Abstract
Recent studies have shown that senile plaque-associated or glial-derived proteins can prevent fibril formation of β-amyloid peptide (Aβ), while increasing the neurotoxicity of the latter (in the case of glutamine synthetase, apolipoprotein J or thrombin). α-1-Antichymotrypsin (ACT) is a glial-derived protein associated with senile plaques in the Alzheimer's brain. In this report we show that ACT, a miner protein component of β-amyloid deposits, is able to inhibit AB (1-40) aggregation into fibrils, but unable to modulate the toxicity of Aβ (1-40) ) in primary rat hippocampal cell cultures. These results are discussed in terms of the potential role of glial-derived proteins (in Aβ aggregation and neurotoxicity.
Original language | English |
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Pages (from-to) | 45-48 |
Number of pages | 4 |
Journal | Neuroscience Letters |
Volume | 211 |
Issue number | 1 |
DOIs | |
State | Published - Jun 14 1996 |
Bibliographical note
Funding Information:We thank Mary G. Engle of the Anatomy and Neurobiology Department, University of Kentucky for consultation and assistance with electron microscopy. This work was supported in part by a grant from NIH (AG-10836).
Keywords
- Amyloid
- Fibril formation
- Neurotoxicity
- α-1-Antichymotrypsin
ASJC Scopus subject areas
- Neuroscience (all)