Show simple item record

dc.rights.licenseCC BY — Creative Commons Attribution
dc.contributor.authorMah, Dylan
dc.contributor.authorZhao, Jing
dc.contributor.authorLiu, Xinyue
dc.contributor.authorZhang, Fuming
dc.contributor.authorLiu, Jian
dc.contributor.authorWang, Lianchun
dc.contributor.authorLinhardt, Robert
dc.contributor.authorWang, Chunyu
dc.date2021
dc.date.accessioned2022-06-21T13:52:20Z
dc.date.available2022-06-21T13:52:20Z
dc.date.issued2021-05-20
dc.identifier.citationThe sulfation code of tauopathies: heparan sulfate proteoglycans in the prion like spread of tau pathology, D. J. Mah, J. Zhao, X. Liu, F. Zhang, J. Liu, L. Wang, R. J. Linhardt, C. Wang, Frontiers in Molecular Biosciences, Molecular Recognition, 7, 594497, 2021.
dc.identifier.issn2296889X
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5038
dc.identifier.urihttps://doi.org/10.3389/fmolb.2021.671458
dc.descriptionFrontiers in Molecular Biosciences, Molecular Recognition, 7, 594497
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractTauopathies are a heterogenous family of progressive neurodegenerative diseases defined by the appearance of proteinaceous lesions within the brain composed of abnormally folded species of Microtubule Associated Protein Tau (tau). Alzheimer's Disease (AD), the most common tauopathy, is the leading cause of cognitive decline among the elderly and is responsible for more than half of all cases of senile dementia worldwide. The characteristic pathology of many tauopathies-AD included-presents as Neurofibrillary Tangles (NFTs), insoluble inclusions found within the neurons of the central nervous system composed primarily of tau protein arranged into Paired Helical Fibrils (PHFs). The spatial extent of this pathology evolves in a remarkably consistent pattern over the course of disease progression. Among the leading hypotheses which seek to explain the stereotypical progression of tauopathies is the prion model, which proposes that the spread of tau pathology is mediated by the transmission of self-propagating tau conformers between cells in a fashion analogous to the mechanism of communicable prion diseases. Protein-glycan interactions between tau and Heparan Sulfate Proteoglycans (HSPGs) have been implicated as a key facilitator in each stage of the prion-like propagation of tau pathology, from the initial secretion of intracellular tau protein into the extracellular matrix, to the uptake of pathogenic tau seeds by cells, and the self-assembly of tau into higher order aggregates. In this review we outline the biochemical basis of the tau-HS interaction and discuss our current understanding of the mechanisms by which these interactions contribute to the propagation of tau pathology in tauopathies, with a particular focus on AD.
dc.description.sponsorshipNational Institutes of Health
dc.languageen_US
dc.language.isoENG
dc.publisherFrontiers Media SA
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofFrontiers in Molecular Biosciences
dc.relation.urihttps://harc.rpi.edu/
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleThe sulfation code of tauopathies: heparan sulfate proteoglycans in the prion like spread of tau pathologyen_US
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.accessRightsOpen Access
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.3389/fmolb.2021.671458
dc.rights.holderCC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.volume8


Files in this item

Thumbnail
Thumbnail

This item appears in the following Collection(s)

Show simple item record

CC BY — Creative Commons Attribution
Except where otherwise noted, this item's license is described as CC BY — Creative Commons Attribution