alpha-1-antichymotrypsin interaction with A beta (1-40) inhibits fibril formation but does not affect the peptide toxicity.
Recent studies have shown that senile plaque-associated or glial-derived proteins can prevent fibril formation of beta-amyloid peptide (A beta), while increasing the neurotoxicity of the latter (in the case of glutamine synthetase, apolipoprotein J or thrombin). alpha-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 minor protein component of beta-amyloid deposits, is able to inhibit A beta (1-40) aggregation into fibrils, but unable to modulate the toxicity of A beta (1-40) in primary rat hippocampal cell cultures. These results are discussed in terms of the potential role of glial-derived proteins on A beta aggregation and neurotoxicity.
Aksenova
M V
MV
Department of Pharmacology, University of Kentucky, Lexington 40536, USA.
Aksenov
M Y
MY
Butterfield
D A
DA
Carney
J M
JM
D016229:Amyloid beta-Peptides / Q000494:pharmacology*; D000818:Animals; D002478:Cells, Cultured; D006624:Hippocampus / Q000166:cytology / Q000378:metabolism; D016874:Neurofibrillary Tangles / Q000473:pathology*; D010446:Peptide Fragments / Q000494:pharmacology*; D051381:Rats; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology*; D000514:alpha 1-Antichymotrypsin / Q000494:pharmacology*
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; D015842:Serine Proteinase Inhibitors; D000514:alpha 1-Antichymotrypsin; C078592:amyloid beta-protein (1-40)