The amyloid β-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae
Open accessAbstract
The amyloid beta-peptide (Abeta) has been suggested to exert its toxicity intracellularly. Mitochondrial functions can be negatively affected by Abeta and accumulation of Abeta has been detected in mitochondria. Because Abeta is not likely to be produced locally in mitochondria, we decided to investigate the mechanisms for mitochondrial Abeta uptake. Our results from rat mitochondria show that Abeta is transported into mitochondria via the translocase of the outer membrane (TOM) machinery. The import was insensitive to valinomycin, indicating that it is independent of the mitochondrial membrane potential. Subfractionation studies following the import experiments revealed Abeta association with the inner membrane fraction, and immunoelectron microscopy after import showed localization of Abeta to mitochondrial cristae. A similar distribution pattern of Abeta in mitochondria was shown by immunoelectron microscopy in human cortical brain biopsies obtained from living subjects with normal pressure hydrocephalus. Thus, we present a unique import mechanism for Abeta in mitochondria and demonstrate both in vitro and in vivo that Abeta is located to the mitochondrial cristae. Importantly, we also show that extracellulary applied Abeta can be internalized by human neuroblastoma cells and can colocalize with mitochondrial markers. Together, these results provide further insight into the mitochondrial uptake of Abeta, a peptide considered to be of major significance in Alzheimer's disease.
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Intracellular Aβ may enter mitochondria and induce additional RS and magnify metabolic deficit.
“Intracellular Aβ may then enter the mitochondria in which it induces additional RS and magnifies the metabolic deficit”
From The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer’s disease (2011) · cites this paper as Hansson Petersen et al., 2008
APP and Aβ, as well as the entire γ-secretase complex, physically associate with mitochondria and can effect changes in mitochondrial function.
“accumulating data certainly do suggest APP and Aβ, as well as the entire γ-secretase complex, physically associate with mitochondria and can effect changes in mitochondrial function [58-67].”
From The Alzheimer’s disease mitochondrial cascade hypothesis: progress and perspectives (2014) · cites this paper as [66]
Cites
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431 · see citing works
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works
Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876 · see citing works
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506 · see citing works
Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91209-9 · Cited by 1,693 · see citing works
Translocation of Proteins into Mitochondria
Neupert, W., & Herrmann, J. M. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.163409 · Cited by 1,486 · see citing works
Mitochondrial abnormalities in Alzheimer's disease
Hirai, K., Aliev, G., Nunomura, A., Fujioka, H., Russell, R. L., Atwood, C. S., Johnson, A. B., Kress, Y., Vinters, H. V., Tabaton, M., et al. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-09-03017.2001 · Cited by 1,367 · see citing works
ABAD Directly Links Aß to Mitochondrial Toxicity in Alzheimer's Disease
Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., et al. (2004) · Science · doi:10.1126/science.1091230 · Cited by 1,303 · see citing works
Manczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., & Reddy, P. H. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl066 · Cited by 1,104 · see citing works
A TECHNIQUE FOR ULTRACRYOTOMY OF CELL SUSPENSIONS AND TISSUES
Tokuyasu, K. T. (1973) · The Journal of Cell Biology · doi:10.1083/jcb.57.2.551 · Cited by 1,080 · see citing works
Intraneuronal Aβ42 Accumulation in Human Brain
Gouras, G. K., Tsai, J., Naslund, J., Vincent, B., Edgar, M., Checler, F., Greenfield, J. P., Haroutunian, V., Buxbaum, J. D., Xu, H., et al. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64700-1 · Cited by 991 · see citing works
Brain glucose metabolism in the early and specific diagnosis of Alzheimer?s disease
Mosconi, L. (2005) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-005-1762-7 · Cited by 900 · see citing works
Devi, L., Prabhu, B. M., Galati, D. F., Avadhani, N. G., & Anandatheerthavarada, H. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1469-06.2006 · Cited by 792 · see citing works
γ-Secretase is a membrane protein complex comprised of presenilin, nicastrin, aph-1, and pen-2
Kimberly, W. T., LaVoie, M. J., Ostaszewski, B. L., Ye, W., Wolfe, M. S., & Selkoe, D. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1037392100 · Cited by 763 · see citing works
Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
Caspersen, C., Wang, N., Yao, J., Sosunov, A., Chen, X., Lustbader, J. W., Xu, H. W., Stern, D., McKhann, G., & Du Yan, S. (2005) · The FASEB Journal · doi:10.1096/fj.05-3735fje · Cited by 738 · see citing works
Mitochondrial abnormalities in Alzheimer brain: Mechanistic implications
Bubber, P., Haroutunian, V., Fisch, G., Blass, J. P., & Gibson, G. E. (2005) · Annals of Neurology · doi:10.1002/ana.20474 · Cited by 622 · see citing works
Cytochrome oxidase deficiency in Alzheimer’s disease
Parker, W. D., Filley, C. M., & Parks, J. K. (1990) · Neurology · doi:10.1212/wnl.40.8.1302 · Cited by 598 · see citing works
Anandatheerthavarada, H. K., Biswas, G., Robin, M.-A., & Avadhani, N. G. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207030 · Cited by 571 · see citing works
Brain cytochrome oxidase in Alzheimer's disease
Kish, S. J., Bergeron, C., Rajput, A., Dozic, S., Mastrogiacomo, F., Chang, L., Wilson, J. M., DiStefano, L. M., & Nobrega, J. N. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb09439.x · Cited by 537 · see citing works
Rasola, A., & Bernardi, P. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0723-y · Cited by 507 · see citing works
The Oligomerization of Amyloid β-Protein Begins Intracellularly in Cells Derived from Human Brain
Walsh, D. M., Tseng, B. P., Rydel, R. E., Podlisny, M. B., & Selkoe, D. J. (2000) · Biochemistry · doi:10.1021/bi001048s · Cited by 502 · see citing works
Oligomerization of Alzheimer's β-Amyloid within Processes and Synapses of Cultured Neurons and Brain
Takahashi, R. H., Almeida, C. G., Kearney, P. F., Yu, F., Lin, M. T., Milner, T. A., & Gouras, G. K. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.5167-03.2004 · Cited by 445 · see citing works
Wirths, O., Multhaup, G., & Bayer, T. A. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02737.x · Cited by 349 · see citing works
Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease
Gouras, G. K., Almeida, C. G., & Takahashi, R. H. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.05.022 · Cited by 338 · see citing works
Crouch, P. J., Blake, R., Duce, J. A., Ciccotosto, G. D., Li, Q.-X., Barnham, K. J., Curtain, C. C., Cherny, R. A., Cappai, R., Dyrks, T., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4276-04.2005 · Cited by 327 · see citing works
Mitochondria dysfunction of Alzheimer's disease cybrids enhances Aβ toxicity
Cardoso, S. M., Santana, I. J., Swerdlow, R. H., & Oliveira, C. R. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02438.x · Cited by 262 · see citing works
Immunocytochemistry-Modern methods and applications
(1990) · Plant Growth Regulation · doi:10.1007/bf00024923 · Cited by 252 · see citing works
Mechanisms of Protein Import into Mitochondria
Truscott, K. N., Brandner, K., & Pfanner, N. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00239-2 · Cited by 225 · see citing works
Degradation of the Amyloid β-Protein by the Novel Mitochondrial Peptidasome, PreP
Falkevall, A., Alikhani, N., Bhushan, S., Pavlov, P. F., Busch, K., Johnson, K. A., Eneqvist, T., Tjernberg, L. O., Ankarcrona, M., & Glaser, E. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602532200 · Cited by 202 · see citing works
Self-citationCytochrome C Oxidase in Alzheimer's Disease Brain: Purification and Characterization
Parker, W. D., & Parks, J. K. (1995) · Neurology · doi:10.1212/wnl.45.3.482 · Cited by 142 · see citing works
Mattiasson, G., Friberg, H., Hansson, M. J., Elmér, E., & Wieloch, T. W. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02026.x · Cited by 120 · see citing works
Internalization of β-Amyloid Peptide by Primary Neurons in the Absence of Apolipoprotein E
Saavedra, L., Mohamed, A., Ma, V., Kar, S., & de Chaves, E. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701823200 · Cited by 118 · see citing works
Insights into amyloid-β-induced mitochondrial dysfunction in Alzheimer disease
Wang, X., Su, B., Perry, G. L., Smith, M. A., & Zhu, X. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.09.007 · Cited by 102 · see citing works
Insertion of Hydrophobic Membrane Proteins into the Inner Mitochondrial Membrane—A Guided Tour
Rehling, P., Pfanner, N., & Meisinger, C. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01440-7 · Cited by 89 · see citing works
Sirk, D. P., Zhu, Z., Wadia, J. S., Shulyakova, N., Phan, N., Fong, J. C., & Mills, L. R. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04907.x · Cited by 78 · see citing works
Södersten, F., Ekman, S., Eloranta, M., Heinegård, D. K., Dudhia, J., & Hultenby, K. R. (2005) · Matrix Biology · doi:10.1016/j.matbio.2005.06.003 · Cited by 69 · see citing works
