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Linking mitochondrial bioenergetics to insulin resistance via redox biology
Open accessAbstract
Chronic overnutrition and physical inactivity are major risk factors for insulin resistance and type 2 diabetes. Recent research indicates that overnutrition generates an increase in hydrogen peroxide (H(2)O(2)) emission from mitochondria, serving as a release valve to relieve the reducing pressure created by fuel overload, as well as a primary signal that ultimately decreases insulin sensitivity. H(2)O(2) is a major input to cellular redox circuits that link to cysteine residues throughout the entire proteome to regulate cell function. Here we review the principles of mitochondrial bioenergetics and redox systems biology and offer new insight into how H(2)O(2) emission may be linked via redox biology to the etiology of insulin resistance.
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“Emergent evidence suggests that a chronic positive energy balance increases by-products of mitochondrial metabolism that may trigger the pathogenesis of insulin resistance and metabolic inflexibility (16,17).”
From Defects in mitochondrial efficiency and H2O2 emissions in obese women are restored to a lean phenotype with aerobic exercise training (2015) · cites this paper as [17]
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“The nutrient burden creates a positive mitochondrial membrane potential, which increases mtH2O2 emissions (17), and chronic exposure to reactive oxygen species has been shown to inhibit insulin-mediated GLUT4 translocation (26).”
From Defects in mitochondrial efficiency and H2O2 emissions in obese women are restored to a lean phenotype with aerobic exercise training (2015) · cites this paper as [17]
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Cites
Biochemistry and molecular cell biology of diabetic complications
Brownlee, M. (2001) · Nature · doi:10.1038/414813a · Cited by 9,107
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
MITCHELL, P. (1961) · Nature · doi:10.1038/191144a0 · Cited by 4,704
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587
A central role for JNK in obesity and insulin resistance
Hirosumi, J., Tuncman, G., Chang, L., Görgün, C. Z., Uysal, K. T., Maeda, K., Karin, M., & Hotamisligil, G. S. (2002) · Nature · doi:10.1038/nature01137 · Cited by 3,359
Reactive oxygen species have a causal role in multiple forms of insulin resistance
Houstis, N., Rosen, E. D., & Lander, E. S. (2006) · Nature · doi:10.1038/nature04634 · Cited by 2,525
Oxidative Stress and Stress-Activated Signaling Pathways: A Unifying Hypothesis of Type 2 Diabetes
Evans, J. L., Goldfine, I. D., Maddux, B. A., & Grodsky, G. M. (2002) · Endocrine Reviews · doi:10.1210/er.2001-0039 · Cited by 2,232
Mitochondrial dysfunction and type 2 diabetes
Lowell, B. B., & Shulman, G. I. (2005) · Science · doi:10.1126/science.1104343 · Cited by 2,070
Yuan, M., Konstantopoulos, N., Lee, J., Hansen, L., Li, Z.-W., Karin, M., & Shoelson, S. E. (2001) · Science · doi:10.1126/science.1061620 · Cited by 1,884
DeFronzo, R. A., Jacot, E., Jequier, E., Maeder, E., Wahren, J., & Felber, J. P. (1981) · Diabetes · doi:10.2337/diab.30.12.1000 · Cited by 1,770
Korshunov, S. S., Skulachev, V. P., & Starkov, A. A. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01159-9 · Cited by 1,727
Extension of murine life span by overexpression of catalase targeted to mitochondria
Schriner, S. E., Linford, N. J., Martin, G. M., Treuting, P., Ogburn, C. E., Emond, M., Coskun, P. E., Ladiges, W., Wolf, N., Van Remmen, H., et al. (2005) · Science · doi:10.1126/science.1106653 · Cited by 1,724
Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity
Um, S. H., Frigerio, F., Watanabe, M., Picard, F., Joaquin, M., Sticker, M., Fumagalli, S., Allegrini, P. R., Kozma, S. C., Auwerx, J., et al. (2004) · Nature · doi:10.1038/nature02866 · Cited by 1,677
Topology of superoxide production from different sites in the mitochondrial electron transport chain
St-Pierre, J., Buckingham, J. A., Roebuck, S. J., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207217200 · Cited by 1,545
