Cited by 401Pancreatic function and diabetesMitochondrial Function and PathologyMetabolism, Diabetes, and Cancer

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Superoxide-mediated activation of uncoupling protein 2 causes pancreatic β cell dysfunction

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Krauss, Stefan, Zhang, Chen-Yu, Scorrano, Luca, Dalgaard, Louise T., St-Pierre, Julie, Grey, Shane T., Lowell, Bradford B.·2003·Journal of Clinical Investigation

DOI 10.1172/jci200319774PMC PMC297000

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Abstract

Failure to secrete adequate amounts of insulin in response to increasing concentrations of glucose is an important feature of type 2 diabetes. The mechanism for loss of glucose responsiveness is unknown. Uncoupling protein 2 (UCP2), by virtue of its mitochondrial proton leak activity and consequent negative effect on ATP production, impairs glucose-stimulated insulin secretion. Of interest, it has recently been shown that superoxide, when added to isolated mitochondria, activates UCP2-mediated proton leak. Since obesity and chronic hyperglycemia increase mitochondrial superoxide production, as well as UCP2 expression in pancreatic β cells, a superoxide-UCP2 pathway could contribute importantly to obesity- and hyperglycemia-induced β cell dysfunction. This study demonstrates that endogenously produced mitochondrial superoxide activates UCP2-mediated proton leak, thus lowering ATP levels and impairing glucose-stimulated insulin secretion. Furthermore, hyperglycemia- and obesity-induced loss of glucose responsiveness is prevented by reduction of mitochondrial superoxide production or gene knockout of UCP2. Importantly, reduction of superoxide has no beneficial effect in the absence of UCP2, and superoxide levels are increased further in the absence of UCP2, demonstrating that the adverse effects of superoxide on β cell glucose sensing are caused by activation of UCP2. Therefore, superoxide-mediated activation of UCP2 could play an important role in the pathogenesis of β cell dysfunction and type 2 diabetes.

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Biochemistry and molecular cell biology of diabetic complications
Brownlee, M. (2001) · Nature · doi:10.1038/414813a · Cited by 9,107
Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage
Nishikawa, T., Edelstein, D., Du, X. L., Yamagishi, S.-I., Matsumura, T., Kaneda, Y., Yorek, M. A., Beebe, D., Oates, P. J., Hammes, H.-P., et al. (2000) · Nature · doi:10.1038/35008121 · Cited by 4,277
Superoxide activates mitochondrial uncoupling proteins
Echtay, K. S., Roussel, D., St-Pierre, J., Jekabsons, M. B., Cadenas, S., Stuart, J. A., Harper, J. A., Roebuck, S. J., Morrison, A., Pickering, S., et al. (2002) · Nature · doi:10.1038/415096a · Cited by 1,382
Self-citation
Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation
Du, X.-L., Edelstein, D., Rossetti, L., Fantus, I. G., Goldberg, H. J., Ziyadeh, F. N., Wu, J., & Brownlee, M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.22.12222 · Cited by 1,152
Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production
Arsenijevic, D., Onuma, H., Pecqueur, C., Raimbault, S., Manning, B. S., Miroux, B., Couplan, E., Alves‐Guerra, M., Goubern, M., Surwit, R. S., et al. (2000) · Nature Genetics · doi:10.1038/82565 · Cited by 1,100
Uncoupling protein-2 negatively regulates insulin secretion and is a major link between obesity, β-cell dysfunction, and type 2 diabetes.
Zhang, C.-Y., Baffy, G., Perret, P., Krauss, S., Peroni, O., Grujic, D., Hagen, T., Vidal-Puig, A. J., Boss, O., Kim, Y.-B., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00378-6 · Cited by 917
Self-citation
A role for uncoupling protein‐2 as a regulator of mitochondrial hydrogen peroxide generation
Nègre‐Salvayre, A., Hirtz, C., Carrera, G., Cazenave, R., Troly, M., Salvayre, R., Pénicaud, L., & Casteilla, L. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.10.9271366 · Cited by 773
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
Beneficial effects of antioxidants in diabetes: possible protection of pancreatic beta-cells against glucose toxicity.
Kaneto, H., Kajimoto, Y., Miyagawa, J., Matsuoka, T., Fujitani, Y., Umayahara, Y., Hanafusa, T., Matsuzawa, Y., Yamasaki, Y., & Hori, M. (1999) · Diabetes · doi:10.2337/diabetes.48.12.2398 · Cited by 713
Energy metabolism in uncoupling protein 3 gene knockout mice
Vidal-Puig, A. J., Grujic, D., Zhang, C.-Y., Hagen, T., Boss, O., Ido, Y., Szczepanik, A., Wade, J., Mootha, V., Cortright, R., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910179199 · Cited by 677
Self-citation

