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rdf:type |
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|
lifeskim:mentions |
|
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pubmed:issue |
13
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pubmed:dateCreated |
2001-10-5
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0959-4965
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2967-70
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11588612-Alzheimer Disease,
pubmed-meshheading:11588612-Amyloid beta-Peptides,
pubmed-meshheading:11588612-Brain,
pubmed-meshheading:11588612-Chromatography, High Pressure Liquid,
pubmed-meshheading:11588612-Drug Interactions,
pubmed-meshheading:11588612-Fibrinolysin,
pubmed-meshheading:11588612-Humans,
pubmed-meshheading:11588612-Peptide Fragments,
pubmed-meshheading:11588612-Protein Structure, Secondary,
pubmed-meshheading:11588612-Thiazoles
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pubmed:year |
2001
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|
pubmed:articleTitle |
Plasmin cleaves Abeta42 in vitro and prevents its aggregation into beta-pleated sheet structures.
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pubmed:affiliation |
Birchall Centre for Inorganic Chemistry and Materials Science, School of Chemistry and Physics, Keele University, Staffordshire, ST5 5BG, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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