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Neuroreport. 2001 Sep 17;12(13):2967-70.

Plasmin cleaves Abeta42 in vitro and prevents its aggregation into beta-pleated sheet structures.

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1
Birchall Centre for Inorganic Chemistry and Materials Science, School of Chemistry and Physics, Keele University, Staffordshire, ST5 5BG, UK.

Abstract

The formation, aggregation and deposition of amyloid beta peptide (Abeta) is implicated in the aetiology of Alzheimer's disease. Impairment of proteolytic degradation of Abeta may be a key factor in the progression of the disease. We have used RP-HPLC and thioflavin T fluorescence to demonstrate that Abeta42 is rapidly cleaved by the protease plasmin and that cleavage prevented the aggregation of Abeta42, and its cleavage products, into beta-pleated sheet structures. Plasmin may fulfil a similar role in vivo.

PMID:
11588612
[Indexed for MEDLINE]
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