Genetically encoded fluorescent indicator for intracellular hydrogen peroxide
Belousov, V. V., Fradkov, A. F., Lukyanov, K. A., Staroverov, D. B., Shakhbazov, K., Terskikh, A. V., & Lukyanov, S. (2006) · Nature Methods · doi:10.1038/nmeth866 · Cited by 1,286
Anderson, E. J., Lustig, M. E., Boyle, K. E., Woodlief, T. L., Kane, D. A., Lin, C.-T., Price, J. W., Kang, L., Rabinovitch, P. S., Szeto, H. H., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37048 · Cited by 1,253
Self-citationRadical-free biology of oxidative stress
Jones, D. P. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00283.2008 · Cited by 1,213
Signaling Functions of Reactive Oxygen Species
Forman, H. J., Maiorino, M., & Ursini, F. (2010) · Biochemistry · doi:10.1021/bi9020378 · Cited by 827
Zhao, K., Zhao, G.-M., Wu, D., Soong, Y., Birk, A. V., Schiller, P. W., & Szeto, H. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402999200 · Cited by 782
THE STRUCTURE AND MECHANISM OF PROTEIN PHOSPHATASES: Insights into Catalysis and Regulation
Barford, D., Das, A. K., & Egloff, M. P. (1998) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.27.1.133 · Cited by 713
Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling
Miller, E. W., Dickinson, B. C., & Chang, C. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1005776107 · Cited by 707
Redox Redux: Revisiting PTPs and the Control of Cell Signaling
Tonks, N. K. (2005) · Cell · doi:10.1016/j.cell.2005.05.016 · Cited by 702
Woo, H. A., Yim, S. H., Shin, D. H., Kang, D., Yu, D., & Rhee, S. G. (2010) · Cell · doi:10.1016/j.cell.2010.01.009 · Cited by 632
Phosphorylation of IRS proteins, insulin action, and insulin resistance
Boura-Halfon, S., & Zick, Y. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90437.2008 · Cited by 598
The Molecular Basis for Oxidative Stress-Induced Insulin Resistance
Evans, J. L., Maddux, B. A., & Goldfine, I. D. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.1040 · Cited by 587
Reactive oxygen species enhance insulin sensitivity
Loh, K., Deng, H., Fukushima, A., Cai, X., Boivin, B., Galic, S., Bruce, C., Shields, B. J., Skiba, B., Ooms, L. M., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.08.009 · Cited by 581
A Molecular Basis for Insulin Resistance
Paz, K., Hemi, R., LeRoith, D., Karasik, A., Elhanany, E., Kanety, H., & Zick, Y. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.47.29911 · Cited by 556
Positive and Negative Regulation of Insulin Signaling by Reactive Oxygen and Nitrogen Species
Bashan, N., Kovsan, J., Kachko, I., Ovadia, H., & Rudich, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00014.2008 · Cited by 542
Fluorescent Protein-Based Redox Probes
Meyer, A. J., & Dick, T. P. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2948 · Cited by 542
Insulin resistance is a cellular antioxidant defense mechanism
Hoehn, K. L., Salmon, A. B., Hohnen-Behrens, C., Turner, N., Hoy, A. J., Maghzal, G. J., Stocker, R., Van Remmen, H., Kraegen, E. W., Cooney, G. J., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902380106 · Cited by 540
Mahadev, K., Motoshima, H., Wu, X., Ruddy, J. M., Arnold, R. S., Cheng, G., Lambeth, J. D., & Goldstein, B. J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.5.1844-1854.2004 · Cited by 520
Characterization of Superoxide-producing Sites in Isolated Brain Mitochondria
Kudin, A. P., Bimpong‐Buta, N., Vielhaber, S., Elger, C. E., & Kunz, W. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310341200 · Cited by 514
The Hyperglycemia-induced Inflammatory Response in Adipocytes
Lin, Y., Berg, A. H., Iyengar, P., Lam, T. K. T., Giacca, A., Combs, T. P., Rajala, M. W., Du, X., Rollman, B., Li, W., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411863200 · Cited by 507
Tanti, J.-F., & Jager, J. (2009) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2009.07.004 · Cited by 430
Nakamura, S., Takamura, T., Matsuzawa-Nagata, N., Takayama, H., Misu, H., Noda, H., Nabemoto, S., Kurita, S., Ota, T., Ando, H., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m901488200 · Cited by 426
Compartmentalization of Redox Signaling Through NADPH Oxidase–Derived ROS
Ushio‐Fukai, M. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2333 · Cited by 375
