Abstract
The cerebral cortex of Alzheimer's and Down syndrome patients is characterized by the presence of protein deposits in neurofibrillary tangles, neuritic plaques, and neuropil threads. These structures were shown to contain forms of beta amyloid precursor protein and ubiquitin-B that are aberrant (+1 proteins) in the carboxyl terminus. The +1 proteins were not found in young control patients, whereas the presence of ubiquitin-B+1 in elderly control patients may indicate early stages of neurodegeneration. The two species of +1 proteins displayed cellular colocalization, suggesting a common origin, operating at the transcriptional level or by posttranscriptional editing of RNA. This type of transcript mutation is likely an important factor in the widely occurring nonfamilial early- and late-onset forms of Alzheimer's disease.
Original language | English |
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Pages (from-to) | 242-247 |
Number of pages | 6 |
Journal | Science |
Volume | 279 |
Issue number | 5348 |
Publication status | Published - 9 Jan 1998 |
Keywords
- Aged
- Aging
- Alzheimer Disease
- Amino Acid Sequence
- Amyloid beta-Protein Precursor
- Base Sequence
- Brain Chemistry
- Cerebral Cortex
- Cloning, Molecular
- Down Syndrome
- Female
- Frameshift Mutation
- Hippocampus
- Humans
- Male
- Molecular Sequence Data
- Neurites
- Neurofibrillary Tangles
- Neuropil
- Polymerase Chain Reaction
- RNA Editing
- Repetitive Sequences, Nucleic Acid
- Sequence Deletion
- Transcription, Genetic
- Ubiquitins
- Journal Article
- Research Support, Non-U.S. Gov't