19 results on '"Stommen, Amaury"'
Search Results
2. Piezo1 Regulation Involves Lipid Domains and the Cytoskeleton and Is Favored by the Stomatocyte–Discocyte–Echinocyte Transformation
- Author
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Stommen, Amaury, Ghodsi, Marine, Cloos, Anne Sophie, Conrard, Louise, Dumitru, Andra C., Henriet, Patrick, Pierreux, Christophe, Alsteens, David, Tyteca, Donatienne, Stommen, Amaury, Ghodsi, Marine, Cloos, Anne Sophie, Conrard, Louise, Dumitru, Andra C., Henriet, Patrick, Pierreux, Christophe, Alsteens, David, and Tyteca, Donatienne
- Abstract
Piezo1 is a mechanosensitive ion channel required for various biological processes, but its regulation remains poorly understood. Here, we used erythrocytes to address this question since they display Piezo1 clusters, a strong and dynamic cytoskeleton and three types of submicrometric lipid domains, respectively enriched in cholesterol, GM1 ganglioside/cholesterol and sphingomyelin/cholesterol. We revealed that Piezo1 clusters were present in both the rim and the dimple erythrocyte regions. Upon Piezo1 chemical activation by Yoda1, the Piezo1 cluster proportion mainly increased in the dimple area. This increase was accompanied by Ca2+ influx and a rise in echinocytes, in GM1/cholesterol-enriched domains in the dimple and in cholesterol-enriched domains in the rim. Conversely, the effects of Piezo1 activation were abrogated upon membrane cholesterol depletion. Furthermore, upon Piezo1-independent Ca2+ influx, the above changes were not observed. In healthy donors with a high echinocyte proportion, Ca2+ influx, lipid domains and Piezo1 fluorescence were high even at resting state, whereas the cytoskeleton membrane occupancy was lower. Accordingly, upon decreases in cytoskeleton membrane occupancy and stiffness in erythrocytes from patients with hereditary spherocytosis, Piezo1 fluorescence was increased. Altogether, we showed that Piezo1 was differentially controlled by lipid domains and the cytoskeleton and was favored by the stomatocyte–discocyte–echinocyte transformation., SCOPUS: ar.j, info:eu-repo/semantics/published
- Published
- 2024
3. A novel missense variant in ATP11C is associated with reduced red blood cell phosphatidylserine flippase activity and mild hereditary hemolytic anemia
- Author
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van Dijk, Myrthe J., primary, van Oirschot, Brigitte A., additional, Harrison, Alexander N., additional, Recktenwald, Steffen M., additional, Qiao, Min, additional, Stommen, Amaury, additional, Cloos, Anne‐Sophie, additional, Vanderroost, Juliette, additional, Terrasi, Romano, additional, Dey, Kuntal, additional, Bos, Jennifer, additional, Rab, Minke A. E., additional, Bogdanova, Anna, additional, Minetti, Giampaolo, additional, Muccioli, Giulio G., additional, Tyteca, Donatienne, additional, Egée, Stéphane, additional, Kaestner, Lars, additional, Molday, Robert S., additional, van Beers, Eduard J., additional, and van Wijk, Richard, additional
- Published
- 2023
- Full Text
- View/download PDF
4. P1481: SYSTEMATICALLY REDUCED RED CELL PHOSPHATIDYLSERINE FLIPPASE ACTIVITY IS SUFFICIENT TO INDUCE HEREDITARY HEMOLYTIC ANEMIA
- Author
