31
Protein carbonylation in dopaminergic cells exposed to rotenone
Chiaradia, E., Renzone, G., Scaloni, A., Caputo, M., Costanzi, E., Gambelunghe, A., Muzi, G., Avellini, L., Emiliani, C., & Buratta, S. (2019) · Toxicology Letters · doi:10.1016/j.toxlet.2019.04.002 · Cited by 30
Germ-Free Swiss Webster Mice on a High-Fat Diet Develop Obesity, Hyperglycemia, and Dyslipidemia
Logan, I. E., Bobe, G., Miranda, C. L., Vasquez‐Perez, S., Choi, J., Lowry, M. B., Sharpton, T. J., Morgun, A., Maier, C. S., Stevens, J. F., et al. (2020) · Microorganisms · doi:10.3390/microorganisms8040520 · Cited by 31
Metabolic and oncogenic adaptations to pyruvate dehydrogenase inactivation in fibroblasts
Wang, H., Lu, J. L., Kulkarni, S., Zhang, W., Gorka, J. E., Mandel, J. A., Goetzman, E. S., & Prochownik, E. V. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005200 · Cited by 29
Reduced half-life of holocarboxylase synthetase from patients with severe Multiple Carboxylase Deficiency
Bailey, L. M., Ivanov, R. A., Jitrapakdee, S., Wilson, C. J., Wallace, J. C., & Polyak, S. W. (2008) · Human Mutation · doi:10.1002/humu.20766 · Cited by 27
Self-citation
Hepatocyte nuclear factor 4α regulates the expression of the murine pyruvate carboxylase gene through the HNF4-specific binding motif in its proximal promoter
Chavalit, T., Rojvirat, P., Muangsawat, S., & Jitrapakdee, S. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.05.001 · Cited by 26
Self-citation
Nearly 50 years in the making: defining the catalytic mechanism of the multifunctional enzyme, pyruvate carboxylase
Menefee, A. L., & Zeczycki, T. N. (2014) · FEBS Journal · doi:10.1111/febs.12713 · Cited by 26
Activation and Inhibition of Pyruvate Carboxylase from Rhizobium etli
Zeczycki, T. N., Menefee, A. L., Jitrapakdee, S., Wallace, J. C., Attwood, P. V., Maurice, M. S., & Cleland, W. W. (2011) · Biochemistry · doi:10.1021/bi201276r · Cited by 25
Self-citation
Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and mammals interact with pyruvate carboxylase and other acetylated biotin-dependent carboxylases
Wirth, M., Karaca, S., Wenzel, D., Ho, L., Tishkoff, D. X., Lombard, D. B., Verdin, E. M., Urlaub, H., Jedrusik, M. A., & Fischle, W. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.02.002 · Cited by 22
Investigation of adipocyte proteome during the differentiation of brown preadipocytes
Kamal, A. H. M., Kim, W. K., Cho, K., Park, A., Min, J., Han, B., Park, S. G., Lee, S. C., & Bae, K. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.10.005 · Cited by 23
Insights into Transcriptional Regulation of Hepatic Glucose Production
Anyamaneeratch, K., Rojvirat, P., Sukjoi, W., & Jitrapakdee, S. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.05.004 · Cited by 25
Self-citation
Acute carbohydrate overfeeding: a redox model of insulin action and its impact on metabolic dysfunction in humans
Istfan, N., Hasson, B., Apovian, C., Meshulam, T., Yu, L., Anderson, W., & Corkey, B. E. (2021) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00094.2021 · Cited by 22
Gluconeogenic enzymes are differentially regulated by fatty acid cocktails in Madin-Darby bovine kidney cells
White, H. M., Koser, S. L., & Donkin, S. S. (2012) · Journal of Dairy Science · doi:10.3168/jds.2011-4644 · Cited by 22
Biotin deprivation impairs mitochondrial structure and function and has implications for inherited metabolic disorders
Ochoa-Ruiz, E., Díaz-Ruiz, R., Hernández-Vázquez, A. D. J., Ibarra‐González, I., Ortíz-Plata, A., Rembao, D., Ortega-Cuéllar, D., Viollet, B., Uribe‐Carvajal, S., Corella, J. A., et al. (2015) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2015.08.009 · Cited by 22
Heterotrophic Carbon Fixation in a Salamander-Alga Symbiosis
Burns, J. A., Kerney, R. R., & Duhamel, S. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01815 · Cited by 22
Assessment of hepatic pyruvate carboxylase activity using hyperpolarized [1‐13C]‐ l ‐lactate
Chen, J., Hackett, E. P., Kovács, Z., Malloy, C. R., & Park, J. M. (2020) · Magnetic Resonance in Medicine · doi:10.1002/mrm.28489 · Cited by 22
Short communication: Regulation of hepatic gluconeogenic enzymes by dietary glycerol in transition dairy cows
White, H. M., Carvalho, E. R., Koser, S. L., Schmelz-Roberts, N. S., Pezzanite, L. M., Slabaugh, A., Doane, P. H., & Donkin, S. S. (2015) · Journal of Dairy Science · doi:10.3168/jds.2015-9953 · Cited by 21
Hepatotoxicity assessment of Rhizoma Paridis in adult zebrafish through proteomes and metabolome
Jia, Z., Zhao, C., Wang, M., Zhao, X., Zhang, W., Han, T., Xia, Q., Han, Z., Lin, R., & Li, X.-R. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109558 · Cited by 21
Characterization of the Distal Promoter of the Human Pyruvate Carboxylase Gene in Pancreatic Beta Cells
Thonpho, A., Rojvirat, P., Jitrapakdee, S., & MacDonald, M. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055139 · Cited by 20
Self-citation
Glutamate dehydrogenase activator BCH stimulating reductive amination prevents high fat/high fructose diet-induced steatohepatitis and hyperglycemia in C57BL/6J mice
Han, S. J., Choi, S., Yi, S., Jung, J. G., Jung, I., Shin, M., Kang, S. Y., Oh, H., Kim, H. J., Kim, D. J., et al. (2016) · Scientific Reports · doi:10.1038/srep37468 · Cited by 19
Transcriptional regulation of the distal promoter of the rat pyruvate carboxylase gene by hepatocyte nuclear factor 3β/Foxa2 and upstream stimulatory factors in insulinoma cells
Boonsaen, T., Rojvirat, P., Surinya, K. H., Wallace, J. C., & Jitrapakdee, S. (2007) · Biochemical Journal · doi:10.1042/bj20070276 · Cited by 20
Self-citation
Cloning the Genomic Sequence and Identification of Promoter Regions of Bovine Pyruvate Carboxylase
Hazelton, S. R., Spurlock, D. M., Bidwell, C. A., & Donkin, S. S. (2007) · Journal of Dairy Science · doi:10.3168/jds.2007-0542 · Cited by 20
Regulation of bovine pyruvate carboxylase mRNA and promoter expression by thermal stress1
White, H. M., Koser, S. L., & Donkin, S. S. (2012) · Journal of Animal Science · doi:10.2527/jas.2010-3408 · Cited by 18
Interplay Between Glucose Metabolism and Chromatin Modifications in Cancer
Ma, R., Wu, Y., Li, S., & Yu, X. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.654337 · Cited by 18
Sex-dependent compensated oxidative stress in the mouse liver upon deletion of catechol O-methyltransferase.
Tenorio-Laranga, J., Männistö, P., Karayiorgou, M., Gogos, J., & García-Horsman, J. A. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.02.004 · Cited by 19
MicroRNA-143-3p targets pyruvate carboxylase expression and controls proliferation and migration of MDA-MB-231 cells
Pinweha, P., Phillips, C. A., Gregory, P. A., Li, X., Chuayboonya, P., Mongkolsiri, P., Goodall, G. J., & Jitrapakdee, S. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.108169 · Cited by 18
Self-citation
Changes of glycolysis and gluconeogenesis key enzymes in the muscle of the shrimp Penaeus vannamei in response to hypoxia and reoxygenation
Cruz-Moreno, D. G., Hernández-Aguirre, L. E., Peregrino-Uriarte, A. B., Leyva‐Carrillo, L., Gómez‐Jiménez, S., Contreras‐Vergara, C. A., Hernández‐López, J., & Yepiz-Plascencia, G. M. (2024) · Journal of Experimental Marine Biology and Ecology · doi:10.1016/j.jembe.2024.152052 · Cited by 16
Anaplerosis in cancer: Another step beyond the warburg effect
Ochoa-Ruiz, E., & Díaz-Ruiz, R. (2012) · American Journal of Molecular Biology · doi:10.4236/ajmb.2012.24031 · Cited by 17
Kinetic and Thermodynamic Analysis of Acetyl-CoA Activation ofStaphylococcus aureusPyruvate Carboxylase
Westerhold, L. E., Bridges, L. C., Shaikh, S. R., & Zeczycki, T. N. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00383 · Cited by 17
Herbal extract dietary supplementation effect on growth performance and meat quality in broiler raised under two stocking densities
Obeidat, M. D., Alkhateeb, M. E. M., Jawasreh, K. I. Z., Riley, D. G., & Sukhni, I. A. A. (2024) · Scientific Reports · doi:10.1038/s41598-024-68138-8 · Cited by 14

