Mitochondrial ATP-synthase in the entorhinal cortex is a target of oxidative stress at stages I/II of Alzheimer’s disease pathology
Open accessAbstract
Oxidative stress has been implicated in the pathogenesis of several neurodegenerative diseases including Alzheimer's disease (AD). Several proteins have been identified as targets of oxidative damage in AD dementia (usually stages V/VI of Braak) and in subjects with mild cognitive impairment associated with middle stages of AD pathology (stage IV of Braak). In this study, we investigate whether brain proteins are locally modified by oxidative stress at the first stages of AD-related pathology when morphological lesions are restricted to the entorhinal and transentorhinal cortices of neurofibrillary pathology (stages I/II of Braak). Using a proteomic approach, we show that the alpha subunit of the mitochondrial adenosine triphosphate (ATP)-synthase is distinctly lipoxidized in the entorhinal cortex at Braak stages I/II compared with age-matched controls. In addition, ATP-synthase activity is significantly lower in Braak stages I/II than age-matched control, while electron transport chain, expressed by the mitochondrial complex I activity, remains not affected. This is the first study showing oxidative damage in the first stage, and clinically silent period, of AD-related pathology characterized by entorhinal and transentorhinal tauopathy.
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The activities of LDH, aconitase, and ATP synthase are significantly decreased as a result of oxidation.
“The activities of LDH, aconitase, and ATP synthase are significantly decreased as a result of oxidation [54,55,56,61]”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [61]
The Results (page unavailable) report a significant decrease in ATP-synthase activity in entorhinal cortex from AD Braak stage I/II cases, and the Discussion associates that loss with lipoxidative damage. The paper does not report decreased LDH or aconitase activity, so it supports only the ATP-synthase part of the claim. (LLM, conf=0.90)
Experimental — accuracy not yet measuredEntorhinal cortex neurons are particularly prone to damage by oxidative stress and mitochondrial dysfunction.
“In this view, entorhinal cortex (EC) neurons are particularly prone to damage by OS and mitochondria dysfunction [94,95].”
From Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery (2021) · cites this paper as [95]
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Cites
Braak, H., Alafuzoff, I., Arzberger, T., Kretzschmar, H., & Del Tredici, K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0127-z · Cited by 3,172 · see citing works
Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
Abrahams, J. P., Leslie, A. G. W., Lutter, R., & Walker, J. E. (1994) · Nature · doi:10.1038/370621a0 · Cited by 3,004 · see citing works
Stadtman, E. R. (1992) · Science · doi:10.1126/science.1355616 · Cited by 2,701 · see citing works
Oxidative stress hypothesis in Alzheimer’s disease
Markesbery, W. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00629-6 · Cited by 2,383 · see citing works
Srere, P. A. (1969) · Methods in Enzymology · doi:10.1016/0076-6879(69)13005-0 · Cited by 2,005 · see citing works
THE ATP SYNTHASE—A SPLENDID MOLECULAR MACHINE
Boyer, P. D. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.717 · Cited by 1,995 · see citing works
Oxidative Damage Is the Earliest Event in Alzheimer Disease
Nunomura, A., Perry, G., Aliev, G., Hirai, K., Takeda, A., Balraj, E. K., Jones, P. K., Ghanbari, H., Wataya, T., Shimohama, S., et al. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.8.759 · Cited by 1,885 · see citing works
Gene regulation and DNA damage in the ageing human brain
Lu, T., Pan, Y., Kao, S.-Y., Li, C., Kohane, I., Chan, J., & Yankner, B. A. (2004) · Nature · doi:10.1038/nature02661 · Cited by 1,874 · see citing works
The oxidative environment and protein damage
Davies, M. J. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.08.007 · Cited by 1,392 · see citing works
Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
Smith, M. A., Harris, P. L. R., Sayre, L. M., & Perry, G. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9866 · Cited by 1,357 · see citing works
Wyss-Coray (2006) · doi:10.1038/nm1484 · Cited by 1,284 · see citing works
4-Hydroxy-2-nonenal: a product and mediator of oxidative stress
Uchida, K. (2003) · Progress in Lipid Research · doi:10.1016/s0163-7827(03)00014-6 · Cited by 1,164 · see citing works
Oxidative stress in Alzheimer’s disease
Smith, M. A., Rottkamp, C. A., Nunomura, A., Raina, A. K., & Perry, G. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00040-5 · Cited by 895 · see citing works
Mark, R. J., Lovell, M. A., Markesbery, W. R., Uchida, K., & Mattson, M. P. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68010255.x · Cited by 781 · see citing works
Advanced Maillard reaction end products are associated with Alzheimer disease pathology.
