Source:http://linkedlifedata.com/resource/pubmed/id/17964692
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4-5
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pubmed:dateCreated |
2008-2-1
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pubmed:abstractText |
One of the major pathological features of Alzheimer's disease (AD) is the appearance of senile plaques characterized by extracellular aggregation of amyloid beta-peptide (Abeta) fibrils. Inhibition of Abeta fibril aggregation is therefore viewed as one possible method to halt the progression of AD. Salvianolic acid B (Sal B) is an active ingredient isolated from Salvia miltiorrhiza, a Chinese herbal medicine commonly used for the treatment of cardiovascular and cerebrovascular disorders. Recent findings show that Sal B prevents Abeta-induced cytotoxicity in a rat neural cell line. To understand the mechanism of Sal B-mediated neuroprotection, its effects on the inhibition of Abeta1-40 fibril formation and destabilization of the preformed Abeta1-40 fibrils were studied. The results were obtained using Thioflavin T fluorescence assay and Abeta aggregating immunoassay. We found that Sal B can inhibit fibril aggregation (IC(50): 1.54-5.37 microM) as well as destabilize preformed Abeta fibril (IC(50): 5.00-5.19 microM) in a dose- and time-dependent manner. Sal B is a better aggregation inhibitor than ferulic acid but less active than curcumin in the inhibition of Abeta1-40 aggregation. In electron microscope study, Sal B-treated Abeta1-40 fibrils are seen in various stages of shortening or wrinkling with numerous deformed aggregates of amorphous structure. Circular dichroism data indicate that Sal B dose dependently prevents the formation of beta-structured aggregates of Abeta1-40. Addition of preincubated Sal B with Abeta1-42 significantly reduces its cytotoxic effects on human neuroblastoma SH-SY5Y cells. These results suggest that Sal B has therapeutic potential in the treatment of AD, and warrant its study in animal models.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Antioxidants,
http://linkedlifedata.com/resource/pubmed/chemical/Benzofurans,
http://linkedlifedata.com/resource/pubmed/chemical/Tetrazolium Salts,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazoles,
http://linkedlifedata.com/resource/pubmed/chemical/salvianolic acid B,
http://linkedlifedata.com/resource/pubmed/chemical/thiazolyl blue,
http://linkedlifedata.com/resource/pubmed/chemical/thioflavin T
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pubmed:status |
MEDLINE
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pubmed:issn |
0197-0186
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pubmed:author |
pubmed-author:ChanWing-SaiWS,
pubmed-author:DurairajanSiva Sundara KumarSS,
pubmed-author:HuangJian-DongJD,
pubmed-author:KleinWilliam LWL,
pubmed-author:KoçLL,
pubmed-author:KooIreneI,
pubmed-author:KumWan-FungWF,
pubmed-author:LiuChenliC,
pubmed-author:SongYouqiangY,
pubmed-author:XieLixiaL,
pubmed-author:YuanQiujuQ
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pubmed:issnType |
Print
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pubmed:volume |
52
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
741-50
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:17964692-Amyloid beta-Peptides,
pubmed-meshheading:17964692-Antioxidants,
pubmed-meshheading:17964692-Benzofurans,
pubmed-meshheading:17964692-Cell Aggregation,
pubmed-meshheading:17964692-Cell Line, Tumor,
pubmed-meshheading:17964692-Circular Dichroism,
pubmed-meshheading:17964692-Data Interpretation, Statistical,
pubmed-meshheading:17964692-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:17964692-Humans,
pubmed-meshheading:17964692-Microfibrils,
pubmed-meshheading:17964692-Microscopy, Electron,
pubmed-meshheading:17964692-Tetrazolium Salts,
pubmed-meshheading:17964692-Thiazoles
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pubmed:articleTitle |
Salvianolic acid B inhibits Abeta fibril formation and disaggregates preformed fibrils and protects against Abeta-induced cytotoxicty.
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pubmed:affiliation |
School of Chinese Medicine, Hong Kong Baptist University, Kowloon Tong, Hong Kong, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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