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Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells
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| Zeitschriftentitel: | The EuroBiotech Journal |
|---|---|
| Personen und Körperschaften: | , , , , , , , , |
| In: | The EuroBiotech Journal, 3, 2019, 2, S. 57-70 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Walter de Gruyter GmbH
|
| Schlagwörter: |
| author_facet |
De Riccardis, Lidia Rizzo, Francesca Urso, Emanuela Garzarelli, Valeria Intini, Vincenza Greco, Marco Maffia, Maria Chiara Danieli, Antonio Maffia, Michele De Riccardis, Lidia Rizzo, Francesca Urso, Emanuela Garzarelli, Valeria Intini, Vincenza Greco, Marco Maffia, Maria Chiara Danieli, Antonio Maffia, Michele |
|---|---|
| author |
De Riccardis, Lidia Rizzo, Francesca Urso, Emanuela Garzarelli, Valeria Intini, Vincenza Greco, Marco Maffia, Maria Chiara Danieli, Antonio Maffia, Michele |
| spellingShingle |
De Riccardis, Lidia Rizzo, Francesca Urso, Emanuela Garzarelli, Valeria Intini, Vincenza Greco, Marco Maffia, Maria Chiara Danieli, Antonio Maffia, Michele The EuroBiotech Journal Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells Genetics Molecular Biology Biomedical Engineering Molecular Medicine Food Science Biotechnology |
| author_sort |
de riccardis, lidia |
| spelling |
De Riccardis, Lidia Rizzo, Francesca Urso, Emanuela Garzarelli, Valeria Intini, Vincenza Greco, Marco Maffia, Maria Chiara Danieli, Antonio Maffia, Michele 2564-615X Walter de Gruyter GmbH Genetics Molecular Biology Biomedical Engineering Molecular Medicine Food Science Biotechnology http://dx.doi.org/10.2478/ebtj-2019-0007 <jats:title>Abstract</jats:title> <jats:p>The Prion Protein (PrP) is mostly known for its role in prion diseases, where its misfolding and aggregation can cause fatal neurodegenerative conditions such as the bovine spongiform encephalopathy and human Creutzfeldt–Jakob disease. Physiologically, PrP is involved in several processes including adhesion, proliferation, differentiation and angiogenesis, but the molecular mechanisms behind its role remain unclear. PrP, due to its well-described structure, is known to be able to regulate copper homeostasis; however, copper dyshomeostasis can lead to developmental defects. We investigated PrP-dependent regulation of copper homeostasis in human endothelial cells (HUVEC) using an RNA-interference protocol. PrP knockdown did not influence cell viability in silenced HUVEC (PrPKD) compared to control cells, but significantly increased PrPKD HUVEC cells sensitivity to cytotoxic copper concentrations. A reduction of PrPKD cells reductase activity and copper ions transport capacity was observed. Furthermore, PrPKD-derived spheroids exhibited altered morphogenesis and their derived cells showed a decreased vitality 24 and 48 hours after seeding. PrPKD spheroid-derived cells also showed disrupted tubulogenesis in terms of decreased coverage area, tubule length and total nodes number on matrigel, preserving unaltered VEGF receptors expression levels. Our results highlight PrP physiological role in cellular copper homeostasis and in the angiogenesis of endothelial cells.</jats:p> Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells The EuroBiotech Journal |
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10.2478/ebtj-2019-0007 |
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| title |
Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells |
| title_unstemmed |
Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells |
| title_full |
Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells |
| title_fullStr |
Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells |
| title_full_unstemmed |
Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells |
| title_short |
Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells |
| title_sort |
physiological role of prion protein in copper homeostasis and angiogenic mechanisms of endothelial cells |
| topic |
Genetics Molecular Biology Biomedical Engineering Molecular Medicine Food Science Biotechnology |
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http://dx.doi.org/10.2478/ebtj-2019-0007 |
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2019 |
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57-70 |
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<jats:title>Abstract</jats:title>
<jats:p>The Prion Protein (PrP) is mostly known for its role in prion diseases, where its misfolding and aggregation can cause fatal neurodegenerative conditions such as the bovine spongiform encephalopathy and human Creutzfeldt–Jakob disease. Physiologically, PrP is involved in several processes including adhesion, proliferation, differentiation and angiogenesis, but the molecular mechanisms behind its role remain unclear. PrP, due to its well-described structure, is known to be able to regulate copper homeostasis; however, copper dyshomeostasis can lead to developmental defects. We investigated PrP-dependent regulation of copper homeostasis in human endothelial cells (HUVEC) using an RNA-interference protocol. PrP knockdown did not influence cell viability in silenced HUVEC (PrPKD) compared to control cells, but significantly increased PrPKD HUVEC cells sensitivity to cytotoxic copper concentrations. A reduction of PrPKD cells reductase activity and copper ions transport capacity was observed. Furthermore, PrPKD-derived spheroids exhibited altered morphogenesis and their derived cells showed a decreased vitality 24 and 48 hours after seeding. PrPKD spheroid-derived cells also showed disrupted tubulogenesis in terms of decreased coverage area, tubule length and total nodes number on matrigel, preserving unaltered VEGF receptors expression levels. Our results highlight PrP physiological role in cellular copper homeostasis and in the angiogenesis of endothelial cells.</jats:p> |
