A sulphated glycosaminoglycan extract from Placopecten magellanicus inhibits the Alzheimer's disease β-site amyloid precursor protein cleaving enzyme 1 (BACE-1)
The clinically important anticoagulant heparin, a member of the glycosaminoglycan family of carbohydrates that is extracted predominantly from porcine and bovine tissue sources, has previously been shown to inhibit the β-site amyloid precursor protein cleaving enzyme 1 (BACE-1), a key drug target in...
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| Vydáno v: | Carbohydrate research Ročník 525; s. 108747 |
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| Hlavní autoři: | , , , , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
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Netherlands
Elsevier Ltd
01.03.2023
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| ISSN: | 0008-6215, 1873-426X, 1873-426X |
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| Abstract | The clinically important anticoagulant heparin, a member of the glycosaminoglycan family of carbohydrates that is extracted predominantly from porcine and bovine tissue sources, has previously been shown to inhibit the β-site amyloid precursor protein cleaving enzyme 1 (BACE-1), a key drug target in Alzheimer's Disease. In addition, heparin has been shown to exert favourable bioactivities through a number of pathophysiological pathways involved in the disease processes of Alzheimer's Disease including inflammation, oxidative stress, tau phosphorylation and amyloid peptide generation. Despite the multi-target potential of heparin as a therapeutic option for Alzheimer's disease, the repurposing of this medically important biomolecule has to-date been precluded by its high anticoagulant potential. An alternative source to mammalian-derived glycosaminoglycans are those extracted from marine environments and these have been shown to display an expanded repertoire of sequence-space and heterogeneity compared to their mammalian counterparts. Furthermore, many marine-derived glycosaminoglycans appear to retain favourable bioactivities, whilst lacking the high anticoagulant potential of their mammalian counterparts. Here we describe a sulphated, marine-derived glycosaminoglycan extract from the Atlantic Sea Scallop, Placopecten magellanicus that displays high inhibitory potential against BACE-1 (IC50 = 4.8 μg.mL−1) combined with low anticoagulant activity; 25-fold less than that of heparin. This extract possesses a more favourable therapeutic profile compared to pharmaceutical heparin of mammalian provenance and is composed of a mixture of heparan sulphate (HS), with a high content of 6-sulphated N-acetyl glucosamine (64%), and chondroitin sulphate.
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•A GAG extract from the Atlantic Sea Scallop, P. magellanicus, inhibits BACE-1, a key drug-target in Alzheimer's disease.•The GAG extract is predominantly HS, containing a high content of UA-GlcNAc(6S), uncommon in mammalian-derived HS.•The GAG extract possesses highly attenuated anticoagulant potential compared to mammalian-derived heparin. |
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| AbstractList | The clinically important anticoagulant heparin, a member of the glycosaminoglycan family of carbohydrates that is extracted predominantly from porcine and bovine tissue sources, has previously been shown to inhibit the β-site amyloid precursor protein cleaving enzyme 1 (BACE-1), a key drug target in Alzheimer's Disease. In addition, heparin has been shown to exert favourable bioactivities through a number of pathophysiological pathways involved in the disease processes of Alzheimer's Disease including inflammation, oxidative stress, tau phosphorylation and amyloid peptide generation. Despite the multi-target potential of heparin as a therapeutic option for Alzheimer's disease, the repurposing of this medically important biomolecule has to-date been precluded by its high anticoagulant potential. An alternative source to mammalian-derived glycosaminoglycans are those extracted from marine environments and these have been shown to display an expanded repertoire of sequence-space and heterogeneity compared to their mammalian counterparts. Furthermore, many marine-derived glycosaminoglycans appear to retain favourable