Αnti-prion effects of anthocyanins
Prion diseases, also known as Transmissible Spongiform Encephalopathies (TSEs), are protein-based neurodegenerative disorders (NDs) affecting humans and animals. They are characterized by the conformational conversion of the normal cellular prion protein, PrPC, into the pathogenic isoform, PrPSc. Pr...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2024-06-01
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| Series: | Redox Biology |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213231724001095 |
| _version_ | 1797230569084420096 |
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| author | Nikoletta Christoudia Nikolaos Bekas Eirini Kanata Athanasia Chatziefsthathiou Spyros Pettas Korina Karagianni Susana Margarida Da Silva Correia Matthias Schmitz Inga Zerr Ioannis Tsamesidis Konstantinos Xanthopoulos Dimitra Dafou Theodoros Sklaviadis |
| author_facet | Nikoletta Christoudia Nikolaos Bekas Eirini Kanata Athanasia Chatziefsthathiou Spyros Pettas Korina Karagianni Susana Margarida Da Silva Correia Matthias Schmitz Inga Zerr Ioannis Tsamesidis Konstantinos Xanthopoulos Dimitra Dafou Theodoros Sklaviadis |
| author_sort | Nikoletta Christoudia |
| collection | DOAJ |
| description | Prion diseases, also known as Transmissible Spongiform Encephalopathies (TSEs), are protein-based neurodegenerative disorders (NDs) affecting humans and animals. They are characterized by the conformational conversion of the normal cellular prion protein, PrPC, into the pathogenic isoform, PrPSc. Prion diseases are invariably fatal and despite ongoing research, no effective prophylactic or therapeutic avenues are currently available. Anthocyanins (ACNs) are unique flavonoid compounds and interest in their use as potential neuroprotective and/or therapeutic agents against NDs, has increased significantly in recent years. Therefore, we investigated the potential anti-oxidant and anti-prion effects of Oenin and Myrtillin, two of the most common anthocyanins, using the most accepted in the field overexpressing PrPSc in vitro model and a cell free protein aggregation model. Our results, indicate both anthocyanins as strong anti-oxidant compounds, upregulating the expression of genes involved in the anti-oxidant response, and reducing the levels of Reactive Oxygen Species (ROS), produced due to pathogenic prion infection, through the activation of the Keap1-Nrf2 pathway. Importantly, they showcased remarkable anti-prion potential, as they not only caused the clearance of pathogenic PrPSc aggregates, but also completely inhibited the formation of PrPSc fibrils in the Cerebrospinal Fluid (CSF) of patients with Creutzfeldt–Jakob disease (CJD). Therefore, Oenin and Myrtillin possess pleiotropic effects, suggesting their potential use as promising preventive and/or therapeutic agents in prion diseases and possibly in the spectrum of neurodegenerative proteinopathies. |
| first_indexed | 2024-04-24T15:30:34Z |
| format | Article |
| id | doaj.art-19173e07dce8450892cda6e75342de7d |
| institution | Directory Open Access Journal |
| issn | 2213-2317 |
| language | English |
| last_indexed | 2024-04-24T15:30:34Z |
| publishDate | 2024-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Redox Biology |
| spelling | doaj.art-19173e07dce8450892cda6e75342de7d2024-04-02T04:14:56ZengElsevierRedox Biology2213-23172024-06-0172103133Αnti-prion effects of anthocyaninsNikoletta Christoudia0Nikolaos Bekas1Eirini Kanata2Athanasia Chatziefsthathiou3Spyros Pettas4Korina Karagianni5Susana Margarida Da Silva Correia6Matthias Schmitz7Inga Zerr8Ioannis Tsamesidis9Konstantinos Xanthopoulos10Dimitra Dafou11Theodoros Sklaviadis12Department of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 541 24, Thessaloniki, GreeceDepartment of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 541 24, Thessaloniki, GreeceNeurodegenerative Diseases Research Group, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 541 24, Thessaloniki, GreeceDepartment