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Unwinding fibril formation of medin, the peptide of the most common form of human amyloid.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Genetics and Pathology.
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2007 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 361, no 4, 822-828 p.Article in journal (Refereed) Published
Abstract [en]

Medin amyloid affects the medial layer of the thoracic aorta of most people above 50 years of age. The consequences of this amyloid are not completely known but the deposits may contribute to diseases such as thoracic aortic aneurysm and dissection or to the general diminished elasticity of blood vessels seen in elderly people. We show that the 50-amino acid residue peptide medin forms amyloid-like fibrils in vitro. With the use of Congo red staining, Thioflavin T fluorescence, electron microscopy, and a solid-phase binding assay on different synthetic peptides, we identified the last 18-19 amino acid residues to constitute the amyloid-promoting region of medin. We also demonstrate that the two C-terminal phenylalanines, previously suggested to be of importance for amyloid formation, are not required for medin amyloid formation.

Place, publisher, year, edition, pages
2007. Vol. 361, no 4, 822-828 p.
Keyword [en]
Amyloid, Fibril formation, Lactadherin, Medin
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-11727DOI: 10.1016/j.bbrc.2007.06.187ISI: 000249181500002PubMedID: 17679143OAI: oai:DiVA.org:uu-11727DiVA: diva2:39496
Available from: 2007-10-15 Created: 2007-10-15 Last updated: 2011-01-26Bibliographically approved

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Larsson, AnnikaEngström, UllaWestermark, Per
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Department of Genetics and PathologyLudwig Institute for Cancer Research
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