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Heparan Sulfate Proteoglycans in Tauopathy
Tauopathies are a class of neurodegenerative diseases, including Alzheimer’s disease, and are characterized by intraneuronal tau inclusion in the brain and the patient’s cognitive decline with obscure pathogenesis. Heparan sulfate proteoglycans, a major type of extracellular matrix, have been believ...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9776397/ https://www.ncbi.nlm.nih.gov/pubmed/36551220 http://dx.doi.org/10.3390/biom12121792 |
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author | Zhu, Yanan Gandy, Lauren Zhang, Fuming Liu, Jian Wang, Chunyu Blair, Laura J. Linhardt, Robert J. Wang, Lianchun |
author_facet | Zhu, Yanan Gandy, Lauren Zhang, Fuming Liu, Jian Wang, Chunyu Blair, Laura J. Linhardt, Robert J. Wang, Lianchun |
author_sort | Zhu, Yanan |
collection | PubMed |
description | Tauopathies are a class of neurodegenerative diseases, including Alzheimer’s disease, and are characterized by intraneuronal tau inclusion in the brain and the patient’s cognitive decline with obscure pathogenesis. Heparan sulfate proteoglycans, a major type of extracellular matrix, have been believed to involve in tauopathies. The heparan sulfate proteoglycans co-deposit with tau in Alzheimer’s patient brain, directly bind to tau and modulate tau secretion, internalization, and aggregation. This review summarizes the current understanding of the functions and the modulated molecular pathways of heparan sulfate proteoglycans in tauopathies, as well as the implication of dysregulated heparan sulfate proteoglycan expression in tau pathology and the potential of targeting heparan sulfate proteoglycan-tau interaction as a novel therapeutic option. |
format | Online Article Text |
id | pubmed-9776397 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-97763972022-12-23 Heparan Sulfate Proteoglycans in Tauopathy Zhu, Yanan Gandy, Lauren Zhang, Fuming Liu, Jian Wang, Chunyu Blair, Laura J. Linhardt, Robert J. Wang, Lianchun Biomolecules Review Tauopathies are a class of neurodegenerative diseases, including Alzheimer’s disease, and are characterized by intraneuronal tau inclusion in the brain and the patient’s cognitive decline with obscure pathogenesis. Heparan sulfate proteoglycans, a major type of extracellular matrix, have been believed to involve in tauopathies. The heparan sulfate proteoglycans co-deposit with tau in Alzheimer’s patient brain, directly bind to tau and modulate tau secretion, internalization, and aggregation. This review summarizes the current understanding of the functions and the modulated molecular pathways of heparan sulfate proteoglycans in tauopathies, as well as the implication of dysregulated heparan sulfate proteoglycan expression in tau pathology and the potential of targeting heparan sulfate proteoglycan-tau interaction as a novel therapeutic option. MDPI 2022-11-30 /pmc/articles/PMC9776397/ /pubmed/36551220 http://dx.doi.org/10.3390/biom12121792 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Zhu, Yanan Gandy, Lauren Zhang, Fuming Liu, Jian Wang, Chunyu Blair, Laura J. Linhardt, Robert J. Wang, Lianchun Heparan Sulfate Proteoglycans in Tauopathy |
title | Heparan Sulfate Proteoglycans in Tauopathy |
title_full | Heparan Sulfate Proteoglycans in Tauopathy |
title_fullStr | Heparan Sulfate Proteoglycans in Tauopathy |
title_full_unstemmed | Heparan Sulfate Proteoglycans in Tauopathy |
title_short | Heparan Sulfate Proteoglycans in Tauopathy |
title_sort | heparan sulfate proteoglycans in tauopathy |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9776397/ https://www.ncbi.nlm.nih.gov/pubmed/36551220 http://dx.doi.org/10.3390/biom12121792 |
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