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van Dijk, Myrthe, primary, van Oirschot, Brigitte, additional, Harrison, Alexander, additional, Recktenwald, Steffen, additional, Stommen, Amaury, additional, Dey, Kuntal, additional, Bos, Jennifer, additional, Rab, Minke, additional, Bogdanova, Anna, additional, Minetti, Giampaolo, additional, Tyteca, Donatienne, additional, Egée, Stéphane, additional, Kaestner, Lars, additional, Molday, Robert, additional, van Beers, Eduard, additional, and Van Wijk, Richard, additional
- Published
- 2023
- Full Text
- View/download PDF
5. Splenectomy improves erythrocyte functionality in spherocytosis based on septin abundance but not maturation defects
- Author
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UCL - SSS/DDUV - Institut de Duve, UCL - SSS/DDUV/CELL - Biologie cellulaire, UCL - SSS/DDUV/CBIO - Computational Biology and Bioinformatics, UCL - SSS/DDUV/GEHU - Génétique, UCL - SSS/DDUV/PHOS - Protein phosphorylation, UCL - SSS/IREC/PEDI - Pôle de Pédiatrie, UCL - SSS/IREC/SLUC - Pôle St.-Luc, UCL - SSS/LDRI - Louvain Drug Research Institute, UCL - (SLuc) Service d'hématologie, UCL - (SLuc) Service d'hématologie et d'oncologie pédiatrique, Cloos, Anne-Sophie, Pollet, Hélène, Stommen, Amaury, Maja, Mauriane, Lingurski, Maxime, Brichard, Bénédicte, Lambert, Catherine, Henriet, Patrick, Pierreux, Christophe, Pyr dit Ruys, Sébastien, Van Der Smissen, Patrick, Vikkula, Miikka, Gatto, Laurent, Martin, Manon, Brouillard, Pascal, Vertommen, Didier, Tyteca, Donatienne, UCL - SSS/DDUV - Institut de Duve, UCL - SSS/DDUV/CELL - Biologie cellulaire, UCL - SSS/DDUV/CBIO - Computational Biology and Bioinformatics, UCL - SSS/DDUV/GEHU - Génétique, UCL - SSS/DDUV/PHOS - Protein phosphorylation, UCL - SSS/IREC/PEDI - Pôle de Pédiatrie, UCL - SSS/IREC/SLUC - Pôle St.-Luc, UCL - SSS/LDRI - Louvain Drug Research Institute, UCL - (SLuc) Service d'hématologie, UCL - (SLuc) Service d'hématologie et d'oncologie pédiatrique, Cloos, Anne-Sophie, Pollet, Hélène, Stommen, Amaury, Maja, Mauriane, Lingurski, Maxime, Brichard, Bénédicte, Lambert, Catherine, Henriet, Patrick, Pierreux, Christophe, Pyr dit Ruys, Sébastien, Van Der Smissen, Patrick, Vikkula, Miikka, Gatto, Laurent, Martin, Manon, Brouillard, Pascal, Vertommen, Didier, and Tyteca, Donatienne
- Published
- 2023
6. A novel missense variant in ATP11C is associated with reduced red blood cell phosphatidylserine flippase activity and mild hereditary hemolytic anemia
- Author
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van Dijk, Myrthe J., van Oirschot, Brigitte A., Harrison, Alexander N., Recktenwald, Steffen M., Qiao, Min, Stommen, Amaury, Cloos, Anne Sophie, Vanderroost, Juliette, Terrasi, Romano, Dey, Kuntal, Bos, Jennifer, Rab, Minke A.E., Bogdanova, Anna, Minetti, Giampaolo, Muccioli, Giulio G., Tyteca, Donatienne, Egée, Stéphane, Kaestner, Lars, Molday, Robert S., van Beers, Eduard J., van Wijk, Richard, van Dijk, Myrthe J., van Oirschot, Brigitte A., Harrison, Alexander N., Recktenwald, Steffen M., Qiao, Min, Stommen, Amaury, Cloos, Anne Sophie, Vanderroost, Juliette, Terrasi, Romano, Dey, Kuntal, Bos, Jennifer, Rab, Minke A.E., Bogdanova, Anna, Minetti, Giampaolo, Muccioli, Giulio G., Tyteca, Donatienne, Egée, Stéphane, Kaestner, Lars, Molday, Robert S., van Beers, Eduard J., and van Wijk, Richard
- Abstract
