Current studentsExisting staffContact us
 

The p75NTR extracellular domain: a potential molecule regulating the solubility and removal of amyloid-β

Simple item page
dc.contributor.authorZhou, X.F.
dc.contributor.authorWang, Y.J.
dc.date.issued2011
dc.description.abstractSenile plaques composed of amyloid-beta (Aβ) in the brain are one of the hallmarks of Alzheimer disease (AD). Removal of Aβ from the brain is the most important therapeutic strategy for AD. The solubility of Aβ is critical for its endocytosis, transcytosis and removal from the brain. Our recent study has found that the extracellular domain of p75NTR, the neurotrophin receptor, plays an important role in the solubility of Aβ and might be one of the endogenous mechanisms in the regulation of Aβ plaque formation. The physiologically shedded extracellular domain of p75NTR is able to inhibit Aβ aggregation and diasggregate preformed Aβ fibrils, while the full p75NTR expressed on neurites, endothelial cells and smooth muscle cells in blood-brain barrier (BBB) might initiate Aβ endocytosis and degradation, and/or remove Aβ from the brain via BBB. Understanding the roles of p75NTR in the solubility and clearance of Aβ may allow targetting p75NTR as a unique opportunity to develop therapeutic drugs for the prevention and treatment of AD.
dc.identifier.citationPrion, 2011; 5(3):161-163
dc.identifier.doi10.4161/pri.5.3.16896
dc.identifier.issn1933-690X
dc.identifier.issn1933-690X
dc.identifier.orcidZhou, X.F. [0000-0002-8687-0175]
dc.identifier.urihttps://hdl.handle.net/11541.2/128889
dc.language.isoen
dc.publisherLandes Bioscience
dc.relation.fundingNHMRC 480422
dc.relation.fundingFMC
dc.relation.fundingNSFC 30973144
dc.relation.fundingNatural Science Foundation Project of CQCSTC CSTC2010BA5004
dc.rightsCopyright 2011 Landes Bioscience (https://creativecommons.org/licenses/by-nc/3.0/au/) Access Condition Notes: This is an open access article under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
dc.source.urihttps://doi.org/10.4161/pri.5.3.16896
dc.subjectAlzheimer disease
dc.subjectamyloid-β
dc.subjectp75NTR
dc.subjectextracellular domain
dc.subjectblood-brain barrier
dc.subjectclearance
dc.subjectHumans
dc.subjectReceptor, Nerve Growth Factor
dc.subjectSolubility
dc.subjectAmyloid beta-Peptides
dc.subjectPlaque, Amyloid
dc.titleThe p75NTR extracellular domain: a potential molecule regulating the solubility and removal of amyloid-β
dc.typeJournal article
pubs.publication-statusPublished
ror.fileinfo12149383920001831 13149373980001831 The p75NTR extracellular domain.pdf
ror.mmsid9916027093101831

Files

Original bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
9916027093101831_12149383920001831_The p75NTR extracellular domain.pdf
Size:
1006.26 KB
Format:
Adobe Portable Document Format
Description:
Published version
Download

Collections