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| author | De Riccardis, Lidia, Rizzo, Francesca, Urso, Emanuela, Garzarelli, Valeria, Intini, Vincenza, Greco, Marco, Maffia, Maria Chiara, Danieli, Antonio, Maffia, Michele |
| author_facet | De Riccardis, Lidia, Rizzo, Francesca, Urso, Emanuela, Garzarelli, Valeria, Intini, Vincenza, Greco, Marco, Maffia, Maria Chiara, Danieli, Antonio, Maffia, Michele, De Riccardis, Lidia, Rizzo, Francesca, Urso, Emanuela, Garzarelli, Valeria, Intini, Vincenza, Greco, Marco, Maffia, Maria Chiara, Danieli, Antonio, Maffia, Michele |
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| description | <jats:title>Abstract</jats:title> <jats:p>The Prion Protein (PrP) is mostly known for its role in prion diseases, where its misfolding and aggregation can cause fatal neurodegenerative conditions such as the bovine spongiform encephalopathy and human Creutzfeldt–Jakob disease. Physiologically, PrP is involved in several processes including adhesion, proliferation, differentiation and angiogenesis, but the molecular mechanisms behind its role remain unclear. PrP, due to its well-described structure, is known to be able to regulate copper homeostasis; however, copper dyshomeostasis can lead to developmental defects. We investigated PrP-dependent regulation of copper homeostasis in human endothelial cells (HUVEC) using an RNA-interference protocol. PrP knockdown did not influence cell viability in silenced HUVEC (PrPKD) compared to control cells, but significantly increased PrPKD HUVEC cells sensitivity to cytotoxic copper concentrations. A reduction of PrPKD cells reductase activity and copper ions transport capacity was observed. Furthermore, PrPKD-derived spheroids exhibited altered morphogenesis and their derived cells showed a decreased vitality 24 and 48 hours after seeding. PrPKD spheroid-derived cells also showed disrupted tubulogenesis in terms of decreased coverage area, tubule length and total nodes number on matrigel, preserving unaltered VEGF receptors expression levels. Our results highlight PrP physiological role in cellular copper homeostasis and in the angiogenesis of endothelial cells.</jats:p> |
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| institution | DE-Zi4, DE-Gla1, DE-15, DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161 |
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| spelling | De Riccardis, Lidia Rizzo, Francesca Urso, Emanuela Garzarelli, Valeria Intini, Vincenza Greco, Marco Maffia, Maria Chiara Danieli, Antonio Maffia, Michele 2564-615X Walter de Gruyter GmbH Genetics Molecular Biology Biomedical Engineering Molecular Medicine Food Science Biotechnology http://dx.doi.org/10.2478/ebtj-2019-0007 <jats:title>Abstract</jats:title> <jats:p>The Prion Protein (PrP) is mostly known for its role in prion diseases, where its misfolding and aggregation can cause fatal neurodegenerative conditions such as the bovine spongiform encephalopathy and human Creutzfeldt–Jakob disease. Physiologically, PrP is involved in several processes including adhesion, proliferation, differentiation and angiogenesis, but the molecular mechanisms behind its role remain unclear. PrP, due to its well-described structure, is known to be able to regulate copper homeostasis; however, copper dyshomeostasis can lead to developmental defects. We investigated PrP-dependent regulation of copper homeostasis in human endothelial cells (HUVEC) using an RNA-interference protocol. PrP knockdown did not influence cell viability in silenced HUVEC (PrPKD) compared to control cells, but significantly increased PrPKD HUVEC cells sensitivity to cytotoxic copper concentrations. A reduction of PrPKD cells reductase activity and copper ions transport capacity was observed. Furthermore, PrPKD-derived spheroids exhibited altered morphogenesis and their derived cells showed a decreased vitality 24 and 48 hours after seeding. PrPKD spheroid-derived cells also showed disrupted tubulogenesis in terms of decreased coverage area, tubule length and total nodes number on matrigel, preserving unaltered VEGF receptors expression levels. Our results highlight PrP physiological role in cellular copper homeostasis and in the angiogenesis of endothelial cells.</jats:p> Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells The EuroBiotech Journal |
| spellingShingle | De Riccardis, Lidia, Rizzo, Francesca, Urso, Emanuela, Garzarelli, Valeria, Intini, Vincenza, Greco, Marco, Maffia, Maria Chiara, Danieli, Antonio, Maffia, Michele, The EuroBiotech Journal, Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells, Genetics, Molecular Biology, Biomedical Engineering, Molecular Medicine, Food Science, Biotechnology |
| title | Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells |
| title_full | Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells |
| title_fullStr | Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells |
| title_full_unstemmed | Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells |
| title_short | Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells |
| title_sort | physiological role of prion protein in copper homeostasis and angiogenic mechanisms of endothelial cells |
| title_unstemmed | Physiological role of Prion Protein in Copper homeostasis and angiogenic mechanisms of endothelial cells |
| topic | Genetics, Molecular Biology, Biomedical Engineering, Molecular Medicine, Food Science, Biotechnology |
| url | http://dx.doi.org/10.2478/ebtj-2019-0007 |