학술논문
Interaction between Oligomers of Stefin B and Amyloid-β in Vitro and in Cells.
Document Type
Article
Author
Source
Subject
*ALZHEIMER'S disease
*OLIGOMERS
*CYSTATINS
*BIOCHEMICAL research
*AMYLOID
*SURFACE plasmon resonance
*MASS spectrometry
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Language
ISSN
0021-9258
Abstract
To contribute to the question of the putative role of cystatins in Alzheimer disease and in neuroprotection in general, we studied the interaction between human stefin B (cystatin B) and amyloid-β-(1-40) peptide (Aβ). Using surface plasmon resonance and electrospray mass spectrometry we were able to show a direct interaction between the two proteins. As an interesting new fact, we show that stefin B binding to Aβ is oligomer specific. The dimers and tetramers of stefin B, which bind Aβ, are domain-swapped as judged from structural studies. Consistent with the binding results, the same oligomers of stefin B inhibit Aβ fibril formation. When expressed in cultured cells, stefin B co-localizes with Aβ intracellular inclusions. It also co-immunoprecipitates with the APP fragment containing the Aβ epitope. Thus, stefin B is another APP/AR-binding protein in vitro and likely in cells. [ABSTRACT FROM AUTHOR]