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Cytochrome c oxidase is decreased in Alzheimer’s disease platelets
Abstract
Cytochrome c oxidase (COX) activity reportedly is reduced in Alzheimer's disease (AD) brain and platelets. The reasons for the defect in either tissue are unknown, but its presence in a non-degenerating tissue suggests it is not simply a consequence of neurodegeneration. We now offer confirmation of the AD platelet COX defect. Compared to age-matched controls, in mitochondria isolated from AD platelets there was a 15% decrease in COX activity despite the fact that COX subunits were present at normal levels. Platelet ATP levels were diminished in AD (from 11.33 +/- 0.52 to 9.11 +/- 0.72 nmol/mg), while reactive oxygen species (ROS) were increased (from 97.03 +/- 25.9 to 338.3 +/- 100 K/mg). Platelet membrane fluidity, Vitamin E, and cholesterol content were similar between groups. We conclude that COX catalytic activity is indeed diminished in AD platelet mitochondria, does not result from altered membrane fluidity, and is associated with ROS overproduction and ATP under-production.
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“however, in mitochondria isolated from AD platelets, the activity of complex IV, or cytochrome c oxidase, is significantly decreased [109,110,111]”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [110]
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Cites
Sequence and organization of the human mitochondrial genome
Anderson, S., Bankier, A. T., Barrell, B. G., de Bruijn, M. H. L., Coulson, A. R., Drouin, J., Eperon, I. C., Nierlich, D. P., Roe, B. A., Sanger, F., et al. (1981) · Nature · doi:10.1038/290457a0 · Cited by 9,740
A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250
SEDMAK, J. J., & Grossberg, S. E. (1977) · Analytical Biochemistry · doi:10.1016/0003-2697(77)90428-6 · Cited by 3,019
Reactive Oxygen Species and the Central Nervous System
Halliwell, B. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb10990.x · Cited by 2,947
Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626
Oxidative damage and mitochondrial decay in aging.
Shigenaga, M. K., Hagen, T. M., & Ames, B. N. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.10771 · Cited by 2,055
Fluidity parameters of lipid regions determined by fluorescence polarization
Shinitzky, M., & Barenholz, Y. (1978) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(78)90010-2 · Cited by 1,885
Bass, D., Parce, J. W., DeChatelet, L. R., Szejda, P., Seeds, M. C., & Thomas, M. (1983) · The Journal of Immunology · doi:10.4049/jimmunol.130.4.1910 · Cited by 1,811
[45] Cytochrome oxidase from beef heart mitochondria
Wharton, D. C., & Tzagoloff, A. (1967) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(67)10048-7 · Cited by 1,264
Beal, M. F. (1992) · Annals of Neurology · doi:10.1002/ana.410310202 · Cited by 962
Lipid peroxidation damage to cell components.
Tappel, A. L. (1973) · PubMed · Cited by 902
Research works printed but not linked: 1
- Ragan CI, Wilson MT, Darley-Usmar VM, Lowe PN. Subfractionation of mitochondria, and isolation of the proteins of oxidative phosphorylation. In: Mitochondria, a practical approach. London: IRL Press; 1987. p. 79–112.
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Leuner, K., Pantel, J., Frey, C., Schindowski, K., Schulz, K. L., Wegat, T., Maurer, K., Eckert, A., & Müller, W. E. G. (2007) · Springer eBooks · doi:10.1007/978-3-211-73574-9_27 · Cited by 74
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Teo, E., Ravi, S., Barardo, D., Kim, H.-S., Fong, S., Cazenave-Gassiot, A., Tan, T. Y., Ching, J., Kovalik, J.-P., Wenk, M. R., et al. (2019) · eLife · doi:10.7554/elife.50069 · Cited by 72
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Mosconi, L., Glodzik, L., Mistur, R., McHugh, P., Rich, K. E., Javier, E., Williams, S., Pirraglia, E., De Santi, S., Mehta, P. D., et al. (2010) · Biological Psychiatry · doi:10.1016/j.biopsych.2010.07.011 · Cited by 46
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Ortiz, G. G., Pacheco-Moisés, F. P., Hafidi, M. E., Jiménez-Delgado, A., Macías-Islas, M. Á., Rosales‐Corral, S., de la Rosa, A. C., Sánchez-González, V., Arias‐Merino, E. D., & Velázquez-Brizuela, I. E. (2008) · Disease Markers · doi:10.1155/2008/642120 · Cited by 28
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de Morais, F. M., Ribeiro, A. M., Moreira, F. A., & Silva, P. V. G. (2020) · Acta Neuropsychiatrica · doi:10.1017/neu.2020.43 · Cited by 27
Yoshida, N., Kato, Y., Takatsu, H., & Fukui, K. (2022) · Biomedicines · doi:10.3390/biomedicines10020281 · Cited by 23
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Vevera, J., Fišar, Z., Nekovářová, T., Vrablı́k, M., Zlatohlávek, L., Hroudová, J., Singh, N., Raboch, J., & Valeš, K. (2016) · Physiological Research · doi:10.33549/physiolres.933264 · Cited by 24
