Abstract:
:Beta-amyloid peptides (A beta) are deposited in an aggregated fibrillar form in both diffuse and senile plaques in the brains of patients with Alzheimer's disease. The neurotoxicity of A beta in cultured neurons is dependent on its aggregation state, but the factors contributing to aggregation and fibril formation are poorly understood. In the present study, we investigated whether alpha2-macroglobulin (alpha2M), a protein present in neuritic plaques and elevated in Alzheimer's disease brain, is a potential regulatory factor for A beta fibril formation. Previous studies in our laboratory have shown that alpha2M is an A beta binding protein. We now report that, in contrast to another plaque-associated protein, alpha1-antichymotrypsin, alpha2M coincubated with A beta significantly reduces aggregation and fibril formation in vitro. Additionally, cultured fetal rat cortical neurons are less vulnerable to the toxic actions of aged A beta following pretreatment with alpha2M. We postulate that alpha2M is able to maintain A beta in a soluble state, preventing fibril formation and associated neurotoxicity.
journal_name
J Neurochemjournal_title
Journal of neurochemistryauthors
Du Y,Bales KR,Dodel RC,Liu X,Glinn MA,Horn JW,Little SP,Paul SMdoi
10.1046/j.1471-4159.1998.70031182.xsubject
Has Abstractpub_date
1998-03-01 00:00:00pages
1182-8issue
3eissn
0022-3042issn
1471-4159journal_volume
70pub_type
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更新日期:2010-01-01 00:00:00
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