-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

doi:10.1016/0304-3940(96)12717-8

-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 journal › Article › peer-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 language	English
Pages (from-to)	45-48
Number of pages	4
Journal	Neuroscience Letters
Volume	211
Issue number	1
DOIs	https://doi.org/10.1016/0304-3940(96)12717-8
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)

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10.1016/0304-3940(96)12717-8

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

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.",

keywords = "Amyloid, Fibril formation, Neurotoxicity, α-1-Antichymotrypsin",

author = "Aksenova, {Marina V.} and Aksenov, {Michael Y.} and Butterfield, {D. Allan} and Carney, {John M.}",

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).",

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AU - Aksenova, Marina V.

AU - Aksenov, Michael Y.

AU - Butterfield, D. Allan

AU - Carney, John M.

N1 - 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).

PY - 1996/6/14

Y1 - 1996/6/14

N2 - 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.

AB - 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.

KW - Amyloid

KW - Fibril formation

KW - Neurotoxicity

KW - α-1-Antichymotrypsin

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

Access to Document

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