-1-Antichymotrypsin interaction with Aβ (1-40) inhibits fibril formation but does not affect the peptide toxicity

Marina V. Aksenova, Michael Y. Aksenov, D. Allan Butterfield, John M. Carney

Research output: Contribution to journalArticlepeer-review

41 Scopus citations

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 languageEnglish
Pages (from-to)45-48
Number of pages4
JournalNeuroscience Letters
Volume211
Issue number1
DOIs
StatePublished - 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)

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