Document Detail

Cell surface binding and internalization of aβ modulated by degree of aggregation.
MedLine Citation:
PMID:  21331340     Owner:  NLM     Status:  PubMed-not-MEDLINE    
The amyloid peptides, Aβ40 and Aβ42, are generated through endoproteolytic cleavage of the amyloid precursor protein. Here we have developed a model to investigate the interaction of living cells with various forms of aggregated Aβ40/42. After incubation at endosomal pH 6, we observed a variety of Aβ conformations after 3 (Aβ(3)), 24 (Aβ(24)), and 90 hours (Aβ(90)). Both Aβ42(24) and Aβ40(24) were observed to rapidly bind and internalize into differentiated PC12 cells, leading to accumulation in the lysosome. In contrast, Aβ40/42(90) were both found to only weakly associate with cells, but were observed as the most aggregated using dynamic light scattering and thioflavin-T. Internalization of Aβ40/42(24) was inhibited with treatment of monodansylcadaverine, an endocytosis inhibitor. These studies indicate that the ability of Aβ40/42 to bind and internalize into living cells increases with degree of aggregation until it reaches a maximum beyond which its ability to interact with cells diminishes drastically.
David A Bateman; Avijit Chakrabartty
Publication Detail:
Type:  Journal Article     Date:  2011-02-07
Journal Detail:
Title:  International journal of Alzheimer's disease     Volume:  2011     ISSN:  2090-0252     ISO Abbreviation:  Int J Alzheimers Dis     Publication Date:  2011  
Date Detail:
Created Date:  2011-02-18     Completed Date:  2011-07-14     Revised Date:  2011-07-25    
Medline Journal Info:
Nlm Unique ID:  101525141     Medline TA:  Int J Alzheimers Dis     Country:  England    
Other Details:
Languages:  eng     Pagination:  962352     Citation Subset:  -    
Laboratory of Biochemistry and Genetics, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA.
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