Show all 52 references

Research works printed but not linked: 3

Matthews, 1997, In Textbook of diabetes. JC Pickup and G Williams, editors Blackwell Science Oxford, United Kingdom, 21, 21
10.1210/en.143.2.339 · DOI · Paper page
Li, 2000, Cancer Res., 60, 3927

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[Role of uncoupling proteins UCP1, UCP2 and UCP3 in energy balance, type 2 diabetes and obesity. Synergism with the thyroid].
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Chapter Six - Mitochondria and Reactive Oxygen Species in Aging and Age-Related Diseases
Giorgi, C., Marchi, S., Simoes, I., Ren, Z., Morciano, G., Perrone, M., Patalas‐Krawczyk, P., Borchard, S., Jędrak, P., Pierzynowska, K., et al. (2018) · UCL Discovery (University College London) · Cited by 1
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The effect of chemical therapy with bleomycin sulfate on the functional parameters of the endocrine pancreas.
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Muslce mitochondria in sepsis
Fredriksson, K. (2006) · Cited by 1
Short Chain Sugars as Endogenous Toxins
Benov, L. (2009) · Wiley eBooks · doi:10.1002/9783527628100.ch6 · Cited by 1
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Lee, S. (2008) · TSpace (University of Toronto) · Cited by 1
Glycemic Control of Apoptosis in the Pancreatic Beta Cell: Danger of Extremes?
Martens, G. A., & de Casteele, M. V. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.9.ft-16 · Cited by 1
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Tang, C., Oprescu, A. I., & Giacca, A. (2009) · Wiley eBooks · doi:10.1002/9783527628100.ch21
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Masur, K., Thévenod, F., & nker, K. S. Z. A. (2008) · Frontiers in diabetes · doi:10.1159/000152030
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Dods, R. F. (2013) · Wiley eBooks · doi:10.1002/9781118530665.ch5
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Anedda, A. (2010) · Tesis Doctorals en Xarxa (Consorci de Serveis Universitaris de Catalunya)
Perfil de expressão de genes modulados pela Pioglitazona em ilhotas pancreáticas murídeas
Lamounier, R. N. (2008) · doi:10.11606/t.5.2008.tde-07042011-145852
5.4 Uncoupling Proteins
Kim‐Han, J. S., Ali, S. S., & Dugan, L. L. (2007) · Springer eBooks · doi:10.1007/978-0-387-30411-3_20
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Nitert, M. D. (2007) · Lund University Publications (Lund University)
The advantages of the treatment of the patients with type 2 diabetes mellitus with gliclazide MR
Пекарева, Е. В. (2012) · Problems of Endocrinology · doi:10.14341/probl201258258-61 · Cited by 1
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Chellan, N. (2011) · SUNScholar (Stellenbosch University)
The pathophysiology of respiratory chain dysfunction
Silva, J. P. (2005) · Figshare
Regulation of glucose metabolism by Alox8
Karki, R. (2014) · OpenSIUC (Southern Illinois University Carbondale)
The effects of prolonged exposure to high glucose on glucose metabolism and metabolomic profiles in pancreatic β-cells
Wallace, M., & Brennan, L. (2008) · Proceedings of The Nutrition Society · doi:10.1017/s0029665108009002
LeakRegulation and Physiology of Mitochondrial Proton
Dalton, N. D., Peterson, K. L., Gu, Y., Matkovich, S. J., Murphy, A. N., Ling, H., Divakaruni, A. S., Zambon, A. C., King, M. S., Kunji, E. R. S., et al. (2015)
CMS and Type 2 Diabetes Mellitus: Bound Together by the Renin Angiotensin Aldosterone System
Gupta, D., Lastra, G., Manrique, C. M., & Sowers, J. R. (2009) · Humana Press eBooks · doi:10.1007/978-1-60761-186-8_13
