Asset Details
Do you wish to reserve the book?
Contribution of syndecans to cellular internalization and fibrillation of amyloid-β(1–42)
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Contribution of syndecans to cellular internalization and fibrillation of amyloid-β(1–42)
Do you wish to request the book?
Contribution of syndecans to cellular internalization and fibrillation of amyloid-β(1–42)
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Contribution of syndecans to cellular internalization and fibrillation of amyloid-β(1–42)
2019
Overview
Intraneuronal accumulation of amyloid-β(1–42) (Aβ1–42) is one of the earliest signs of Alzheimer’s disease (AD). Cell surface heparan sulfate proteoglycans (HSPGs) have profound influence on the cellular uptake of Aβ1–42 by mediating its attachment and subsequent internalization into the cells. Colocalization of amyloid plaques with members of the syndecan family of HSPGs, along with the increased expression of syndecan-3 and -4 have already been reported in postmortem AD brains. Considering the growing evidence on the involvement of syndecans in the pathogenesis of AD, we analyzed the contribution of syndecans to cellular uptake and fibrillation of Aβ1–42. Among syndecans, the neuron specific syndecan-3 isoform increased cellular uptake of Aβ1–42 the most. Kinetics of Aβ1–42 uptake also proved to be fairly different among SDC family members: syndecan-3 increased Aβ1–42 uptake from the earliest time points, while other syndecans facilitated Aβ1–42 internalization at a slower pace. Internalized Aβ1–42 colocalized with syndecans and flotillins, highlighting the role of lipid-rafts in syndecan-mediated uptake. Syndecan-3 and 4 also triggered fibrillation of Aβ1–42, further emphasizing the pathophysiological relevance of syndecans in plaque formation. Overall our data highlight syndecans, especially the neuron-specific syndecan-3 isoform, as important players in amyloid pathology and show that syndecans, regardless of cell type, facilitate key molecular events in neurodegeneration.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 13/31
/ 14/19
/ 14/28
/ 14/34
/ 14/35
/ 42/35
/ 42/70
/ 82/80
/ Amyloid
/ Amyloid beta-Peptides - metabolism
/ Amyloid beta-Peptides - ultrastructure
/ Autopsy
/ Heparan sulfate proteoglycans
/ Humanities and Social Sciences
/ Humans
/ Kinetics
/ Membrane Microdomains - metabolism
/ Membrane Proteins - metabolism
/ Peptide Fragments - metabolism
/ Peptide Fragments - ultrastructure
/ Science
/ Syndecan
