Abstract:
:Immunocytochemical, biochemical, and molecular genetic studies indicate that apolipoprotein E (apoE) plays an important role in the process of amyloidogenesis-beta. However, there is still no clear translation of these data into the pathogenesis of amyloidosis-beta. Previous studies demonstrated sodium dodecyl sulfate (SDS)-resistant binding of apoE to the main component of Alzheimer's amyloid-A beta and modulation of A beta aggregation by apoE in vitro. To more closely characterize apoE-A beta interactions, we have studied the binding of thrombolytic fragments of apoE3 to A beta in vitro by using SDS-polyacrylamide gel electrophoresis and intrinsic fluorescence quenching. Here we demonstrate that SDS-resistant binding of A beta is mediated by the receptor-binding, N-terminal domain of apoE3. Under native conditions, both the N- and C-terminal domains of apoE3 bind A beta; however, the former does so with higher affinity. We propose that the modulation of A beta binding to the N-terminal domain of apoE is a potential therapeutic target for the treatment of amyloidosis-beta.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Golabek AA,Kida E,Walus M,Perez C,Wisniewski T,Soto Cdoi
10.1016/S0006-3495(00)76354-5subject
Has Abstractpub_date
2000-08-01 00:00:00pages
1008-15issue
2eissn
0006-3495issn
1542-0086pii
S0006-3495(00)76354-5journal_volume
79pub_type
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