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Ultrastructure of perivascular amyloid fibrils in Alzheimer's disease
T Miyakawa1, S Katsuragi, R Kuramoto
1Department of Neuropsychiatry, Kumamoto University Medical School, Japan.
Virchows Archiv. B, Cell Pathology Including Molecular Pathology
|January 1, 1988
Abstract:
Perivascular amyloid fibrils in the brains of patients with Alzheimer's disease have been examined by electron microscopy. The amyloid fibrils showed a hollow rod structure and consisted of globular substances. Each turn appeared to be composed of five globular subunits. These findings coincide with the ultrastructure of amyloid fibrils obtained from replicas made by a rapid freezing method.
Insights
Alzheimer
Area of Science:
- Neuroscience
- Biochemistry
- Pathology
Background:
- Alzheimer's disease is characterized by amyloid plaques.
- Perivascular amyloid deposition is a feature of Alzheimer's disease.
- The ultrastructure of these fibrils is not fully understood.
Purpose of the Study:
- To examine the ultrastructure of perivascular amyloid fibrils in Alzheimer's disease brains.
- To compare findings with amyloid fibrils prepared by rapid freezing.
Main Methods:
- Electron microscopy was used to examine perivascular amyloid fibrils.
- Replicas of amyloid fibrils were made using a rapid freezing method.
Main Results:
- Perivascular amyloid fibrils exhibit a hollow rod structure.
- Fibrils are composed of globular substances.
- Each turn of the fibril appears to consist of five globular subunits.
Conclusions:
- The observed ultrastructure of perivascular amyloid fibrils is consistent with findings from rapid-freezing methods.
- This provides insights into the molecular assembly of amyloid in Alzheimer's disease.