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The amyloid beta-pe...
The amyloid beta-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae
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Hansson Petersen, Camilla A. (author)
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- Alikhani, Nyosha (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Behbahani, Homira (author)
- Karolinska Institutet
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- Wiehager, Birgitta (author)
- Karolinska Institutet
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- Pavlov, Pavel F (author)
- Karolinska Institutet
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- Alafuzoff, Irina (author)
- Department of Neuroscience and Neurology, University of Kuopio Finland
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Leinonen, Ville (author)
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Ito, Akira (author)
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- Winblad, Bengt (author)
- Karolinska Institutet
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- Glaser, Elzbieta (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Ankarcrona, Maria (author)
- Karolinska Institutet
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(creator_code:org_t)
- 2008-09-02
- 2008
- English.
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In: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 105:35, s. 13145-13150
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http://www.pnas.org/...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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https://urn.kb.se/re...
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http://kipublication...
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Abstract
Subject headings
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- 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.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi -- Medicinsk bioteknologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology -- Medical Biotechnology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Cellbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Cell Biology (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Klinisk medicin -- Klinisk laboratoriemedicin (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Clinical Medicine -- Clinical Laboratory Medicine (hsv//eng)
Keyword
- Alzheimer disease
- protein import
- human brain biopsies
- Biochemistry
- Biokemi
- Cell biology
- Cellbiologi
- Pathology
Publication and Content Type
- ref (subject category)
- art (subject category)
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Hansson Petersen ...
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Alikhani, Nyosha
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Behbahani, Homir ...
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Wiehager, Birgit ...
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Pavlov, Pavel F
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Alafuzoff, Irina
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show more...
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Leinonen, Ville
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Ito, Akira
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Winblad, Bengt
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Glaser, Elzbieta
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Ankarcrona, Mari ...
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- About the subject
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- MEDICAL AND HEALTH SCIENCES
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MEDICAL AND HEAL ...
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and Medical Biotechn ...
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and Medical Biotechn ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Cell Biology
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MEDICAL AND HEAL ...
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and Clinical Medicin ...
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and Clinical Laborat ...
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Proceedings of t ...
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Stockholm University
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Uppsala University
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Karolinska Institutet