of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 541 24, Thessaloniki, GreeceDepartment of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 541 24, Thessaloniki, Greece; Neurodegenerative Diseases Research Group, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 541 24, Thessaloniki, GreeceDepartment of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 541 24, Thessaloniki, GreeceDepartment of Neurology, German Center for Neurodegenerative Diseases (DZNE), University Medicine Goettingen, 37075, Goettingen, GermanyDepartment of Neurology, German Center for Neurodegenerative Diseases (DZNE), University Medicine Goettingen, 37075, Goettingen, GermanyDepartment of Neurology, German Center for Neurodegenerative Diseases (DZNE), University Medicine Goettingen, 37075, Goettingen, GermanyDepartment of Prosthodontics, School of Dentistry, Faculty of Health Sciences, Aristotle University of Thessaloniki, 541 24, Thessaloniki, GreeceNeurodegenerative Diseases Research Group, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 541 24, Thessaloniki, GreeceDepartment of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 541 24, Thessaloniki, Greece; Corresponding author.Neurodegenerative Diseases Research Group, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 541 24, Thessaloniki, GreecePrion diseases, also known as Transmissible Spongiform Encephalopathies (TSEs), are protein-based neurodegenerative disorders (NDs) affecting humans and animals. They are characterized by the conformational conversion of the normal cellular prion protein, PrPC, into the pathogenic isoform, PrPSc. Prion diseases are invariably fatal and despite ongoing research, no effective prophylactic or therapeutic avenues are currently available. Anthocyanins (ACNs) are unique flavonoid compounds and interest in their use as potential neuroprotective and/or therapeutic agents against NDs, has increased significantly in recent years. Therefore, we investigated the potential anti-oxidant and anti-prion effects of Oenin and Myrtillin, two of the most common anthocyanins, using the most accepted in the field overexpressing PrPSc in vitro model and a cell free protein aggregation model. Our results, indicate both anthocyanins as strong anti-oxidant compounds, upregulating the expression of genes involved in the anti-oxidant response, and reducing the levels of Reactive Oxygen Species (ROS), produced due to pathogenic prion infection, through the activation of the Keap1-Nrf2 pathway. Importantly, they showcased remarkable anti-prion potential, as they not only caused the clearance of pathogenic PrPSc aggregates, but also completely inhibited the formation of PrPSc fibrils in the Cerebrospinal Fluid (CSF) of patients with Creutzfeldt–Jakob disease (CJD). Therefore, Oenin and Myrtillin possess pleiotropic effects, suggesting their potential use as promising preventive and/or therapeutic agents in prion diseases and possibly in the spectrum of neurodegenerative proteinopathies.http://www.sciencedirect.com/science/article/pii/S2213231724001095PrionAnthocyaninsAnti-oxidantNeuroprotectionProteinopathiesPrPSc |
| spellingShingle | Nikoletta Christoudia Nikolaos Bekas Eirini Kanata Athanasia Chatziefsthathiou Spyros Pettas Korina Karagianni Susana Margarida Da Silva Correia Matthias Schmitz Inga Zerr Ioannis Tsamesidis Konstantinos Xanthopoulos Dimitra Dafou Theodoros Sklaviadis Αnti-prion effects of anthocyanins Redox Biology Prion Anthocyanins Anti-oxidant Neuroprotection Proteinopathies PrPSc |
| title | Αnti-prion effects of anthocyanins |
| title_full | Αnti-prion effects of anthocyanins |
| title_fullStr | Αnti-prion effects of anthocyanins |
| title_full_unstemmed | Αnti-prion effects of anthocyanins |
| title_short | Αnti-prion effects of anthocyanins |
| title_sort | αnti prion effects of anthocyanins |
| topic | Prion Anthocyanins Anti-oxidant Neuroprotection Proteinopathies PrPSc |
| url | http://www.sciencedirect.com/science/article/pii/S2213231724001095 |
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