Smith, M. A., Taneda, S., Richey, P. L., Miyata, S., Yan, S. D., Stern, D., Sayre, L. M., Monnier, V. M., & Perry, G. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.12.5710 · Cited by 715 · see citing works
Early Aβ accumulation and progressive synaptic loss, gliosis, and tangle formation in AD brain
Ingelsson, M., Fukumoto, H., Newell, K. L., Growdon, J. H., Hedley–Whyte, E. T., Frosch, M. P., Albert, M. S., Hyman, B. T., & Irizarry, M. C. (2004) · Neurology · doi:10.1212/01.wnl.0000115115.98960.37 · Cited by 666 · see citing works
Chemistry and Biochemistry of Oxidative Stress in Neurodegenerative Disease
Sayre, L. M., Smith, M. A., & Perry, G. L. (2001) · Current Medicinal Chemistry · doi:10.2174/0929867013372922 · Cited by 614 · see citing works
Involvement of oxidative stress in Alzheimer disease
Nunomura, A., Castellani, R. J., Zhu, X., Moreira, P. I., Perry, G., & Smith, M. A. (2006) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/01.jnen.0000228136.58062.bf · Cited by 611 · see citing works
Glycated tau protein in Alzheimer disease: a mechanism for induction of oxidant stress.
Yan, S. D., Chen, X., Schmidt, A. M., Brett, J., Godman, G., Zou, Y. S., Scott, C. W., Caputo, C., Frappier, T., & Smith, M. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.16.7787 · Cited by 565 · see citing works
Evidence of increased oxidative damage in subjects with mild cognitive impairment
Keller, J. N., Schmitt, F. A., Scheff, S. W., Ding, Q., Chen, Q., Butterfield, D. A., & Markesbery, W. R. (2005) · Neurology · doi:10.1212/01.wnl.0000156156.13641.ba · Cited by 539 · see citing works
Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer's disease
Lovell, M. A., & Markesbery, W. R. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm821 · Cited by 515 · see citing works
A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients
Maurer, I. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00112-3 · Cited by 475 · see citing works
Elevated 4-Hydroxynonenal in Ventricular Fluid in Alzheimer’s Disease
Lovell, M. A., Ehmann, W. D., Mattson, M. P., & Markesbery, W. R. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00108-5 · Cited by 413 · see citing works
Williams, T. I., Lynn, B. C., Markesbery, W. R., & Lovell, M. A. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.06.004 · Cited by 391 · see citing works
Mild cognitive impairment: transition between aging and Alzheimer's disease.
Petersen, R. C. (2000) · PubMed · Cited by 383 · see citing works
Butterfield, D. A., Poon, H. F., St. Clair, D., Keller, J. N., Pierce, W. M., Klein, J. B., & Markesbery, W. R. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.11.002 · Cited by 377 · see citing works
Identification of nitrated proteins in Alzheimer’s disease brain using a redox proteomics approach
Sultana, R., Poon, H. F., Cai, J., Pierce, W. M., Merchant, M., Klein, J. B., Markesbery, W. R., & Butterfield, D. A. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.10.004 · Cited by 364 · see citing works
Bosetti, F. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00314-1 · Cited by 348 · see citing works
Abnormalities of mitochondrial enzymes in Alzheimer disease
Gibson, G. E., Sheu, K.-F. R., & Blass, J. P. (1998) · Journal of Neural Transmission · doi:10.1007/s007020050099 · Cited by 345 · see citing works
Rukhsana Sultana, A., Debra Boyd-kimball, A., Poon, H. F., Cai, J., Pierce, W. M. J., Klein, J. B., Merchant, M. L., Markesbery, W. R., & Butterfield, D. A. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.09.021 · Cited by 334 · see citing works
Analysis of microtubule-associated protein tau glycation in paired helical filaments.
Ledesma, M. D., Bonay, P., Colaço, C., & Avila, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31849-5 · Cited by 333 · cited 1× · see citing works
“Increased levels of glycation end products and lipid peroxidation markers have been observed in brains of patients with AD in association with NFTs and Ab deposits (23, 47, 56).”