Adenosine Triphosphatase (ATPase) Phospholipid Transporting 11C gene (ATP11C) encodes the major phosphatidylserine (PS) flippase in human red blood cells (RBCs). Flippases actively transport phospholipids (e.g., PS) from the outer to the inner leaflet to establish and maintain phospholipid asymmetry of the lipid bilayer of cell membranes. This asymmetry is crucial for survival since externalized PS triggers phagocytosis by splenic macrophages. Here we report on pathophysiological consequences of decreased flippase activity, prompted by a patient with hemolytic anemia and hemizygosity for a novel c.2365C > T p.(Leu789Phe) missense variant in ATP11C. ATP11C protein expression was strongly reduced by 58% in patient-derived RBC ghosts. Furthermore, functional characterization showed only 26% PS flippase activity. These results were confirmed by recombinant mutant ATP11C protein expression in HEK293T cells, which was decreased to 27% compared to wild type, whereas PS-stimulated ATPase activity was decreased by 57%. Patient RBCs showed a mild increase in PS surface exposure when compared to control RBCs, which further increased in the most dense RBCs after RBC storage stress. The increase in PS was not due to higher global membrane content of PS or other phospholipids. In contrast, membrane lipid lateral distribution showed increased abundance of cholesterol-enriched domains in RBC low curvature areas. Finally, more dense RBCs and subtle changes in RBC morphology under flow hint toward alterations in flow behavior of ATP11C-deficient RBCs. Altogether, ATP11C deficiency is the likely cause of hemolytic anemia in our patient, thereby underlining the physiological role and relevance of this flippase in human RBCs.
- Published
- 2023
7. A novel missense variant in ATP11C is associated with reduced red blood cell phosphatidylserine flippase activity and mild hereditary hemolytic anemia
- Author
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CDL Rode cel, Unit Opleiding Aios, CDL Research analisten, Secretariaat Hematologie, Circulatory Health, Poli Van Creveldkliniek Medisch, Child Health, CDL Cluster Speciële Diagnostiek, van Dijk, Myrthe J., van Oirschot, Brigitte A., Harrison, Alexander N., Recktenwald, Steffen M., Qiao, Min, Stommen, Amaury, Cloos, Anne Sophie, Vanderroost, Juliette, Terrasi, Romano, Dey, Kuntal, Bos, Jennifer, Rab, Minke A.E., Bogdanova, Anna, Minetti, Giampaolo, Muccioli, Giulio G., Tyteca, Donatienne, Egée, Stéphane, Kaestner, Lars, Molday, Robert S., van Beers, Eduard J., van Wijk, Richard, CDL Rode cel, Unit Opleiding Aios, CDL Research analisten, Secretariaat Hematologie, Circulatory Health, Poli Van Creveldkliniek Medisch, Child Health, CDL Cluster Speciële Diagnostiek, van Dijk, Myrthe J., van Oirschot, Brigitte A., Harrison, Alexander N., Recktenwald, Steffen M., Qiao, Min, Stommen, Amaury, Cloos, Anne Sophie, Vanderroost, Juliette, Terrasi, Romano, Dey, Kuntal, Bos, Jennifer, Rab, Minke A.E., Bogdanova, Anna, Minetti, Giampaolo, Muccioli, Giulio G., Tyteca, Donatienne, Egée, Stéphane, Kaestner, Lars, Molday, Robert S., van Beers, Eduard J., and van Wijk, Richard
- Published
- 2023
8. A novel missense variant in $ATP11C$ is associated with reduced red blood cell phosphatidylserine flippase activity and mild hereditary hemolytic anemia
- Author