Söderberg, L., Bogdanović, N., Axelsson, B., Winblad, B. G., Näslund, J., & Tjernberg, L. O. (2006) · Biochemistry · doi:10.1021/bi060331+ · Cited by 38 · see citing works
Self-citationStable insertion of Alzheimer Aβ peptide into the ER membrane strongly correlates with its length
Lundin, C., Johansson, S., Johnson, A. E., Näslund, J., von HEIJNE, G., & Nilsson, I. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.07.003 · Cited by 8 · see citing works
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Mangialasche, F., Solomon, A., Winblad, B., Mecocci, P., & Kivipelto, M. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70119-8 · Cited by 1,217 · see citing works
Self-citationMitochondria and Mitochondrial Cascades in Alzheimer’s disease
Swerdlow, R. H. (2018) · Journal of Alzheimer’s Disease · doi:10.3233/jad-170585 · Cited by 850 · see citing works
The Alzheimer’s disease mitochondrial cascade hypothesis: progress and perspectives
Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.010 · Cited by 786 · see citing works
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Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100339 · Cited by 562 · see citing works
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Liu, J., Chang, L., Song, Y., Li, H., & Wu, Y. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00043 · Cited by 535 · see citing works
Hedskog, L., Pinho, C. M., Filadi, R., Rönnbäck, A., Hertwig, L., Wiehager, B., Larssen, P., Gellhaar, S., Sandebring, A., Westerlund, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300677110 · Cited by 478 · see citing works
Self-citationAmyloid toxicity in Alzheimer’s disease
Reiss, A. B., Arain, H. A., Stecker, M. M., Siegart, N. M., & Kasselman, L. J. (2018) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0063 · Cited by 447 · see citing works
McManus, M. J., Murphy, M. P., & Franklin, J. L. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.0552-11.2011 · Cited by 432 · see citing works
Reddy, P. H., Tripathi, R., Troung, Q., Tirumala, K., Reddy, T. P., Anekonda, V., Shirendeb, U. P., Calkins, M. J., Reddy, A. P., Mao, P., et al. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.011 · Cited by 394 · see citing works
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Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383 · see citing works
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Gouras, G. K., Tampellini, D., Takahashi, R. H., & Capetillo-Zarate, E. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0679-9 · Cited by 372 · see citing works
Manczak, M., & Reddy, P. H. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds360 · Cited by 348 · see citing works
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Takuma, K., Fang, F., Zhang, W., Yan, S., Fukuzaki, E., Du, H., Sosunov, A., McKhann, G., Funatsu, Y., Nakamichi, N., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905686106 · Cited by 290 · see citing works
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- Authors
- Hansson Petersen, C. A., Alikhani, N., Behbahani, H., Wiehager, B., Pavlov, P. F., Alafuzoff, I., Leinonen, V., Ito, A., Winblad, B., Glaser, E., & Ankarcrona, M.
- Affiliations
- *Karolinska Institutet Dainippon Sumitomo Pharma Alzheimer Center, NVS, Novum, 141 57 Huddinge, Sweden;
- Stockholm University (SE)
- Karolinska Institutet (SE)
- Kuopio University Hospital (FI)
- Department of Neurosurgery, 70211 Kuopio, Finland; and
- Dainippon Sumitomo Pharma Company Ltd., 564-0053 Osaka, Japan
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2008-09-02
- Volume
- 105
- Issue
- 35
- Pages
- 13145-13150
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2527349
- OpenAlex
- W2170398463
- Cited by
- 693
- References
- 38
- Citations by year
- 2026: 25 · 2025: 34 · 2024: 26 · 2023: 51 · 2022: 43 · 2021: 49 · 2020: 48 · 2019: 36 · 2018: 38 · 2017: 36 · 2016: 35 · 2015: 32 · 2014: 36 · 2013: 32 · 2012: 52
- FWCI
- 26.86
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- 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 › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- amyloid-beta, mitochondrial protein import, TOM complex, translocase of the outer membrane, mitochondrial cristae, mitochondrial dysfunction, Alzheimer's disease, normal pressure hydrocephalus, neuroblastoma cells, mitochondrial membrane potential, valinomycin
- MeSH terms
- Animals, Endocytosis, Extracellular Space, Flow Cytometry, Fluorescent Antibody Technique, Humans, Male, Mitochondria, Mitochondria, Liver, Neuroblastoma, Peptides, Amyloid beta-Peptides, Microscopy, Immunoelectron, Rats, Sprague-Dawley, Endopeptidase K, Protein Transport, Mitochondrial Proteins, Cell Line, Tumor, Rats
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