BackgroundThe rotary mechanism of ATP synthase
Stock, D., Gibbons, C., Aréchaga, I., Leslie, A. G. W., & Walker, J. E. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00147-0 · Cited by 325 · see citing works
Giasson, B. I., Ischiropoulos, H., Lee, V. M. ‐., & Trojanowski, J. Q. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00804-3 · Cited by 281 · see citing works
Proteins in Human Brain Cortex Are Modified by Oxidation, Glycoxidation, and Lipoxidation
Pamplona, R., Dalfó, E., Ayala, V., Bellmunt, M. J., Prat, J., Ferrer, I., & Portero‐Otín, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502255200 · Cited by 278 · see citing works
Self-citationReed, T., Perluigi, M., Sultana, R., Pierce, W. M., Klein, J. B., Turner, D. M., Coccia, R., Markesbery, W. R., & Butterfield, D. A. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.12.007 · Cited by 257 · see citing works
Mild Cognitive Impairment: A Systematic Review
Mariani, E., Monastero, R., & Mecocci, P. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-12104 · Cited by 248 · see citing works
Butterfield, D. A., Reed, T., Perluigi, M., De Marco, C., Coccia, R., Cini, C., & Sultana, R. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2005.12.017 · Cited by 246 · see citing works
HUTTER, E., RENNER, K., PFISTER, G., STÖCKL, P., JANSEN-DÜRR, P., & GNAIGER, E. (2004) · Biochemical Journal · doi:10.1042/bj20040095 · Cited by 235 · see citing works
The α-ketoglutarate dehydrogenase complex in neurodegeneration
Gibson, G. E., Park, L. C. H., Sheu, K. R., Blass, J. P., & Calingasan, N. Y. (2000) · Neurochemistry International · doi:10.1016/s0197-0186(99)00114-x · Cited by 199 · see citing works
Gibson, G. E., Blass, J. P., Beal, M. F., & Bunik, V. I. (2005) · Molecular Neurobiology · doi:10.1385/mn:31:1-3:043 · Cited by 178 · see citing works
Evaluation of Mitochondrial Respiratory Function in Small Biopsies of Liver
Kuznetsov, A. V., Strobl, D., Ruttmann, E., Königsrainer, A., Margreiter, R., & Gnaiger, E. (2002) · Analytical Biochemistry · doi:10.1006/abio.2002.5658 · Cited by 137 · see citing works
Renner, K., Amberger, A., Konwalinka, G., Kofler, R., & Gnaiger, E. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(03)00105-8 · Cited by 123 · see citing works
Butterfield, D. A., Gnjec, A., Poon, H. F., Castegna, A., Pierce, W. M. J., Klein, J. B., & Martins, R. N. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-10407 · Cited by 120 · see citing works
Oxidative modification of proteins in the frontal cortex of Alzheimer's disease brain
Korolainen, M. A., Goldsteins, G., Nyman, T. A., Alafuzoff, I. I., Koıstınaho, J., & Pirttilä, T. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.11.010 · Cited by 103 · see citing works
Neurodegeneration: The Molecular Pathology of Dementia and Movement Disorders
MNH (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.6.677 · Cited by 103 · see citing works
Oxidative Damage, Protein Synthesis, and Protein Degradation in Alzheimers Disease
Ding, Q., Dimayuga, E. R., & Keller, J. N. (2007) · Current Alzheimer Research · doi:10.2174/156720507779939788 · Cited by 95 · see citing works
Temporal Sequence of Alzheimer’s Disease-Related Pathology
Braak, H., & Braak, E. (1999) · Cerebral cortex · doi:10.1007/978-1-4615-4885-0_14 · Cited by 94 · see citing works
Hyun, D., Lee, M., Halliwell, B. B., & Jenner, P. G. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01125.x · Cited by 93 · see citing works
Oxidatively modified RNA in mild cognitive impairment
Lovell, M. A., & Markesbery, W. R. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.07.030 · Cited by 93 · see citing works
Neuropathology of mild cognitive impairment
Saito, Y., & Murayama, S. (2007) · Neuropathology · doi:10.1111/j.1440-1789.2007.00806.x · Cited by 92 · see citing works
Sultana, R., Reed, T., Perluigi, M., Coccia, R., Pierce, W. M., & Butterfield, D. A. (2007) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2007.00065.x · Cited by 87 · see citing works
Naudí, A., Caro, P., Jové, M., Gómez, J., Boada, J., Ayala, V., Portero‐Otín, M., Barja, G., & Pamplona, R. (2007) · Rejuvenation Research · doi:10.1089/rej.2007.0538 · Cited by 85 · see citing works
Self-citationIron, copper, and iron regulatory protein 2 in Alzheimer's disease and related dementias
Magaki, S., Raghavan, R., Mueller, C., Oberg, K. C., Vinters, H. V., & Kirsch, W. M. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.02.077 · Cited by 77 · see citing works
[2] Preparation and properties of NADH: Cytochrome c oxidoreductase (complex I–III)
Hatefi, Y., & Stiggall, D. L. (1978) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(78)53005-x · Cited by 73 · see citing works
Dystrophic neurites of senile plaques in Alzheimer’s disease are deficient in cytochrome c oxidase
Pérez-Gracia, E., Torrejón-Escribano, B., & Ferrer, I. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0370-6 · Cited by 71 · see citing works