bioactivities, whilst lacking the high anticoagulant potential of their mammalian counterparts. Here we describe a sulphated, marine-derived glycosaminoglycan extract from the Atlantic Sea Scallop, Placopecten magellanicus that displays high inhibitory potential against BACE-1 (IC₅₀ = 4.8 μg.mL⁻¹) combined with low anticoagulant activity; 25-fold less than that of heparin. This extract possesses a more favourable therapeutic profile compared to pharmaceutical heparin of mammalian provenance and is composed of a mixture of heparan sulphate (HS), with a high content of 6-sulphated N-acetyl glucosamine (64%), and chondroitin sulphate. The clinically important anticoagulant heparin, a member of the glycosaminoglycan family of carbohydrates that is extracted predominantly from porcine and bovine tissue sources, has previously been shown to inhibit the β-site amyloid precursor protein cleaving enzyme 1 (BACE-1), a key drug target in Alzheimer's Disease. In addition, heparin has been shown to exert favourable bioactivities through a number of pathophysiological pathways involved in the disease processes of Alzheimer's Disease including inflammation, oxidative stress, tau phosphorylation and amyloid peptide generation. Despite the multi-target potential of heparin as a therapeutic option for Alzheimer's disease, the repurposing of this medically important biomolecule has to-date been precluded by its high anticoagulant potential. An alternative source to mammalian-derived glycosaminoglycans are those extracted from marine environments and these have been shown to display an expanded repertoire of sequence-space and heterogeneity compared to their mammalian counterparts. Furthermore, many marine-derived glycosaminoglycans appear to retain favourable bioactivities, whilst lacking the high anticoagulant potential of their mammalian counterparts. Here we describe a sulphated, marine-derived glycosaminoglycan extract from the Atlantic Sea Scallop, Placopecten magellanicus that displays high inhibitory potential against BACE-1 (IC = 4.8 μg.mL ) combined with low anticoagulant activity; 25-fold less than that of heparin. This extract possesses a more favourable therapeutic profile compared to pharmaceutical heparin of mammalian provenance and is composed of a mixture of heparan sulphate (HS), with a high content of 6-sulphated N-acetyl glucosamine (64%), and chondroitin sulphate. The clinically important anticoagulant heparin, a member of the glycosaminoglycan family of carbohydrates that is extracted predominantly from porcine and bovine tissue sources, has previously been shown to inhibit the β-site amyloid precursor protein cleaving enzyme 1 (BACE-1), a key drug target in Alzheimer's Disease. In addition, heparin has been shown to exert favourable bioactivities through a number of pathophysiological pathways involved in the disease processes of Alzheimer's Disease including inflammation, oxidative stress, tau phosphorylation and amyloid peptide generation. Despite the multi-target potential of heparin as a therapeutic option for Alzheimer's disease, the repurposing of this medically important biomolecule has to-date been precluded by its high anticoagulant potential. An alternative source to mammalian-derived glycosaminoglycans are those extracted from marine environments and these have been shown to display an expanded repertoire of sequence-space and heterogeneity compared to their mammalian counterparts. Furthermore, many marine-derived glycosaminoglycans appear to retain favourable bioactivities, whilst lacking the high anticoagulant potential of their mammalian counterparts. Here we describe a sulphated, marine-derived glycosaminoglycan extract from the Atlantic Sea Scallop, Placopecten magellanicus that displays high inhibitory potential against BACE-1 (IC50 = 4.8 μg.mL−1) combined with low anticoagulant activity; 25-fold less than that of heparin. This extract possesses a more favourable therapeutic profile compared to pharmaceutical heparin of mammalian provenance and is composed of a mixture of heparan sulphate (HS), with a high content of 6-sulphated N-acetyl glucosamine (64%), and chondroitin sulphate. [Display omitted] •A GAG extract from the Atlantic Sea Scallop, P. magellanicus, inhibits BACE-1, a key drug-target in Alzheimer's disease.