Bost, F., Aouadi, M., Caron, L., Even, P. C., Belmonte, N., Prot, M., Dani, C., Hofman, P. M., Pagès, G., Pouysségur, J., et al. (2005) · Diabetes · doi:10.2337/diabetes.54.2.402 · Cited by 351
Targeting and Regulation of Reactive Oxygen Species Generation by Nox Family NADPH Oxidases
Leto, T. L., Morand, S. C., Hurt, D. E., & Ueyama, T. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2637 · Cited by 347
Lee, H.-Y., Choi, C. S., Birkenfeld, A. L., Alves, T. C., Jornayvaz, F. R., Jurczak, M. J., Zhang, D., Woo, D. K., Shadel, G. S., Ladiges, W., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.004 · Cited by 319
IRS1-Independent Defects Define Major Nodes of Insulin Resistance
Hoehn, K. L., Hohnen-Behrens, C., Cederberg, A., Wu, L. E., Turner, N. A., Yuasa, T., Ebina, Y., & James, D. E. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.04.005 · Cited by 318
Cochemé, H. M., Quin, C., McQuaker, S. J., Cabreiro, F., Logan, A., Prime, T. A., Abakumova, I., Patel, J. V., Fearnley, I. M., James, A. M., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.02.003 · Cited by 313
Seifert, E. L., Estey, C., Xuan, J. Y., & Harper, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.026203 · Cited by 289
Mitochondria-Targeted Cytoprotective Peptides for Ischemia–Reperfusion Injury
Szeto, H. H. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1892 · Cited by 274
Reactive oxygen species and insulin resistance: the good, the bad and the ugly
Tiganis, T. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.11.006 · Cited by 256
Mothe‐Satney, I., & OBBERGHEN, E. V. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.19.11222 · Cited by 254
Superoxide dismutase: A comparison of rate constants
Forman, H. J., & Fridovich, I. (1973) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(73)90636-x · Cited by 252
Preferential Uptake of Dietary Fatty Acids in Adipose Tissue and Muscle in the Postprandial Period
Bickerton, A. S. T., Roberts, R., Fielding, B. A., Hodson, L., Blaak, E. E., Wagenmakers, A. J. M., Gilbert, M., Karpe, F., & Frayn, K. N. (2006) · Diabetes · doi:10.2337/db06-0822 · Cited by 247
Role of insulin-induced reactive oxygen species in the insulin signaling pathway
Goldstein, B. J., Mahadev, K., Wu, X., Zhu, L., & Motoshima, H. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.1021 · Cited by 238
Turning Signals On and Off: GLUT4 Traffic in the Insulin-Signaling Highway
Thong, F. S. L., Dugani, S. B., & Klip, A. (2005) · Physiology · doi:10.1152/physiol.00017.2005 · Cited by 227
Haber, C. A., Lam, T. K. T., Yu, Z., Gupta, N., Goh, T. T., Bogdanovic, E., Giacca, A., & Fantus, I. G. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00355.2002 · Cited by 226
Generating, Partitioning, Targeting and Functioning of Superoxide in Mitochondria
Liu, S. (1997) · Bioscience Reports · doi:10.1023/a:1027328510931 · Cited by 218
Buettner, G. R., Ng, C. F., Wang, M., Rodgers, V. G. J., & Schafer, F. Q. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.07.015 · Cited by 199
Paz, K., Liu, Y., Shorer, H., Hemi, R., LeRoith, D., Quan, M., Kanety, H., Seger, R., & Zick, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28816 · Cited by 194
Perry, C. G. R., Kane, D. A., Lin, C., Kozy, R., Cathey, B. L., Lark, D. S., Kane, C. L., Brophy, P. M., Gavin, T. P., Anderson, E. J., et al. (2011) · Biochemical Journal · doi:10.1042/bj20110366 · Cited by 176
Self-citationLü, G., Ren, S. V., Kôrge, P., Choi, J., Dong, Y., Weiss, J. N., Koehler, C. M., Chen, J., & Wang, Y. (2007) · Genes & Development · doi:10.1101/gad.1499107 · Cited by 157
Espinosa, A., Leiva, A., Peña, M., Müller, M., Anibal Debandi, L., Hidalgo, C., Carrasco, M. A., & Jaimovich, E. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20745 · Cited by 155
ReviewPTPs versus PTKs: The redox side of the coin
Chiarugi, P. (2005) · Free Radical Research · doi:10.1080/10715760400027987 · Cited by 155
Anderson, E. J., Yamazaki, H., & Neufer, P. D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706129200 · Cited by 151
Self-citationReduction of mitochondrial H2O2 by overexpressing peroxiredoxin 3 improves glucose tolerance in mice
