Cited by 69Proteoglycans and glycosaminoglycans researchAlzheimer's disease research and treatmentsOsteoarthritis Treatment and Mechanisms

Glycosaminoglycans from Alzheimer’s disease hippocampus have altered capacities to bind and regulate growth factors activities and to bind tau

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Huynh, Minh Bao, Ouidja, Mohand Ouidir, Chantepie, Sandrine, Carpentier, Gilles, Maïza, Auriane, Zhang, Ganlin, Vilares, Joao, Raisman-Vozari, Rita +1 more·2019·PLOS ONE

Abstract

Glycosaminoglycans (GAGs), including heparan sulfates and chondroitin sulfates, are major components of the extracellular matrix. Upon interacting with heparin binding growth factors (HBGF), GAGs participate to the maintaintenance of tissue homeostasis and contribute to self-healing. Although several processes regulated by HBGF are altered in Alzheimer's disease, it is unknown whether the brain GAG capacities to bind and regulate the function of HBGF or of other heparin binding proteins, as tau, are modified in this disease. Here, we show that total sulfated GAGs from hippocampus of Alzheimer's disease have altered capacities to bind and potentiate the activities of growth factors including FGF-2, VEGF, and BDNF while their capacity to bind to tau is remarkable increased. Alterations of GAG structures and capacities to interact with and regulate the activity of heparin binding proteins might contribute to impaired tissue homeostasis in the Alzheimer's disease brain.

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  • CHST8 encodes carbohydrate sulfotransferase 8, which has been suggested to be enriched in Alzheimer's disease pathology progression and increased in the hippocampus of Alzheimer's disease brains.

    “This enzyme has been suggested to be enriched in AD pathology progression [144] and increased in the hippocampus of AD brains [64].”

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References 48 · Cited by 69

Research works printed but not linked: 1

  1. [35]Suttkus A, Holzer M, Morawski M, Arendt T. The neuronal extracellular matrix restricts distribution and internalization of aggregated Tau-protein. Neuroscience. 2016 1 28; 313: 225– 35. Epub 2015/11/24. 10.1016/j.neuroscience.2015.11.040. 26621125 · DOI · Paper page

Authors
Huynh, M. B., Ouidja, M. O., Chantepie, S., Carpentier, G., Maïza, A., Zhang, G., Vilares, J., Raisman-Vozari, R., & Papy-Garcia, D.
Affiliations
  • Centre National de la Recherche Scientifique (FR)
  • Universidade Federal de São Paulo (BR)
Venue
PLOS ONE
Published
2019-01-04
Volume
14
Issue
1
Pages
e0209573
ISSN
1932-6203 (ISSN-L)
OpenAlex
W2907733456
Cited by
69
References
48
Citations by year
2026: 7 · 2025: 7 · 2024: 9 · 2023: 9 · 2022: 11 · 2021: 19 · 2020: 3 · 2019: 4
FWCI
4.90
Type
journal article
Language
en
Open access
Locations
  • PLoS ONE (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • HAL (submittedVersion, other-oa)
  • HAL (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Figshare (submittedVersion, cc-by)
Funders
  • H2020 Future and Emerging Technologies (737390)
  • Fondation Vaicre Alzheimer (FR-15055)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Health Sciences › Medicine › Rheumatology › Osteoarthritis Treatment and Mechanisms
Keywords
glycosaminoglycans, Alzheimer's disease, hippocampus, heparan sulfate, chondroitin sulfate, heparin-binding growth factors, FGF2, vascular endothelial growth factor, brain-derived neurotrophic factor, tau protein, extracellular matrix, growth factor binding, tissue homeostasis
MeSH terms
Aged, Aged, 80 and over, Alzheimer Disease, Brain, Brazil, Chondroitin Sulfates, Extracellular Matrix, Female, Glycosaminoglycans, Heparin, Heparan Sulfate, Hippocampus, Humans, Male, Middle Aged, Protein Binding, Temporal Lobe, Fibroblast Growth Factor 2, tau Proteins, Brain-Derived Neurotrophic Factor, Vascular Endothelial Growth Factor A

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