Glycosaminoglycans from <i>Litopenaeus vannamei</i> Inhibit the Alzheimer’s Disease β Secretase, BACE1
Only palliative therapeutic options exist for the treatment of Alzheimer’s Disease; no new successful drug candidates have been developed in over 15 years. The widely used clinical anticoagulant heparin has been reported to exert beneficial effects through multiple pathophysiological pathways involv...
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MDPI AG
2021-04-01
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Series: | Marine Drugs |
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Online Access: | https://www.mdpi.com/1660-3397/19/4/203 |
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author | Courtney J. Mycroft-West Anthony J. Devlin Lynsay C. Cooper Scott E. Guimond Patricia Procter Marco Guerrini Gavin J. Miller David G. Fernig Edwin A. Yates Marcelo A. Lima Mark A. Skidmore |
author_facet | Courtney J. Mycroft-West Anthony J. Devlin Lynsay C. Cooper Scott E. Guimond Patricia Procter Marco Guerrini Gavin J. Miller David G. Fernig Edwin A. Yates Marcelo A. Lima Mark A. Skidmore |
author_sort | Courtney J. Mycroft-West |
collection | DOAJ |
description | Only palliative therapeutic options exist for the treatment of Alzheimer’s Disease; no new successful drug candidates have been developed in over 15 years. The widely used clinical anticoagulant heparin has been reported to exert beneficial effects through multiple pathophysiological pathways involved in the aetiology of Alzheimer’s Disease, for example, amyloid peptide production and clearance, tau phosphorylation, inflammation and oxidative stress. Despite the therapeutic potential of heparin as a multi-target drug for Alzheimer’s disease, the repurposing of pharmaceutical heparin is proscribed owing to the potent anticoagulant activity of this drug. Here, a heterogenous non-anticoagulant glycosaminoglycan extract, obtained from the shrimp <i>Litopenaeus vannamei,</i> was found to inhibit the key neuronal β-secretase, BACE1, displaying a more favorable therapeutic ratio compared to pharmaceutical heparin when anticoagulant activity is considered. |
first_indexed | 2024-03-10T12:37:51Z |
format | Article |
id | doaj.art-9cb423e1e6474f8a8ed5966155f70135 |
institution | Directory Open Access Journal |
issn | 1660-3397 |
language | English |
last_indexed | 2024-03-10T12:37:51Z |
publishDate | 2021-04-01 |
publisher | MDPI AG |
record_format | Article |
series | Marine Drugs |
spelling | doaj.art-9cb423e1e6474f8a8ed5966155f701352023-11-21T14:09:40ZengMDPI AGMarine Drugs1660-33972021-04-0119420310.3390/md19040203Glycosaminoglycans from <i>Litopenaeus vannamei</i> Inhibit the Alzheimer’s Disease β Secretase, BACE1Courtney J. Mycroft-West0Anthony J. Devlin1Lynsay C. Cooper2Scott E. Guimond3Patricia Procter4Marco Guerrini5Gavin J. Miller6David G. Fernig7Edwin A. Yates8Marcelo A. Lima9Mark A. Skidmore10Molecular & Structural Biosciences, School of Life Sciences, Keele University, Huxley Building, Keele, Staffordshire ST5 5BG, UKMolecular & Structural Biosciences, School of Life Sciences, Keele University, Huxley Building, Keele, Staffordshire ST5 5BG, UKMolecular & Structural Biosciences, School of Life Sciences, Keele University, Huxley Building, Keele, Staffordshire ST5 5BG, UKSchool of Medicine, Keele University, Huxley Building, Keele, Staffordshire ST5 5BG, UKMolecular & Structural Biosciences, School of Life Sciences, Keele University, Huxley Building, Keele, Staffordshire ST5 5BG, UKIstituto di Ricerche Chimiche e Biochimiche G. Ronzoni, via G. Colombo 81, 20133 Milan, ItalySchool of Chemistry, Keele University, Huxley Building, Keele, Staffordshire ST5 5BG, UKDepartment of Biochemistry and Systems Biology, ISMIB, University of Liverpool, Crown Street, Liverpool L69 7ZB, UKDepartment of Biochemistry and Systems Biology, ISMIB, University of Liverpool, Crown Street, Liverpool L69 7ZB, UKMolecular & Structural Biosciences, School of Life Sciences, Keele University, Huxley Building, Keele, Staffordshire ST5 5BG, UKMolecular & Structural Biosciences, School of Life Sciences, Keele University, Huxley Building, Keele, Staffordshire ST5 5BG, UKOnly palliative therapeutic options exist for the treatment of Alzheimer’s Disease; no new successful drug candidates have been developed in over 15 years. The widely used clinical anticoagulant heparin has been reported to exert beneficial effects through multiple pathophysiological pathways involved in the aetiology of Alzheimer’s Disease, for example, amyloid peptide production and clearance, tau phosphorylation, inflammation and oxidative stress. Despite the therapeutic potential of heparin as a multi-target drug for Alzheimer’s disease, the repurposing of pharmaceutical heparin is proscribed owing to the potent anticoagulant activity of this drug. Here, a heterogenous non-anticoagulant glycosaminoglycan extract, obtained from the shrimp <i>Litopenaeus vannamei,</i> was found to inhibit the key neuronal β-secretase, BACE1, displaying a more favorable therapeutic ratio compared to pharmaceutical heparin when anticoagulant activity is considered.https://www.mdpi.com/1660-3397/19/4/203Alzheimer’s diseaseamyloid-βBACE1β-secretaseglycosaminoglycanchondroitin sulfate |
spellingShingle | Courtney J. Mycroft-West Anthony J. Devlin Lynsay C. Cooper Scott E. Guimond Patricia Procter Marco Guerrini Gavin J. Miller David G. Fernig Edwin A. Yates Marcelo A. Lima Mark A. Skidmore Glycosaminoglycans from <i>Litopenaeus vannamei</i> Inhibit the Alzheimer’s Disease β Secretase, BACE1 Marine Drugs Alzheimer’s disease amyloid-β BACE1 β-secretase glycosaminoglycan chondroitin sulfate |
title | Glycosaminoglycans from <i>Litopenaeus vannamei</i> Inhibit the Alzheimer’s Disease β Secretase, BACE1 |
title_full | Glycosaminoglycans from <i>Litopenaeus vannamei</i> Inhibit the Alzheimer’s Disease β Secretase, BACE1 |
title_fullStr | Glycosaminoglycans from <i>Litopenaeus vannamei</i> Inhibit the Alzheimer’s Disease β Secretase, BACE1 |
title_full_unstemmed | Glycosaminoglycans from <i>Litopenaeus vannamei</i> Inhibit the Alzheimer’s Disease β Secretase, BACE1 |
title_short | Glycosaminoglycans from <i>Litopenaeus vannamei</i> Inhibit the Alzheimer’s Disease β Secretase, BACE1 |
title_sort | glycosaminoglycans from i litopenaeus vannamei i inhibit the alzheimer s disease β secretase bace1 |
topic | Alzheimer’s disease amyloid-β BACE1 β-secretase glycosaminoglycan chondroitin sulfate |
url | https://www.mdpi.com/1660-3397/19/4/203 |
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