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Bagnati, M. (2015)
Bcl-xL protects pancreatic beta-cells from high glucose-induced failure by dampening mitochondrial metabolism
Shih, A. Z. L. (2015) · Open Collections · doi:10.14288/1.0166247
from diabetic patients, and in an established murine model of type 2 diabetes mellitus. Taken together, our data indicate that RyR2 channels play a crucial role in the regulation of insulin secretion and glucose homeostasis. Calcium release channel RyR2 regulates insulin release and glucose homeostasis
Santulli, G., Pagano, G., Sardu, C., Xie, W., Reiken, S. R., Cannone, M., Marziliano, N., Trimarco, B., Guise, T. A., Lacampagne, A., et al. (2015)
Role of insulin receptor substrate 1 in energy homeostasis in vivo
Stöhr, O. (2012) · Kölner Universitäts PublikationsServer (Universität zu Köln)
Alterações na homeostase redox das células beta pancreáticas em resposta à glicose.
Valle, M. M. R. (2014) · doi:10.11606/t.42.2014.tde-19022015-163014
The use of a genetic strategy to study the role of modulation of oxidative stress by uncoupling proteins 2 and 3 in the pathogenesis of Type 2 Diabetes.
Gable, D. R. (2008) · OpenGrey (Institut de l'Information Scientifique et Technique)
The role of uncoupling protein 2 (UCP2) on the development of type 2 diabetes mellitus and its chronic complications Papel da proteína desacopladora 2 (UCP2) no desenvolvimento do diabetes melito tipo 2 e de suas complicações crônicas
de Souza, B. M., Assmann, T. S., Kliemann, L. M., Gross, J. L., Canani, L. H. S., & Crispim, D. (2011)
Obesity, Nutrigenomics, Metabolic Syndrome, and Type 2 Diabetes
Heber, D. (2007) · Oxidative stress and disease · doi:10.1201/9781420043792.ch7
Role of Uncoupling Protein 2 in Pancreatic _ Cell Function
Diao, J., Chan, C. B., & Wheeler, M. B. (2007) · Oxidative stress and disease · doi:10.1201/9781420043792.ch13
Mechanisms of fatty acid induced decrease in β-cell function.
Oprescu, A. I. (2009) · TSpace (University of Toronto)
Oxidative Stress and Diabetes 145
Pitocco, D., Martini, F., Scavone, G., Zaccardi, F., & Ghirlanda, G. (2014)
INVOLVEMENT OF FREE RADICALS IN CARDIOVASCULAR COMPLICATION IN TYPE 2 DIABETES - A REVIEW
Kakadiya, J., & Township, A. (2009)
Regulation of pancreatic beta-cell function by the renin-angiotensin system in type 2 diabetes
Shoemaker, R. (2015) · UKnowledge (University of Kentucky)
Disfunção mitocondrial no tecido adiposo perivascular e seu papel nas alterações vasculares em modelo experimental de obesidade
da Costa, R. M. (2017) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.17.2017.tde-20072016-144840
Examination of metabolism in diabetic offspring
Russell, R. (2011) · Louisiana State University · doi:10.31390/gradschool_dissertations.1588
Obesity in the Pathophysiology of Diabetes
Paniagua, J. A., & Vidal‐Puig, A. (2019) · Springer eBooks · doi:10.1007/978-3-030-11815-0_13
Physiopathologie des états diabétiques
(2010) · Elsevier eBooks · doi:10.1016/b978-2-294-70868-8.50002-5
Physiopathologie des états diabétiques
(2014) · Elsevier eBooks · doi:10.1016/b978-2-294-73954-5.00002-0
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Alebrahimdehkordi, N., & Justus Liebig University Giessen (2021) · Universitätsbibliothek Gießen · doi:10.22029/jlupub-29
Physiopathologie des états diabétiques
(2019) · Elsevier eBooks · doi:10.1016/b978-2-294-75889-8.00002-6
Molecular evidence of the inhibitory potential of melatonin against sodium arsenite toxicity
