-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).

Funding

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).

Funders	Funder number
National Institutes of Health (NIH)
National Institute on Aging	P01AG010836

Keywords

Amyloid
Fibril formation
Neurotoxicity
α-1-Antichymotrypsin

ASJC Scopus subject areas

General Neuroscience

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10.1016/0304-3940(96)12717-8

Cite this

@article{0d41ac7940464816bb3ed685346f6c81,

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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T1 - -1-Antichymotrypsin interaction with Aβ (1-40) inhibits fibril formation but does not affect the peptide toxicity

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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AN - SCOPUS:0029661902

SN - 0304-3940

VL - 211

SP - 45

EP - 48

JO - Neuroscience Letters

JF - Neuroscience Letters

IS - 1

ER -

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

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

Access to Document

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