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van Dijk, Myrthe J; https://orcid.org/0000-0002-9377-0367, van Oirschot, Brigitte A, Harrison, Alexander N; https://orcid.org/0000-0002-7290-4725, Recktenwald, Steffen M; https://orcid.org/0000-0003-1235-1521, Qiao, Min; https://orcid.org/0000-0002-2734-6824, Stommen, Amaury; https://orcid.org/0000-0003-4761-8521, Cloos, Anne‐Sophie, Vanderroost, Juliette, Terrasi, Romano, Dey, Kuntal; https://orcid.org/0000-0001-6590-2804, Bos, Jennifer, Rab, Minke A E, Bogdanova, Anna; https://orcid.org/0000-0003-0502-5381, Minetti, Giampaolo; https://orcid.org/0000-0003-3063-4613, Muccioli, Giulio G, Tyteca, Donatienne; https://orcid.org/0000-0002-7334-2648, Egée, Stéphane, Kaestner, Lars; https://orcid.org/0000-0001-6796-9535, Molday, Robert S; https://orcid.org/0000-0002-4479-1831, van Beers, Eduard J; https://orcid.org/0000-0002-3934-7189, van Wijk, Richard; https://orcid.org/0000-0002-8236-8292, van Dijk, Myrthe J; https://orcid.org/0000-0002-9377-0367, van Oirschot, Brigitte A, Harrison, Alexander N; https://orcid.org/0000-0002-7290-4725, Recktenwald, Steffen M; https://orcid.org/0000-0003-1235-1521, Qiao, Min; https://orcid.org/0000-0002-2734-6824, Stommen, Amaury; https://orcid.org/0000-0003-4761-8521, Cloos, Anne‐Sophie, Vanderroost, Juliette, Terrasi, Romano, Dey, Kuntal; https://orcid.org/0000-0001-6590-2804, Bos, Jennifer, Rab, Minke A E, Bogdanova, Anna; https://orcid.org/0000-0003-0502-5381, Minetti, Giampaolo; https://orcid.org/0000-0003-3063-4613, Muccioli, Giulio G, Tyteca, Donatienne; https://orcid.org/0000-0002-7334-2648, Egée, Stéphane, Kaestner, Lars; https://orcid.org/0000-0001-6796-9535, Molday, Robert S; https://orcid.org/0000-0002-4479-1831, van Beers, Eduard J; https://orcid.org/0000-0002-3934-7189, and van Wijk, Richard; https://orcid.org/0000-0002-8236-8292
- Abstract
Adenosine Triphosphatase (ATPase) Phospholipid Transporting 11C gene (ATP11C) encodes the major phosphatidylserine (PS) flippase in human red blood cells (RBCs). Flippases actively transport phospholipids (e.g., PS) from the outer to the inner leaflet to establish and maintain phospholipid asymmetry of the lipid bilayer of cell membranes. This asymmetry is crucial for survival since externalized PS triggers phagocytosis by splenic macrophages. Here we report on pathophysiological consequences of decreased flippase activity, prompted by a patient with hemolytic anemia and hemizygosity for a novel c.2365C > T p.(Leu789Phe) missense variant in ATP11C. ATP11C protein expression was strongly reduced by 58% in patient‐derived RBC ghosts. Furthermore, functional characterization showed only 26% PS flippase activity. These results were confirmed by recombinant mutant ATP11C protein expression in HEK293T cells, which was decreased to 27% compared to wild type, whereas PS‐stimulated ATPase activity was decreased by 57%. Patient RBCs showed a mild increase in PS surface exposure when compared to control RBCs, which further increased in the most dense RBCs after RBC storage stress. The increase in PS was not due to higher global membrane content of PS or other phospholipids. In contrast, membrane lipid lateral distribution showed increased abundance of cholesterol‐enriched domains in RBC low curvature areas. Finally, more dense RBCs and subtle changes in RBC morphology under flow hint toward alterations in flow behavior of ATP11C‐deficient RBCs. Altogether, ATP11C deficiency is the likely cause of hemolytic anemia in our patient, thereby underlining the physiological role and relevance of this flippase in human RBCs.
