Isolation and Characterization of Heparan Sulfate Containing Amyloid Precursor Protein Degradation Products
Mani, Katrin LU
(2022)
In Methods in Molecular Biology
2303.
p.279-288
- Abstract
Numerous studies indicate that heparan sulfate proteoglycans (HSPGs) participate in a network of complex molecular events involving amyloid precursor protein (APP) processing and formation, oligomerization, intracellular targeting, clearance, and propagation of amyloid β in Alzheimer’s disease (AD). A mutual functional interplay between recycling glypican-1 and APP processing has been demonstrated where the HS released from glypican-1 by a Cu/NO-ascorbate-dependent reaction forms a conjugate with APP degradation products and undergoes an endosome-nucleus-autophagosome co-trafficking. HS has been shown to display contradictory and dual effects in AD involving both prevention and promotion of amyloid β formation. It is therefore important... (More)
Numerous studies indicate that heparan sulfate proteoglycans (HSPGs) participate in a network of complex molecular events involving amyloid precursor protein (APP) processing and formation, oligomerization, intracellular targeting, clearance, and propagation of amyloid β in Alzheimer’s disease (AD). A mutual functional interplay between recycling glypican-1 and APP processing has been demonstrated where the HS released from glypican-1 by a Cu/NO-ascorbate-dependent reaction forms a conjugate with APP degradation products and undergoes an endosome-nucleus-autophagosome co-trafficking. HS has been shown to display contradictory and dual effects in AD involving both prevention and promotion of amyloid β formation. It is therefore important to identify the source, detailed structural features as well as factors that favor formation of the neuroprotective forms of HS. Here, a method for isolation and identification of HS-containing APP degradation products has been described. The method is based on isolation of radiolabeled HS followed by identification of accompanying APP degradation products by SDS-PAGE and Western blotting.
(Less)
- author
- Mani, Katrin
LU
- organization
- publishing date
- 2022
- type
- Chapter in Book/Report/Conference proceeding
- publication status
- published
- subject
- keywords
- Alzheimer’s disease, Amyloid β, Glypican-1, Heparan sulfate
- host publication
- Methods in Molecular Biology
- series title
- Methods in Molecular Biology
- volume
- 2303
- pages
- 10 pages
- publisher
- Humana Press
- external identifiers
-
- pmid:34626386
- scopus:85117145188
- ISSN
- 1064-3745
- 1940-6029
- DOI
- 10.1007/978-1-0716-1398-6_22
- language
- English
- LU publication?
- yes
- additional info
- Publisher Copyright: © 2022, Springer Science+Business Media, LLC, part of Springer Nature.
- id
- 7962cb7d-3098-41d0-8218-0e0db8105ab2
- date added to LUP
- 2021-11-01 13:41:08
- date last changed
- 2024-04-06 12:18:26
@inbook{7962cb7d-3098-41d0-8218-0e0db8105ab2,
abstract = {{<p>Numerous studies indicate that heparan sulfate proteoglycans (HSPGs) participate in a network of complex molecular events involving amyloid precursor protein (APP) processing and formation, oligomerization, intracellular targeting, clearance, and propagation of amyloid β in Alzheimer’s disease (AD). A mutual functional interplay between recycling glypican-1 and APP processing has been demonstrated where the HS released from glypican-1 by a Cu/NO-ascorbate-dependent reaction forms a conjugate with APP degradation products and undergoes an endosome-nucleus-autophagosome co-trafficking. HS has been shown to display contradictory and dual effects in AD involving both prevention and promotion of amyloid β formation. It is therefore important to identify the source, detailed structural features as well as factors that favor formation of the neuroprotective forms of HS. Here, a method for isolation and identification of HS-containing APP degradation products has been described. The method is based on isolation of radiolabeled HS followed by identification of accompanying APP degradation products by SDS-PAGE and Western blotting.</p>}},
author = {{Mani, Katrin}},
booktitle = {{Methods in Molecular Biology}},
issn = {{1064-3745}},
keywords = {{Alzheimer’s disease; Amyloid β, Glypican-1; Heparan sulfate}},
language = {{eng}},
pages = {{279--288}},
publisher = {{Humana Press}},
series = {{Methods in Molecular Biology}},
title = {{Isolation and Characterization of Heparan Sulfate Containing Amyloid Precursor Protein Degradation Products}},
url = {{http://dx.doi.org/10.1007/978-1-0716-1398-6_22}},
doi = {{10.1007/978-1-0716-1398-6_22}},
volume = {{2303}},
year = {{2022}},
}