Chen, L., Na, R., Gu, M., Salmon, A. B., Liu, Y., Liang, H., Qi, W., Remmen, H. V., Richardson, A. G., & Ran, Q. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2008.00432.x · Cited by 146
Batinic̈‐Haberle, I., Cuzzocrea, S., Reboucas, J. S., Ferrer‐Sueta, G., Mazzon, E., Paola, R. D., Radí, R., Spasojević, I., Benov, L., & Salvemini, D. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.09.042 · Cited by 140
Redox Chemistry of Biological Thiols
Nagy, P., & Winterbourn, C. C. (2010) · Advances in molecular toxicology · doi:10.1016/s1872-0854(10)04006-3 · Cited by 129
Kraegen, E. W., Saha, A. K., Preston, E., Wilks, D. L., Hoy, A. J., Cooney, G. J., & Ruderman, N. B. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00316.2005 · Cited by 126
Liu, S. (1999) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1018650103259 · Cited by 119
Downstream Targets and Intracellular Compartmentalization in Nox Signaling
Chen, K., Craige, S. M., & Keaney, J. F. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2594 · Cited by 106
Espinosa, A., García, A., Härtel, S., Hidalgo, C., & Jaimovich, E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804249200 · Cited by 100
Hoy, A. J., Brandon, A. E., Turner, N., Watt, M. J., Bruce, C. R., Cooney, G. J., & Kraegen, E. W. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90945.2008 · Cited by 92
Redox Control of Neural Function: Background, Mechanisms, and Significance
Maher, P. A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1941 · Cited by 92
Dasgupta, J., Kar, S., Liu, R., Joseph, J., Kalyanaraman, B., Remington, S. J., Chen, C., & Melendez, J. A. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22193 · Cited by 90
Bhattacharya, A., Müller, F. L., Liu, Y., Sabia, M., Liang, H., Song, W. J., Jang, Y. C., Ran, Q., & Remmen, H. V. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806311200 · Cited by 90
Hydrogen-Peroxide Metabolism in Skeletal-Muscle Mitochondria
Phung, C.-T., Ezieme, J. A., & Turrens, J. F. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1528 · Cited by 89
Danielsson, A., Öst, A., Nyström, F. H., & Strålfors, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500230200 · Cited by 89
Fetrow, J. S., Siew, N., & Skolnick, J. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.13.1866 · Cited by 88
Wright, V. P., Reiser, P. J., & Clanton, T. L. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.178285 · Cited by 82
Malonyl CoenzymeA Decarboxylase Regulates Lipid and Glucose Metabolism in Human Skeletal Muscle
Bouzakri, K., Austin, R., Rune, A., Lassman, M. E., Garcia-Roves, P. M., Berger, J. P., Krook, A., Chibalin, A. V., Zhang, B. B., & Zierath, J. R. (2008) · Diabetes · doi:10.2337/db07-0583 · Cited by 77
Gardner, R., Salvador, A., & Moradas‐Ferreira, P. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00861-4 · Cited by 72
Covey, T. M., Edes, K., Coombs, G. S., Virshup, D. M., & Fitzpatrick, F. A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013545 · Cited by 72
Oxidants Positively or Negatively Regulate Nuclear Factor κB in a Context-dependent Manner
Loukili, N., Rosenblatt‐Velin, N., Rolli, J., Levrand, S., Feihl, F., Waeber, B., Pacher, P., & Liaudet, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.103259 · Cited by 71
Weigert, C., Kron, M., Kalbacher, H., Pohl, A. K., Runge, H., Häring, H., Schleicher, E. D., & Lehmann, R. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0102 · Cited by 68
Oxidative Inhibition of Protein Phosphatase 2A Activity: Role of Catalytic Subunit Disulfides
Foley, T. D., Petro, L. A., Stredny, C. M., & Coppa, T. M. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9394-x · Cited by 65
Luo, M., Langlais, P. R., Yi, Z., Lefort, N., Filippis, E. A. D., Hwang, H., Christ-Roberts, C. Y., & Mandarino, L. J. (2007) · Endocrinology · doi:10.1210/en.2007-0049 · Cited by 63
Weigert, C., Hennige, A. M., Brischmann, T., Beck, A., Moeschel, K., Schaüble, M., Brodbeck, K., Häring, H.-U., Schleicher, E. D., & Lehmann, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506134200 · Cited by 50
[7] Reaction of superoxide with glutathioneand other thiols
Winterbourn, C. C., & Metodiewa, D. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)51112-1 · Cited by 46