•The GAG extract is predominantly HS, containing a high content of UA-GlcNAc(6S), uncommon in mammalian-derived HS.•The GAG extract possesses highly attenuated anticoagulant potential compared to mammalian-derived heparin. The clinically important anticoagulant heparin, a member of the glycosaminoglycan family of carbohydrates that is extracted predominantly from porcine and bovine tissue sources, has previously been shown to inhibit the β-site amyloid precursor protein cleaving enzyme 1 (BACE-1), a key drug target in Alzheimer's Disease. In addition, heparin has been shown to exert favourable bioactivities through a number of pathophysiological pathways involved in the disease processes of Alzheimer's Disease including inflammation, oxidative stress, tau phosphorylation and amyloid peptide generation. Despite the multi-target potential of heparin as a therapeutic option for Alzheimer's disease, the repurposing of this medically important biomolecule has to-date been precluded by its high anticoagulant potential. An alternative source to mammalian-derived glycosaminoglycans are those extracted from marine environments and these have been shown to display an expanded repertoire of sequence-space and heterogeneity compared to their mammalian counterparts. Furthermore, many marine-derived glycosaminoglycans appear to retain favourable bioactivities, whilst lacking the high anticoagulant potential of their mammalian counterparts. Here we describe a sulphated, marine-derived glycosaminoglycan extract from the Atlantic Sea Scallop, Placopecten magellanicus that displays high inhibitory potential against BACE-1 (IC50 = 4.8 μg.mL-1) combined with low anticoagulant activity; 25-fold less than that of heparin. This extract possesses a more favourable therapeutic profile compared to pharmaceutical heparin of mammalian provenance and is composed of a mixture of heparan sulphate (HS), with a high content of 6-sulphated N-acetyl glucosamine (64%), and chondroitin sulphate.The clinically important anticoagulant heparin, a member of the glycosaminoglycan family of carbohydrates that is extracted predominantly from porcine and bovine tissue sources, has previously been shown to inhibit the β-site amyloid precursor protein cleaving enzyme 1 (BACE-1), a key drug target in Alzheimer's Disease. In addition, heparin has been shown to exert favourable bioactivities through a number of pathophysiological pathways involved in the disease processes of Alzheimer's Disease including inflammation, oxidative stress, tau phosphorylation and amyloid peptide generation. Despite the multi-target potential of heparin as a therapeutic option for Alzheimer's disease, the repurposing of this medically important biomolecule has to-date been precluded by its high anticoagulant potential. An alternative source to mammalian-derived glycosaminoglycans are those extracted from marine environments and these have been shown to display an expanded repertoire of sequence-space and heterogeneity compared to their mammalian counterparts. Furthermore, many marine-derived glycosaminoglycans appear to retain favourable bioactivities, whilst lacking the high anticoagulant potential of their mammalian counterparts. Here we describe a sulphated, marine-derived glycosaminoglycan extract from the Atlantic Sea Scallop, Placopecten magellanicus that displays high inhibitory potential against BACE-1 (IC50 = 4.8 μg.mL-1) combined with low anticoagulant activity; 25-fold less than that of heparin. This extract possesses a more favourable therapeutic profile compared to pharmaceutical heparin of mammalian provenance and is composed of a mixture of heparan sulphate (HS), with a high content of 6-sulphated N-acetyl glucosamine (64%), and chondroitin sulphate. |
| ArticleNumber | 108747 |
| Author | Procter, Patricia Fernig, David G. Cooper, Lynsay C. Yates, Edwin A. Miller, Gavin J. Skidmore, Mark A. Devlin, Anthony J. Guimond, Scott E. Mycroft-West, Courtney J. Guerrini, Marco Lima, Marcelo A. |
