CaltechAUTHORS
Published October 2018 | Version public
Journal Article Metadata-only

Specific Glycosaminoglycan Chain Length and Sulfation Patterns Are Required for Cell Uptake of Tau vs. α-Synuclein and β-Amyloid Aggregates

Creators

Abstract

Transcellular propagation of protein aggregate "seeds" has been proposed to mediate the progression of neurodegeneraive diseases in tauopathies and α-synucleinopathies. We previously reported that tau and α-synuclein aggregates bind heparan sulfate proteoglycans (HSPGs) on the cell surface, promoting cellular uptake and intracellular seeding. However, the specificity and binding mode of these protein aggregates to HSPGs remain unknown. Here, we measured direct binding to modified heparins to determine the size and sulfation requirements for tau, α-synuclein, and β-amyloid (Aβ) aggregate binding to glycosaminoglycans (GAGs).

Additional Information

© 2018 American Neurological Association. Issue Online: 05 October 2018; Version of Record online: 05 October 2018. Manuscript accepted: 01 January 2018.

Additional details

Identifiers

Eprint ID
90430
DOI
10.1002/ana.25331
Resolver ID
CaltechAUTHORS:20181026-104635688

Related works

Describes
10.1002/ana.25331 (DOI)

Dates

Created
2018-10-26
Created from EPrint's datestamp field
Updated
2021-11-16
Created from EPrint's last_modified field