Farhadi, R., Daniali, M., Baeeri, M., Khorasani, R., Haghi‐Aminjan, H., Gholami, M., Rahimifard, M., Nigjeh, M. N., & Abdollahi, M. R. (2025) · Heliyon · doi:10.1016/j.heliyon.2025.e42113
Glucotoxicity in insulin-producing β-cells.
Nyblom, H. K. (2007) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
The Role of Mitochondrial Uncoupling in the Development of Diabetic Nephropathy
Persson, M. F. (2012)
Role of Cell-cell Interactions and Palmitate on β-cells Function
Chowdhury, A. I. (2014) · Uppsala University Publications (Uppsala University)
FGFs and Wnts in pancreatic growth and β-cell function
Papadopoulou, S. (2005) · DiVA at Umeå University (Umeå University)
Uncoupling proteins : regulation by IGF-1 and neuroprotection during hyperglycemia in vitro.
Gustafsson, H. (2004) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Additional file 4 of Association of UCP1 and UCP2 variants with diabetic retinopathy susceptibility in type-2 diabetes mellitus patients: a meta-analysis
Liu, X., Jiang, Z., Zhang, G., Ng, T. K., & Wu, Z. (2021) · Figshare · doi:10.6084/m9.figshare.13979080
Les effets cellulaires des inhibiteurs de la protéase virale utilisés en thérapie anti-VIH sur le muscle strié squelettique humain.
Mercier, O. (2010) · theses.fr (ABES) · doi:10.70675/45632f96zc2adz4b7azbdfcza75ab5bdd7a5
A novel strategy for the treatment of Obesity using the small molecule ABX300, a modulator of the LMNA gene splicing
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Authors: Krauss, S., Zhang, C.-Y., Scorrano, L., Dalgaard, L. T., St-Pierre, J., Grey, S. T., & Lowell, B. B.
Affiliations: Beth Israel Deaconess Medical Center (US)
Roskilde University (DK)
Harvard University (US)
Corresponding author: Lowell, Bradford B.
ORCID: Scorrano, Luca
Dalgaard, Louise T.
Grey, Shane T.
Lowell, Bradford B.
Venue: Journal of Clinical Investigation
Publisher: American Society for Clinical Investigation
Published: 2003-12-15
Volume: 112
Issue: 12
Pages: 1831-1842
ISSN: 0021-9738 (ISSN-L)
DOI: 10.1172/jci200319774
PMC: PMC297000
OpenAlex: W2121338998
Cited by: 401
References: 52
Citations by year: 2026: 2 · 2025: 7 · 2024: 10 · 2023: 4 · 2022: 9 · 2021: 12 · 2020: 7 · 2019: 7 · 2018: 10 · 2017: 14 · 2016: 8 · 2015: 23 · 2014: 16 · 2013: 7 · 2012: 24
FWCI: 29.08
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Journal of Clinical Investigation (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Padua Research Archive (University of Padova) (submittedVersion)
Funders: American Diabetes Association
Sundhed og Sygdom, Det Frie Forskningsråd
National Institutes of Health
Medical Research Council
National Institute of Diabetes and Digestive and Kidney Diseases (R37DK053477)
Topics: Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
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: UCP2, superoxide, pancreatic beta cells, beta-cell dysfunction, glucose-stimulated insulin secretion, mitochondrial proton leak, mitochondrial superoxide production, ATP depletion, type 2 diabetes, obesity, hyperglycemia
MeSH terms: Uncoupling Protein 2, Insulin Secretion, Adenosine Triphosphate, Animals, Glucose, Hyperglycemia, Insulin, Ion Channels, Islets of Langerhans, Male, Membrane Potentials, Mitochondria, Obesity, Oxygen Consumption, Protons, Rhodamines, RNA, Messenger, Superoxides, Superoxide Dismutase, Thymus Gland, Time Factors, Mice, Knockout, Mitochondrial Proteins, Membrane Transport Proteins, Mice

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Superoxide-mediated activation of uncoupling protein 2 causes pancreatic β cell dysfunction

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