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.
|Number of pages||4|
|State||Published - Jun 14 1996|
Bibliographical noteFunding 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).
- Fibril formation
ASJC Scopus subject areas
- Neuroscience (all)