Excess exposure to insulin may be the primary cause of insulin resistance
Cao, W., Liu, H.-Y., Hong, T., & Liu, Z. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00677.2009 · Cited by 33
The Peroxide Dilemma: Opposing and Mediating Insulin Action
Szypowska, A. A., & Burgering, B. M. T. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3794 · Cited by 33
Alternative Pathways Might Mediate Toxicity of High Concentrations of Superoxide Dismutase
Kowald, A., & Klipp, E. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1297.065 · Cited by 31
Robinson, K. A., & Buse, M. G. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00644.2007 · Cited by 31
Hydrogen peroxide triggers the proteolytic cleavage and the inactivation of calcineurin
Lee, J., Kim, H., Jang, H., Cho, E., & Youn, H. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04340.x · Cited by 26
The evolution of insulin resistance in muscle of the glucose infused rat
Brandon, A. E., Hoy, A. J., Wright, L. E., Turner, N. A., Hegarty, B. D., Iseli, T. J., Xu, X. J., Cooney, G. J., Saha, A. K., Ruderman, N. B., et al. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.03.008 · Cited by 17
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- Goldstein, 2005, Role of insulin-induced reactive oxygen species in the insulin signaling pathway, Antioxid. Redox Signal., 7, 1021, 10.1089/ars.2005.7.1021 · DOI · Paper page
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James, D. E., Stöckli, J., & Birnbaum, M. J. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00390-6 · Cited by 736
Comprehensive review on lactate metabolism in human health
Adeva‐Andany, M. M., López-Ojén, M., Funcasta-Calderón, R., Ameneiros-Rodríguez, E., Donapetry, C., Vila-Altesor, M., & Rodríguez-Seijas, J. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.05.007 · Cited by 636
“Pyruvate is then reduced to L-lactate by LDH (Glinghammar et al., 2009).”
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Muriach, M., Flores‐Bellver, M., Romero, F. J., & Barcia, J. M. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/102158 · Cited by 495
“Moreover, insulin regulates mitochondrial metabolism and oxidative capacity throughPI3K/Akt signaling [36, 37]; therefore, decreased Akt signaling by hyperinsulinemia- mediated IR may have profound effects on mitochondrial function in neurons and result in subsequent increased oxidative stress [38].”
BackgroundThe rise of mitochondria in medicine
Picard, M. A., Wallace, D. C., & Burelle, Y. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.07.003 · Cited by 475
“The detrimental effect of metabolic oversupply is thought to result from mitochondrial substrate overload (Fisher-Wellman and Neufer, 2012), which entails excessive reduction of the respiratory chain and consequent ROS production (Anderson et al., 2009), mitochondrial fission and oxidative stress…”
Background
Metadata
- Authors
- Fisher-Wellman, K. H., & Neufer, P. D.
- Affiliations
- East Carolina University (US)
- Corresponding author
- Neufer, P. Darrell
- ORCID
- Neufer, P. Darrell
- Venue
- Trends in Endocrinology & Metabolism
- Publisher
- Elsevier BV
- Published
- 2012-03
- Volume
- 23
- Issue
- 3
- Pages
- 142-153
- ISSN
- 1043-2760 (ISSN-L)
- PMC
- PMC3313496
- OpenAlex
- W2069466682
- Cited by
- 316
- References
- 89
- Citations by year
- 2026: 17 · 2025: 12 · 2024: 16 · 2023: 22 · 2022: 14 · 2021: 24 · 2020: 16 · 2019: 28 · 2018: 24 · 2017: 25 · 2016: 20 · 2015: 25 · 2014: 29 · 2013: 30 · 2012: 12
- FWCI
- 2.80
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Trends in Endocrinology and Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK073488, R01DK074825)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- mitochondrial bioenergetics, insulin resistance, type 2 diabetes, hydrogen peroxide, mitochondrial reactive oxygen species, redox signaling, cysteine residues, overnutrition, physical inactivity
- MeSH terms
- Animals, Energy Metabolism, Humans, Hydrogen Peroxide, Insulin Resistance, Mitochondria, Oxidation-Reduction, Signal Transduction
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 ›
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