- Published
- 2023
9. Vers une meilleure compréhension des microvésicules dans les concentrés érythrocytaires
- Author
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Ghodsi, Marine, primary, Cloos, Anne-Sophie, additional, Stommen, Amaury, additional, Vanderroost, Juliette, additional, Van Der Smissen, Patrick, additional, Cellier, Nicolas, additional, Najdovski, Tome, additional, and Tyteca, Donatienne, additional
- Published
- 2021
- Full Text
- View/download PDF
10. Probing PIEZO1 Localization upon Activation Using High-Resolution Atomic Force and Confocal Microscopy
- Author
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Dumitru, Andra C., primary, Stommen, Amaury, additional, Koehler, Melanie, additional, Cloos, Anne-Sophie, additional, Yang, Jinsung, additional, Leclercqz, Arnaud, additional, Tyteca, Donatienne, additional, and Alsteens, David, additional
- Published
- 2021
- Full Text
- View/download PDF
11. Impaired Cytoskeletal and Membrane Biophysical Properties of Acanthocytes in Hypobetalipoproteinemia – A Case Study
- Author
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UCL - SST/LIBST - Louvain Institute of Biomolecular Science and Technology, UCL - SSS/DDUV - Institut de Duve, UCL - SSS/DDUV/CELL - Biologie cellulaire, UCL - SSS/LDRI - Louvain Drug Research Institute, Cloos, Anne-Sophie, Daenen, Laura G. M., Maja, Mauriane, Stommen, Amaury, Vanderroost, Juliette, Van Der Smissen, Patrick, Rab, Minke, Westerink, Jan, Mignolet, Eric, Larondelle, Yvan, Terrasi, Romano, Muccioli, Giulio, Dumitru, Andra-Cristina, Alsteens, David, van Wijk, Richard, Tyteca, Donatienne, UCL - SST/LIBST - Louvain Institute of Biomolecular Science and Technology, UCL - SSS/DDUV - Institut de Duve, UCL - SSS/DDUV/CELL - Biologie cellulaire, UCL - SSS/LDRI - Louvain Drug Research Institute, Cloos, Anne-Sophie, Daenen, Laura G. M., Maja, Mauriane, Stommen, Amaury, Vanderroost, Juliette, Van Der Smissen, Patrick, Rab, Minke, Westerink, Jan, Mignolet, Eric, Larondelle, Yvan, Terrasi, Romano, Muccioli, Giulio, Dumitru, Andra-Cristina, Alsteens, David, van Wijk, Richard, and Tyteca, Donatienne
- Abstract
Familial hypobetalipoproteinemia is a metabolic disorder mainly caused by mutations in the apolipoprotein B gene. In its homozygous form it can lead without treatment to severe ophthalmological and neurological manifestations. In contrast, the heterozygous form is generally asymptomatic but associated with a low risk of cardiovascular disease. Acanthocytes or thorny red blood cells (RBCs) are described for both forms of the disease. However, those morphological changes are poorly characterized and their potential consequences for RBC functionality are not understood. Thus, in the present study, we asked whether, to what extent and how acanthocytes from a patient with heterozygous familial hypobetalipoproteinemia could exhibit altered RBC functionality. Acanthocytes represented 50% of the total RBC population and contained mitoTracker-positive surface patches, indicating the presence of mitochondrial fragments. While RBC osmotic fragility, calcium content and ATP homeostasis were preserved, a slight decrease of RBC deformability combined with an increase of intracellular free reactive oxygen species were observed. The spectrin cytoskeleton was altered, showing a lower density and an enrichment in patches. At the membrane level, no obvious modification of the RBC membrane fatty acids nor of the cholesterol content were detected but the ceramide species were all increased. Membrane stiffness and curvature were also increased whereas transversal asymmetry was preserved. In contrast, lateral asymmetry was highly impaired showing: (i) increased abundance and decreased functionality of sphingomyelin-enriched domains; (ii) cholesterol enrichment in spicules; and (iii) ceramide enrichment in patches. We propose that oxidative stress induces cytoskeletal alterations, leading to increased membrane stiffness and curvature and impaired lipid lateral distribution in domains and spicules. In addition, ceramide- and spectrin-enriched patches could result from a RBC maturation defec