Correia, S. C., Machado, N. J., Alves, M. G., Oliveira, P. F., & Moreira, P. I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22010461 · Cited by 25
Malishev, R., Nandi, S., Śmiłowicz, D., Bakavayev, S., Engel, S., Bujanover, N., Gazit, R., Metzler‐Nolte, N., & Jelinek, R. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00177 · Cited by 21
Moreira, P. I., Zhu, X., Lee, H., Honda, K., Smith, M. A., & Perry, G. L. (2006) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2006.01.024 · Cited by 22
Jung, M. E., Agarwal, R., & Simpkins, J. W. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.01.065 · Cited by 22
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Chadha, S., Behl, T., Sehgal, A., Kumar, A., & BUNGAU, S. G. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.11.008 · Cited by 20
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Duce, J. A., Bush, A. I., & Adlard, P. A. (2011) · Future Neurology · doi:10.2217/fnl.11.43 · Cited by 20
Gomez‐Virgilio, L., Luarte, A., Ponce, D. P., Bruna, B., & Behrens, M. I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126311 · Cited by 18
Omori, C., Motodate, R., Shiraki, Y., Chiba, K., Sobu, Y., Kimura, A., Nakaya, T., Kondo, H., Kurumiya, S., Tanaka, T., et al. (2016) · Nutritional Neuroscience · doi:10.1080/1028415x.2016.1199114 · Cited by 20
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Moreira, P. I., Nunomura, A., Honda, K., Aliev, G. M., Casadesús, G., Zhu, X., Smith, M. A., & Perry, G. L. (2007) · Elsevier eBooks · doi:10.1016/b978-044452809-4/50153-8 · Cited by 18
Martínez, T., & Pascual, A. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05646.x · Cited by 18
Sangüesa, G., Batlle, M., Muñoz‐Moreno, E., Sòria, G., Alcarraz, A., Rubies, C., Sitjà‐Roqueta, L., Solana, E., Martínez‐Heras, E., Meza‐Ramos, A., et al. (2022) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14912 · Cited by 16
Kugler, B. A., Lysaker, C. R., Franczak, E., Hauger, B. M., Csikós, V., Stopperan, J. A., Allen, J., Stanford, J. A., Koch, L. G., Britton, S. L., et al. (2024) · GeroScience · doi:10.1007/s11357-024-01248-3 · Cited by 17
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Shen, Y., Wang, Y., Yu, G., Liu, C., Zhang, Z., & Zhang, L. (2013) · Neurotoxicity Research · doi:10.1007/s12640-012-9370-3 · Cited by 17
Bobba, A., Amadoro, G., Petragallo, V. A., Calissano, P., & Atlante, A. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.04.001 · Cited by 17
Dynamic Interplay between Copper Toxicity and Mitochondrial Dysfunction in Alzheimer’s Disease
Tassone, G., Kola, A., Valensin, D., & Pozzi, C. (2021) · Life · doi:10.3390/life11050386 · Cited by 16
Detection of Alzheimer's disease by Raman spectra of rat's platelet with a simple feature selection
Park, A., Baek, S., Shen, A., & Hu, J. (2012) · Chemometrics and Intelligent Laboratory Systems · doi:10.1016/j.chemolab.2012.11.011 · Cited by 16
Schadauer, F., Geiss, A. F., Srajer, J., Siebenhofer, B., Frank, P., Reiner‐Rozman, C., Ludwig, B., Richter, O. H., Nowak, C., & Naumann, R. L. C. (2015) · Langmuir · doi:10.1021/la504417j · Cited by 16
Shi, C., Zou, J., Li, G., Zhenying, G., Yao, Z., & Xu, J. (2010) · Journal of Molecular Neuroscience · doi:10.1007/s12031-010-9388-z · Cited by 15
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Metadata
- Authors
- Cardoso, S. M., Proença, M. T., Santos, S., Santana, I., & Oliveira, C. R.
- Affiliations
- University of Coimbra (PT)
- Unidade Local de Saúde de Coimbra (PT)
- Corresponding author
- Oliveira, Catarina R
- Venue
- Neurobiology of Aging
- Publisher
- Elsevier BV
- Published
- 2004-01
- Volume
- 25
- Issue
- 1
- Pages
- 105-110
- ISSN
- 0197-4580 (ISSN-L)
- OpenAlex
- W2072453593
- Cited by
- 281
- References
- 38
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 9 · 2023: 15 · 2022: 13 · 2021: 16 · 2020: 14 · 2019: 16 · 2018: 7 · 2017: 9 · 2016: 14 · 2015: 10 · 2014: 13 · 2013: 22 · 2012: 17
- FWCI
- 3.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neurobiology of Aging (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
- Keywords
- cytochrome c oxidase, Alzheimer's disease, platelets, mitochondrial dysfunction, ATP production, reactive oxygen species, platelet mitochondria, platelet membrane fluidity, vitamin E, cholesterol
- MeSH terms
- Adenine Nucleotides, Adenosine Triphosphate, Aged, Alzheimer Disease, Blood Platelets, Cholesterol, Chromatography, High Pressure Liquid, Citrate (si)-Synthase, Electron Transport Complex IV, Free Radicals, Humans, Middle Aged, Mitochondria, NADP, Succinate Cytochrome c Oxidoreductase, Vitamin E, Electrophoresis, Gel, Two-Dimensional, Case-Control Studies, Age of Onset, Electron Transport Complex I
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