Linked Life Data

11376898

Source:http://linkedlifedata.com/resource/pubmed/id/11376898

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-5-29
pubmed:abstractText
Amyloid beta-protein (Abeta) fibril in senile plaques may possibly be related to the pathogenesis of Alzheimer's disease (AD). Basement membrane (BM) components are localized to the plaques. Entactin binds the plaque associated BM components. We investigated the potential of entactin to prevent Abeta fibril formation. Thioflavin T fluorometric assay and electron microscopy revealed that entactin significantly inhibited Abeta1-40 (Abeta40) fibril formation at an Abeta40:entactin molar ratio of 50:1. The inhibitory effect of entactin was displayed in a dose-dependent manner. Circular dichroism spectroscopy data indicated that entactin induced a random coil structure in Abeta40. We propose that the ability of entactin to induce random structure is linked to the inhibition of Abeta fibril formation. Entactin may be related to the pathogenesis of AD by regulating Abeta40 fibril formation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0304-3940
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
305
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
119-22
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Entactin-induced inhibition of human amyloid beta-protein fibril formation in vitro.
pubmed:affiliation
Pharmacology Laboratory, Pharmaceutical Research Laboratories, Taisho Pharmaceutical Company, Limited, 403, Yoshino-cho 1-chome, Omiya, 330-8530, Saitama, Japan. s14806@taisho.co.jp
pubmed:publicationType
Journal Article, In Vitro