- Published
- 2021
12. Probing PIEZO1 Localization upon Activation Using High-Resolution Atomic Force and Confocal Microscopy
- Author
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UCL - SST/LIBST - Louvain Institute of Biomolecular Science and Technology, Dumitru, Andra C., Stommen, Amaury, Koehler, Melanie, Cloos, Anne-Sophie, Yang, Jinsung, Leclercqz, Arnaud, Tyteca, Donatienne, Alsteens, David, UCL - SST/LIBST - Louvain Institute of Biomolecular Science and Technology, Dumitru, Andra C., Stommen, Amaury, Koehler, Melanie, Cloos, Anne-Sophie, Yang, Jinsung, Leclercqz, Arnaud, Tyteca, Donatienne, and Alsteens, David
- Abstract
PIEZO1 ion channels are activated by mechanical stimuli, triggering intracellular chemical signals. Recent structural studies suggest that plasma membrane tension or local curvature changes modulate PIEZO1 channel gating and activation. However, whether PIEZO1 localization is governed by tension gradients or long-range mechanical perturbations across the cells is still unclear. Here, we probe the nanoscale localization of PIEZO1 on red blood cells (RBCs) at high resolution (∼30 nm), and we report for the first time the existence of submicrometric PIEZO1 clusters in native conditions. Upon interaction with Yoda1, an allosteric modulator, PIEZO1 clusters increase in abundance in regions of higher membrane tension and lower curvature. We further show that PIEZO1 ion channels interact with the spectrin cytoskeleton in both resting and activated states. Our results point toward a strong interplay between plasma membrane tension gradients, curvature, and cytoskeleton association of PIEZO1.
- Published
- 2021
13. Impaired Cytoskeletal and Membrane Biophysical Properties of Acanthocytes in Hypobetalipoproteinemia – A Case Study
- Author
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MS Hematologie, CDL Rode cel, Unit Opleiding Aios, Circulatory Health, MS Interne Geneeskunde, CDL Arcadia, Cloos, Anne Sophie, Daenen, Laura G.M., Maja, Mauriane, Stommen, Amaury, Vanderroost, Juliette, Van Der Smissen, Patrick, Rab, Minke, Westerink, Jan, Mignolet, Eric, Larondelle, Yvan, Terrasi, Romano, Muccioli, Giulio G., Dumitru, Andra C., Alsteens, David, van Wijk, Richard, Tyteca, Donatienne, MS Hematologie, CDL Rode cel, Unit Opleiding Aios, Circulatory Health, MS Interne Geneeskunde, CDL Arcadia, Cloos, Anne Sophie, Daenen, Laura G.M., Maja, Mauriane, Stommen, Amaury, Vanderroost, Juliette, Van Der Smissen, Patrick, Rab, Minke, Westerink, Jan, Mignolet, Eric, Larondelle, Yvan, Terrasi, Romano, Muccioli, Giulio G., Dumitru, Andra C., Alsteens, David, van Wijk, Richard, and Tyteca, Donatienne
- Published
- 2021
14. Impaired Cytoskeletal and Membrane Biophysical Properties of Acanthocytes in Hypobetalipoproteinemia – A Case Study
- Author
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Cloos, Anne-Sophie, primary, Daenen, Laura G. M., additional, Maja, Mauriane, additional, Stommen, Amaury, additional, Vanderroost, Juliette, additional, Van Der Smissen, Patrick, additional, Rab, Minke, additional, Westerink, Jan, additional, Mignolet, Eric, additional, Larondelle, Yvan, additional, Terrasi, Romano, additional, Muccioli, Giulio G., additional, Dumitru, Andra C., additional, Alsteens, David, additional, van Wijk, Richard, additional, and Tyteca, Donatienne, additional
- Published
- 2021
- Full Text
- View/download PDF
15. Interplay Between Plasma Membrane Lipid Alteration, Oxidative Stress and Calcium-Based Mechanism for Extracellular Vesicle Biogenesis From Erythrocytes During Blood Storage.
