Abstract：
:Deposition of amyloid beta-peptide (Abeta) into amyloid plaques is one of the invariant neuropathological features of Alzheimer's disease. Proteins that codeposit with Abeta are potentially important for the pathogenesis, and a recently discovered plaque-associated protein is the collagenous Alzheimer amyloid plaque component (CLAC). In this study, we investigated the molecular interactions between Abeta aggregates and CLAC using surface plasmon resonance spectroscopy and a solid-phase binding immunoassay. We found that CLAC binds to Abeta with high affinity, that the central region of Abeta is necessary and sufficient for CLAC interaction, and that the aggregation state of Abeta as well as the presence of negatively charged residues is important. We also show that this binding results in a reduced rate of fibril elongation. Taken together, we suggest that CLAC becomes involved at an intermediate stage in the pathogenesis by binding to Abeta fibrils, including fibrils formed from peptides with truncated N- or C-termini, and thereby slows their growth.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Kakuyama H,Söderberg L,Horigome K,Winblad B,Dahlqvist C,Näslund J,Tjernberg LOdoi
10.1021/bi051263esubject
Has Abstractpub_date
2005-11-29 00:00:00pages
15602-9issue
47eissn
0006-2960issn
1520-4995journal_volume
44pub_type
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