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Article: Salvianolic acid B inhibits Aβ fibril formation and disaggregates preformed fibrils and protects against Aβ-induced cytotoxicty
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TitleSalvianolic acid B inhibits Aβ fibril formation and disaggregates preformed fibrils and protects against Aβ-induced cytotoxicty
 
AuthorsDurairajan, SSK2
Yuan, Q1
Xie, L2
Chan, WS2
Kum, WF2
Koo, I2
Liu, C1
Song, Y1
Huang, JD1
Klein, WL3
Li, M2
 
Issue Date2008
 
PublisherElsevier Ltd. The Journal's web site is located at http://www.elsevier.com/locate/neuint
 
CitationNeurochemistry International, 2008, v. 52 n. 4-5, p. 741-750 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.neuint.2007.09.006
 
AbstractOne of the major pathological features of Alzheimer's disease (AD) is the appearance of senile plaques characterized by extracellular aggregation of amyloid β-peptide (Aβ) fibrils. Inhibition of Aβ 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 Aβ-induced cytotoxicity in a rat neural cell line. To understand the mechanism of Sal B-mediated neuroprotection, its effects on the inhibition of Aβ1-40 fibril formation and destabilization of the preformed Aβ1-40 fibrils were studied. The results were obtained using Thioflavin T fluorescence assay and Aβ aggregating immunoassay. We found that Sal B can inhibit fibril aggregation (IC50: 1.54-5.37 μM) as well as destabilize preformed Aβ fibril (IC50: 5.00-5.19 μM) 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 Aβ1-40 aggregation. In electron microscope study, Sal B-treated Aβ1-40 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 β-structured aggregates of Aβ1-40. Addition of preincubated Sal B with Aβ1-42 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. © 2007 Elsevier Ltd. All rights reserved.
 
ISSN0197-0186
2012 Impact Factor: 2.659
2012 SCImago Journal Rankings: 0.980
 
DOIhttp://dx.doi.org/10.1016/j.neuint.2007.09.006
 
ISI Accession Number IDWOS:000254968300026
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorDurairajan, SSK
 
dc.contributor.authorYuan, Q
 
dc.contributor.authorXie, L
 
dc.contributor.authorChan, WS
 
dc.contributor.authorKum, WF
 
dc.contributor.authorKoo, I
 
dc.contributor.authorLiu, C
 
dc.contributor.authorSong, Y
 
dc.contributor.authorHuang, JD
 
dc.contributor.authorKlein, WL
 
dc.contributor.authorLi, M
 
dc.date.accessioned2010-09-06T06:00:31Z
 
dc.date.available2010-09-06T06:00:31Z
 
dc.date.issued2008
 
dc.description.abstractOne of the major pathological features of Alzheimer's disease (AD) is the appearance of senile plaques characterized by extracellular aggregation of amyloid β-peptide (Aβ) fibrils. Inhibition of Aβ 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 Aβ-induced cytotoxicity in a rat neural cell line. To understand the mechanism of Sal B-mediated neuroprotection, its effects on the inhibition of Aβ1-40 fibril formation and destabilization of the preformed Aβ1-40 fibrils were studied. The results were obtained using Thioflavin T fluorescence assay and Aβ aggregating immunoassay. We found that Sal B can inhibit fibril aggregation (IC50: 1.54-5.37 μM) as well as destabilize preformed Aβ fibril (IC50: 5.00-5.19 μM) 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 Aβ1-40 aggregation. In electron microscope study, Sal B-treated Aβ1-40 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 β-structured aggregates of Aβ1-40. Addition of preincubated Sal B with Aβ1-42 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. © 2007 Elsevier Ltd. All rights reserved.
 
dc.description.natureLink_to_subscribed_fulltext
 
dc.identifier.citationNeurochemistry International, 2008, v. 52 n. 4-5, p. 741-750 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.neuint.2007.09.006
 
dc.identifier.doihttp://dx.doi.org/10.1016/j.neuint.2007.09.006
 
dc.identifier.epage750
 
dc.identifier.hkuros145499
 
dc.identifier.isiWOS:000254968300026
 
dc.identifier.issn0197-0186
2012 Impact Factor: 2.659
2012 SCImago Journal Rankings: 0.980
 
dc.identifier.issue4-5
 
dc.identifier.openurl
 
dc.identifier.pmid17964692
 
dc.identifier.scopuseid_2-s2.0-38349160407
 
dc.identifier.spage741
 
dc.identifier.urihttp://hdl.handle.net/10722/68014
 
dc.identifier.volume52
 
dc.languageeng
 
dc.publisherElsevier Ltd. The Journal's web site is located at http://www.elsevier.com/locate/neuint
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofNeurochemistry International
 
dc.relation.referencesReferences in Scopus
 
dc.rightsNeurochemistry International. Copyright © Elsevier Ltd.
 
dc.subject.meshAmyloid beta-Peptides - antagonists & inhibitors - biosynthesis - toxicity
 
dc.subject.meshAntioxidants - pharmacology
 
dc.subject.meshBenzofurans - pharmacology
 
dc.subject.meshCell Aggregation - drug effects
 
dc.subject.meshCell Line, Tumor
 
dc.subject.meshCircular Dichroism
 
dc.subject.meshData Interpretation, Statistical
 
dc.subject.meshEnzyme-Linked Immunosorbent Assay
 
dc.subject.meshHumans
 
dc.subject.meshMicrofibrils - drug effects - ultrastructure
 
dc.subject.meshMicroscopy, Electron
 
dc.subject.meshTetrazolium Salts
 
dc.subject.meshThiazoles - pharmacology
 
dc.titleSalvianolic acid B inhibits Aβ fibril formation and disaggregates preformed fibrils and protects against Aβ-induced cytotoxicty
 
dc.typeArticle
 
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<description.abstract>One of the major pathological features of Alzheimer&apos;s disease (AD) is the appearance of senile plaques characterized by extracellular aggregation of amyloid &#946;-peptide (A&#946;) fibrils. Inhibition of A&#946; 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 A&#946;-induced cytotoxicity in a rat neural cell line. To understand the mechanism of Sal B-mediated neuroprotection, its effects on the inhibition of A&#946;1-40 fibril formation and destabilization of the preformed A&#946;1-40 fibrils were studied. The results were obtained using Thioflavin T fluorescence assay and A&#946; aggregating immunoassay. We found that Sal B can inhibit fibril aggregation (IC50: 1.54-5.37 &#956;M) as well as destabilize preformed A&#946; fibril (IC50: 5.00-5.19 &#956;M) 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 A&#946;1-40 aggregation. In electron microscope study, Sal B-treated A&#946;1-40 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 &#946;-structured aggregates of A&#946;1-40. Addition of preincubated Sal B with A&#946;1-42 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. &#169; 2007 Elsevier Ltd. All rights reserved.</description.abstract>
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Author Affiliations
  1. The University of Hong Kong Li Ka Shing Faculty of Medicine
  2. Hong Kong Baptist University
  3. Northwestern University