- Author
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UCL - SSS/DDUV - Institut de Duve, UCL - SSS/DDUV/CELL - Biologie cellulaire, UCL - SSS/DDUV/GECE - Génétique cellulaire, UCL - SSS/IONS - Institute of NeuroScience, UCL - SSS/IONS/CEMO - Pôle Cellulaire et moléculaire, UCL - SSS/LDRI - Louvain Drug Research Institute, UCL - SST/LIBST - Louvain Institute of Biomolecular Science and Technology, Cloos, Anne-Sophie, Ghodsi, Marine, Stommen, Amaury, Vanderroost, Juliette, Dauguet, Nicolas, Pollet, Hélène, D'Auria, Ludovic, Mignolet, Eric, Larondelle, Yvan, Terrasi, Romano, Muccioli, Giulio, Van Der Smissen, Patrick, Tyteca, Donatienne, UCL - SSS/DDUV - Institut de Duve, UCL - SSS/DDUV/CELL - Biologie cellulaire, UCL - SSS/DDUV/GECE - Génétique cellulaire, UCL - SSS/IONS - Institute of NeuroScience, UCL - SSS/IONS/CEMO - Pôle Cellulaire et moléculaire, UCL - SSS/LDRI - Louvain Drug Research Institute, UCL - SST/LIBST - Louvain Institute of Biomolecular Science and Technology, Cloos, Anne-Sophie, Ghodsi, Marine, Stommen, Amaury, Vanderroost, Juliette, Dauguet, Nicolas, Pollet, Hélène, D'Auria, Ludovic, Mignolet, Eric, Larondelle, Yvan, Terrasi, Romano, Muccioli, Giulio, Van Der Smissen, Patrick, and Tyteca, Donatienne
- Abstract
The shedding of extracellular vesicles (EVs) from the red blood cell (RBC) surface is observed during senescence and RBC storage . Two main models for EV shedding, respectively based on calcium rise and oxidative stress, have been proposed in the literature but the role of the plasma membrane lipid composition and properties is not understood. Using blood in K/EDTA tubes stored for up to 4 weeks at 4°C as a relevant RBC vesiculation model, we showed here that the RBC plasma membrane lipid composition, organization in domains and biophysical properties were progressively modified during storage and contributed to the RBC vesiculation. First, the membrane content in cholesterol and linoleic acid decreased whereas lipid peroxidation and spectrin:membrane occupancy increased, all compatible with higher membrane rigidity. Second, phosphatidylserine surface exposure showed a first rapid rise due to membrane cholesterol decrease, followed by a second calcium-dependent increase. Third, lipid domains mainly enriched in GM1 or sphingomyelin strongly increased from the 1st week while those mainly enriched in cholesterol or ceramide decreased during the 1st and 4th week, respectively. Fourth, the plasmatic acid sphingomyelinase activity considerably increased upon storage following the sphingomyelin-enriched domain rise and potentially inducing the loss of ceramide-enriched domains. Fifth, in support of the shedding of cholesterol- and ceramide-enriched domains from the RBC surface, the number of cholesterol-enriched domains lost and the abundance of EVs released during the 1st week perfectly matched. Moreover, RBC-derived EVs were enriched in ceramide at the 4th week but depleted in sphingomyelin. Then, using K/EDTA tubes supplemented with glucose to longer preserve the ATP content, we better defined the sequence of events. Altogether, we showed that EV shedding from lipid domains only represents part of the global vesiculation mechanistics, for which we propose four successiv
- Published
- 2020
16. Aberrant Membrane Composition and Biophysical Properties Impair Erythrocyte Morphology and Functionality in Elliptocytosis
- Author