Self-citationCharacterization of 8‐Epiprostaglandin F2α as aMarker of Amyloid β‐Peptide‐Induced Oxidative Damage
Mark, R. J., Fuson, K. S., & May, P. C. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0721146.x · Cited by 46 · see citing works
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Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., & Collin, F. (2018) · Redox Biology · doi:10.1016/j.redox.2017.10.014 · Cited by 2,185 · see citing works
Sultana, R., Perluigi, M., & Butterfield, D. A. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.027 · Cited by 478 · see citing works
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Tramutola, A., Lanzillotta, C., Perluigi, M., & Butterfield, D. A. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.06.005 · Cited by 303 · see citing works
Parallel findings in age-related macular degeneration and Alzheimer’s disease
Ohno-Matsui, K. (2011) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2011.02.004 · Cited by 280 · see citing works
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Jové, M., Portero-Otín, M., Naudí, A., Ferrer, I., & Pamplona, R. (2014) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000091 · Cited by 195 · see citing works
Self-citationBlanch, M., Mosquera, J. L., Ansoleaga, B., Ferrer, I., & Barrachina, M. (2016) · The American Journal of Pathology · doi:10.1016/j.ajpath.2015.10.004 · Cited by 192 · see citing works
Self-citationBuccellato, F. R., D’Anca, M., Fenoglio, C., Scarpini, E., & Galimberti, D. (2021) · Antioxidants · doi:10.3390/antiox10091353 · Cited by 179 · see citing works
Ferrer, I. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.03.005 · Cited by 174 · see citing works
Self-citationCha, M.-Y., Cho, H. J., Kim, C., Jung, Y. O., Kang, M. J., Murray, M. E., Hong, H. S., Choi, Y.-J., Choi, H., Kim, D. K., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv358 · Cited by 95 · see citing works
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Butterfield, D. A., & Boyd-Kimball, D. (2020) · Antioxidants · doi:10.3390/antiox9090818 · Cited by 85 · see citing works
“These include the tricarboxylic acid cycle enzymes aconitase in late AD [54] and malate dehydrogenase (MDH) in early AD [55] and the alpha-subunit of ATP synthase, or complex V of the electron transport chain, in MCI [56], early AD [55,61], and late AD [54,57].”
BackgroundOxidative stress damage and oxidative stress responses in the choroid plexus in Alzheimer’s disease
Perez-Gracia, E., Blanco, R., Carmona, M., Carro, E., & Ferrer, I. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0574-4 · Cited by 63 · see citing works
Self-citationWalia, V., Kaushik, D., Mittal, V., Kumar, K., Verma, R., Parashar, J., Akter, R., Rahman, M. H., Bhatia, S., Al-Harrasi, A., et al. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02617-1 · Cited by 47 · see citing works
Identification of metabolism-related subtypes and feature genes in Alzheimer’s disease
Lian, P., Cai, X., Wang, C., Liu, K., Yang, X., Wu, Y., Zhang, Z., Ma, Z., Cao, X., & Xu, Y. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04324-y · Cited by 29 · see citing works
- Authors
- Terni, B., Boada, J., Portero‐Otin, M., Pamplona, R., & Ferrer, I.
- Affiliations
- Bellvitge University Hospital (ES)
- Universitat de Lleida (ES)
- Venue
- Brain Pathology
- Publisher
- Wiley
- Published
- 2009-12-07
- Volume
- 20
- Issue
- 1
- Pages
- 222-233
- ISSN
- 1015-6305 (ISSN-L)
- 1750-3639
- PMC
- PMC8094794
- OpenAlex
- W2130376265
- Cited by
- 159
- References
- 56
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 13 · 2023: 13 · 2022: 12 · 2021: 21 · 2020: 12 · 2019: 4 · 2018: 9 · 2017: 7 · 2016: 12 · 2015: 2 · 2014: 6 · 2013: 7 · 2012: 12
- FWCI
- 6.63
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Brain Pathology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Repositori ObertUDL (University of Lleida) (publishedVersion)
- RECERCAT (Consorci de Serveis Universitaris de Catalunya) (submittedVersion)
- Funders
- “la Caixa” Foundation
- European Commission
- Generalitat de Catalunya
- Universitat de Barcelona
- Fundación Bancaria Caixa d'Estalvis i Pensions de Barcelona
- Instituto de Salud Carlos III
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, oxidative stress, mitochondrial ATP synthase, entorhinal cortex, transentorhinal cortex, lipid oxidation, Braak stages, neurofibrillary pathology, tauopathy, mitochondrial complex I, electron transport chain, early Alzheimer's disease, mild cognitive impairment
- MeSH terms
- Adenosine Triphosphatases, Aged, Alzheimer Disease, Borohydrides, Carrier Proteins, Female, Humans, Hydrolysis, Male, Membrane Proteins, Middle Aged, Mitochondria, Mass Spectrometry, Trypsin, Blotting, Western, Electrophoresis, Gel, Two-Dimensional, Lipid Peroxidation, Neurofibrillary Tangles, Oxidative Stress, Disease Progression, Microscopy, Confocal, Entorhinal Cortex, Fluorescent Antibody Technique, Direct, Mitochondrial Proton-Translocating ATPases
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