| Author_xml | – sequence: 1 givenname: Courtney J. surname: Mycroft-West fullname: Mycroft-West, Courtney J. email: courtney.mycroft-west@rfi.ac.uk organization: Centre for Glycoscience Research and Training, Keele University, Keele, Staffordshire, ST5 5BG, UK – sequence: 2 givenname: Anthony J. surname: Devlin fullname: Devlin, Anthony J. email: anthony.devlin@rfi.ac.uk organization: Centre for Glycoscience Research and Training, Keele University, Keele, Staffordshire, ST5 5BG, UK – sequence: 3 givenname: Lynsay C. surname: Cooper fullname: Cooper, Lynsay C. email: lcooper1@glos.ac.uk organization: University of Gloucestershire, Francis Close Hall Campus, Swindon Rd, Cheltenham, GL50 4AZ, UK – sequence: 4 givenname: Scott E. surname: Guimond fullname: Guimond, Scott E. email: s.e.guimond@keele.ac.uk organization: Centre for Glycoscience Research and Training, Keele University, Keele, Staffordshire, ST5 5BG, UK – sequence: 5 givenname: Patricia surname: Procter fullname: Procter, Patricia email: p.procter@keele.ac.uk organization: Centre for Glycoscience Research and Training, Keele University, Keele, Staffordshire, ST5 5BG, UK – sequence: 6 givenname: Gavin J. surname: Miller fullname: Miller, Gavin J. email: g.j.miller@keele.ac.uk organization: Centre for Glycoscience Research and Training, Keele University, Keele, Staffordshire, ST5 5BG, UK – sequence: 7 givenname: Marco surname: Guerrini fullname: Guerrini, Marco email: guerrini@ronzoni.it organization: Istituto di Ricerche Chimiche e Biochimiche G. Ronzoni, Via G. Colombo 81, 20133, Milan, Italy – sequence: 8 givenname: David G. surname: Fernig fullname: Fernig, David G. email: dgfernig@liverpool.ac.uk organization: Department of Biochemistry and Systems Biology, ISMIB, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK – sequence: 9 givenname: Edwin A. surname: Yates fullname: Yates, Edwin A. email: E.A.Yates@liverpool.ac.uk organization: Department of Biochemistry and Systems Biology, ISMIB, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK – sequence: 10 givenname: Marcelo A. surname: Lima fullname: Lima, Marcelo A. email: m.andrade.de.lima@keele.ac.uk organization: Centre for Glycoscience Research and Training, Keele University, Keele, Staffordshire, ST5 5BG, UK – sequence: 11 givenname: Mark A. surname: Skidmore fullname: Skidmore, Mark A. email: m.a.skidmore@keele.ac.uk organization: Centre for Glycoscience Research and Training, Keele University, Keele, Staffordshire, ST5 5BG, UK |
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| Cites_doi | 10.1100/tsw.2009.100 10.1002/chem.201204519 10.1016/j.carbpol.2017.12.018 10.1016/j.biotechadv.2017.07.008 10.1016/j.bmc.2008.09.020 10.1007/s11033-021-06229-9 10.3390/md17050293 10.1021/ac100188x 10.1016/j.chroma.2006.09.064 10.1021/acscentsci.2c01176 10.1016/j.vibspec.2016.12.008 10.1369/0022155412464638 10.1146/annurev.bi.53.070184.004215 10.1042/bj2611035 10.4103/1673-5374.274341 10.1016/j.nbd.2010.06.008 10.1038/85064 10.1016/S0008-6215(00)86160-1 10.1056/NEJMra0909142 10.1016/j.jshs.2016.10.004 10.1074/jbc.M503645200 10.1016/j.carres.2014.03.002 10.3390/biom5032003 10.2174/092986709789878193 10.1083/jcb.200303059 10.1021/jm051221o 10.1016/j.ab.2004.04.031 10.1038/nprot.2007.321 10.1016/j.carres.2007.12.019 10.1042/BST20170404 10.1046/j.1471-4159.1998.70020736.x 10.3390/md19040203 10.1369/0022155412464972 |
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| Keywords | β-site amyloid precursor protein cleaving enzyme 1 Placopecten magellanicus Heparan sulphate BACE-1 β-secretase Glycosaminoglycan Amyloid-β Chondroitin sulphate Heparin Alzheimer's disease |
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| SubjectTerms | Alzheimer disease Alzheimer Disease - drug therapy Alzheimer's disease amyloid Amyloid beta-Peptides Amyloid beta-Protein Precursor - metabolism Amyloid beta-Protein Precursor - therapeutic use Amyloid Precursor Protein Secretases Amyloid-β Animals anticoagulant activity anticoagulants Anticoagulants - chemistry BACE-1 Cattle chondroitin sulfate Chondroitin sulphate enzymes family glucosamine Glycosaminoglycan Glycosaminoglycans - pharmacology heparan sulfate Heparan sulphate Heparin Heparin - pharmacology inflammation Mammals - metabolism oxidative stress Pectinidae - metabolism peptides phosphorylation Placopecten magellanicus provenance Swine therapeutics β-secretase β-site amyloid precursor protein cleaving enzyme 1 |
| Title | A sulphated glycosaminoglycan extract from Placopecten magellanicus inhibits the Alzheimer's disease β-site amyloid precursor protein cleaving enzyme 1 (BACE-1) |
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