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Pollet, Hélène, primary, Cloos, Anne-Sophie, additional, Stommen, Amaury, additional, Vanderroost, Juliette, additional, Conrard, Louise, additional, Paquot, Adrien, additional, Ghodsi, Marine, additional, Carquin, Mélanie, additional, Léonard, Catherine, additional, Guthmann, Manuel, additional, Lingurski, Maxime, additional, Vermylen, Christiane, additional, Killian, Theodore, additional, Gatto, Laurent, additional, Rider, Mark, additional, Pyr dit Ruys, Sébastien, additional, Vertommen, Didier, additional, Vikkula, Miikka, additional, Brouillard, Pascal, additional, Van Der Smissen, Patrick, additional, Muccioli, Giulio G., additional, and Tyteca, Donatienne, additional
- Published
- 2020
- Full Text
- View/download PDF
17. Interplay Between Plasma Membrane Lipid Alteration, Oxidative Stress and Calcium-Based Mechanism for Extracellular Vesicle Biogenesis From Erythrocytes During Blood Storage
- Author
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Cloos, Anne-Sophie, primary, Ghodsi, Marine, additional, Stommen, Amaury, additional, Vanderroost, Juliette, additional, Dauguet, Nicolas, additional, Pollet, Hélène, additional, D’Auria, Ludovic, additional, Mignolet, Eric, additional, Larondelle, Yvan, additional, Terrasi, Romano, additional, Muccioli, Giulio G., additional, Van Der Smissen, Patrick, additional, and Tyteca, Donatienne, additional
- Published
- 2020
- Full Text
- View/download PDF
18. Spatial Relationship and Functional Relevance of Three Lipid Domain Populations at the Erythrocyte Surface
- Author
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Conrard, Louise, primary, Stommen, Amaury, additional, Cloos, Anne-Sophie, additional, Steinkühler, Jan, additional, Dimova, Rumiana, additional, Pollet, Hélène, additional, and Tyteca, Donatienne, additional
- Published
- 2018
- Full Text
- View/download PDF
19. Piezo1 Regulation Involves Lipid Domains and the Cytoskeleton and Is Favored by the Stomatocyte-Discocyte-Echinocyte Transformation.
- Author
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Stommen A, Ghodsi M, Cloos AS, Conrard L, Dumitru AC, Henriet P, Pierreux CE, Alsteens D, and Tyteca D
- Subjects
- Humans, Cholesterol, Erythrocytes, G(M1) Ganglioside, Lipid Bilayers chemistry, Lipid Bilayers metabolism, Cytoskeleton, Microtubules, Ion Channels metabolism
- Abstract
Piezo1 is a mechanosensitive ion channel required for various biological processes, but its regulation remains poorly understood. Here, we used erythrocytes to address this question since they display Piezo1 clusters, a strong and dynamic cytoskeleton and three types of submicrometric lipid domains, respectively enriched in cholesterol, GM1 ganglioside/cholesterol and sphingomyelin/cholesterol. We revealed that Piezo1 clusters were present in both the rim and the dimple erythrocyte regions. Upon Piezo1 chemical activation by Yoda1, the Piezo1 cluster proportion mainly increased in the dimple area. This increase was accompanied by Ca
2+ influx and a rise in echinocytes, in GM1/cholesterol-enriched domains in the dimple and in cholesterol-enriched domains in the rim. Conversely, the effects of Piezo1 activation were abrogated upon membrane cholesterol depletion. Furthermore, upon Piezo1-independent Ca2+ influx, the above changes were not observed. In healthy donors with a high echinocyte proportion, Ca2+ influx, lipid domains and Piezo1 fluorescence were high even at resting state, whereas the cytoskeleton membrane occupancy was lower. Accordingly, upon decreases in cytoskeleton membrane occupancy and stiffness in erythrocytes from patients with hereditary spherocytosis, Piezo1 fluorescence was increased. Altogether, we showed that Piezo1 was differentially controlled by lipid domains and the cytoskeleton and was favored by the stomatocyte-discocyte-echinocyte transformation.- Published
- 2023
- Full Text
- View/download PDF
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