Published in

Elsevier, Journal of Biological Chemistry, 5(285), p. 3201-3210, 2010

DOI: 10.1074/jbc.m109.024620

Links

Tools

Export citation

Search in Google Scholar

Interaction between Oligomers of Stefin B and Amyloid-β in Vitro and in Cells

Journal article published in 2010 by Katja Škerget, Ajda Taler-Verčič, Andrej Bavdek, Vesna Hodnik, Slavko Čeru, Magda Tušek-Žnidarič, Tiina Kumm, Didier Pitsi, Maruša Pompe-Novak ORCID, Peep Palumaa, Salvador Soriano, Nataša Kopitar-Jerala ORCID, Vito Turk, Gregor Anderluh, Eva Žerovnik
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Green circle
Preprint: archiving allowed
Upload
Green circle
Postprint: archiving allowed
Upload
Green circle
Published version: archiving allowed
Upload
Policy details
Data provided by SHERPA/RoMEO

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-beta-(1-40) peptide (Abeta). 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 Abeta is oligomer specific. The dimers and tetramers of stefin B, which bind Abeta, are domain-swapped as judged from structural studies. Consistent with the binding results, the same oligomers of stefin B inhibit Abeta fibril formation. When expressed in cultured cells, stefin B co-localizes with Abeta intracellular inclusions. It also co-immunoprecipitates with the APP fragment containing the Abeta epitope. Thus, stefin B is another APP/Abeta-binding protein in vitro and likely in cells.