Authors: Jitrapakdee, S., Vidal-Puig, A., & Wallace, J. C.
Affiliations: Mahidol University (TH)
The University of Adelaide (AU)
Corresponding author: Jitrapakdee, S.
ORCID: Jitrapakdee, S.
Venue: Cellular and Molecular Life Sciences
Publisher: Springer Science and Business Media LLC
Published: 2006-02-28
Volume: 63
Issue: 7-8
Pages: 843-854
ISSN: 1420-682X (ISSN-L)
1420-9071
DOI: 10.1007/s00018-005-5410-y
PMC: PMC11136034
OpenAlex: W1986860566
Cited by: 149
References: 97
Citations by year: 2026: 5 · 2025: 2 · 2024: 8 · 2023: 4 · 2022: 2 · 2021: 10 · 2020: 9 · 2019: 12 · 2018: 9 · 2017: 3 · 2016: 7 · 2015: 10 · 2014: 12 · 2013: 12 · 2012: 12
FWCI: 2.87
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Cellular and Molecular Life Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Adelaide Research & Scholarship (AR&S) (University of Adelaide) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Keywords: pyruvate carboxylase, anaplerosis, TCA cycle, oxaloacetate, gluconeogenesis, fatty acid synthesis, glyceroneogenesis, PPARγ, metabolic switch, lipogenesis, glucose-stimulated insulin secretion, malate, islets, astrocytes, glutamate synthesis, hyperglycemia, hyperlipidemia, tissue-specific gene expression, transcription factors
MeSH terms: Animals, Humans, Kidney, Liver, Pancreas, Pyruvate Carboxylase, Signal Transduction, Pyruvic Acid, Oxaloacetic Acid

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Anaplerotic roles of pyruvate carboxylase in mammalian tissues

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks