User menu

Accès à distance ? S'identifier sur le proxy UCLouvain

Plasma Membrane Lipid Domains as Platforms for Vesicle Biogenesis and Shedding?

Primary tabs

download
  • Open access
  • PDF
  • 2.72 M
Pollet, Hélène [UCL] Conrard, Louise [UCL] Cloos, Anne-Sophie [UCL] Tyteca, Donatienne [UCL]

Extracellular vesicles (EVs) contribute to several pathophysiological processes and appear as emerging targets for disease diagnosis and therapy. However, successful translation from bench to bedside requires deeper understanding of EVs, in particular their diversity, composition, biogenesis and shedding mechanisms. In this review, we focus on plasma membrane-derived microvesicles (MVs), far less appreciated than exosomes. We integrate documented mechanisms involved in MV biogenesis and shedding, focusing on the red blood cell as a model. We then provide a perspective for the relevance of plasma membrane lipid composition and biophysical properties in microvesiculation on red blood cells but also platelets, immune and nervous cells as well as tumor cells. Although only a few data are available in this respect, most of them appear to converge to the idea that modulation of plasma membrane lipid content, transversal asymmetry and lateral heterogeneity in lipid domains may play a significant role in the vesiculation process. We suggest that lipid domains may represent platforms for inclusion/exclusion of membrane lipids and proteins into MVs and that MVs could originate from distinct domains during physiological processes and disease evolution.

Document type Article de périodique (Journal article) – Synthèse de littérature
Access type Accès libre
Publication date 2018
Language Anglais
Journal information "Biomolecules" - Vol. 8, no.3, p. 94 [1-38] (2018)
Peer reviewed yes
Publisher MDPI AG ((Switzerland) Basel)
e-issn 2218-273X
Publication status Publié
Affiliation UCL - SSS/DDUV/CELL - Biologie cellulaire
Keywords calcium ; ceramide ; cholesterol ; cytoskeleton ; lipid domains ; microvesicle ; oxidative stress ; raft ; red blood cell ; sphingomyelinase
Links
  1. Deatherage Brooke L., Cookson Brad T., Membrane Vesicle Release in Bacteria, Eukaryotes, and Archaea: a Conserved yet Underappreciated Aspect of Microbial Life, 10.1128/iai.06014-11
  2. Robinson David G., Ding Yu, Jiang Liwen, Unconventional protein secretion in plants: a critical assessment, 10.1007/s00709-015-0887-1
  3. Gould Stephen J., Raposo Graça, As we wait: coping with an imperfect nomenclature for extracellular vesicles, 10.3402/jev.v2i0.20389
  4. Raposo Graça, Stoorvogel Willem, Extracellular vesicles: Exosomes, microvesicles, and friends, 10.1083/jcb.201211138
  5. György Bence, Szabó Tamás G., Pásztói Mária, Pál Zsuzsanna, Misják Petra, Aradi Borbála, László Valéria, Pállinger Éva, Pap Erna, Kittel Ágnes, Nagy György, Falus András, Buzás Edit I., Membrane vesicles, current state-of-the-art: emerging role of extracellular vesicles, 10.1007/s00018-011-0689-3
  6. Sedgwick Alanna E., D'Souza-Schorey Crislyn, The biology of extracellular microvesicles, 10.1111/tra.12558
  7. Turturici Giuseppina, Tinnirello Rosaria, Sconzo Gabriella, Geraci Fabiana, Extracellular membrane vesicles as a mechanism of cell-to-cell communication: advantages and disadvantages, 10.1152/ajpcell.00228.2013
  8. Kowal Joanna, Arras Guillaume, Colombo Marina, Jouve Mabel, Morath Jakob Paul, Primdal-Bengtson Bjarke, Dingli Florent, Loew Damarys, Tkach Mercedes, Théry Clotilde, Proteomic comparison defines novel markers to characterize heterogeneous populations of extracellular vesicle subtypes, 10.1073/pnas.1521230113
  9. Booth Amy M., Fang Yi, Fallon Jonathan K., Yang Jr-Ming, Hildreth James E.K., Gould Stephen J., Exosomes and HIV Gag bud from endosome-like domains of the T cell plasma membrane, 10.1083/jcb.200508014
  10. Marzesco A.-M., Release of extracellular membrane particles carrying the stem cell marker prominin-1 (CD133) from neural progenitors and other epithelial cells, 10.1242/jcs.02439
  11. Nabhan J. F., Hu R., Oh R. S., Cohen S. N., Lu Q., Formation and release of arrestin domain-containing protein 1-mediated microvesicles (ARMMs) at plasma membrane by recruitment of TSG101 protein, 10.1073/pnas.1200448109
  12. Ciana Annarita, Achilli Cesare, Gaur Anjali, Minetti Giampaolo, Membrane Remodelling and Vesicle Formation During Ageing of Human Red Blood Cells, 10.1159/000478768
  13. Yuana Yuana, Sturk Auguste, Nieuwland Rienk, Extracellular vesicles in physiological and pathological conditions, 10.1016/j.blre.2012.12.002
  14. Gupta Archana, Pulliam Lynn, Exosomes as mediators of neuroinflammation, 10.1186/1742-2094-11-68
  15. Shen Beiyi, Fang Yi, Wu Ning, Gould Stephen J., Biogenesis of the Posterior Pole Is Mediated by the Exosome/Microvesicle Protein-sorting Pathway, 10.1074/jbc.m111.274803
  16. Muralidharan-Chari V., Clancy J. W., Sedgwick A., D'Souza-Schorey C., Microvesicles: mediators of extracellular communication during cancer progression, 10.1242/jcs.064386
  17. Barteneva Natasha S., Maltsev Natalia, Vorobjev Ivan A., Microvesicles and intercellular communication in the context of parasitism, 10.3389/fcimb.2013.00049
  18. Wu Kerui, Xing Fei, Wu Shih-Ying, Watabe Kounosuke, Extracellular vesicles as emerging targets in cancer: Recent development from bench to bedside, 10.1016/j.bbcan.2017.10.001
  19. Lutz Hans U., Bogdanova Anna, Mechanisms tagging senescent red blood cells for clearance in healthy humans, 10.3389/fphys.2013.00387
  20. Antonelou, Blood Transfus., 8, S39 (2010)
  21. Leal Joames K. F., Adjobo-Hermans Merel J. W., Bosman Giel J. C. G. M., Red Blood Cell Homeostasis: Mechanisms and Effects of Microvesicle Generation in Health and Disease, 10.3389/fphys.2018.00703
  22. Antonelou Marianna H., Seghatchian Jerard, Update on extracellular vesicles inside red blood cell storage units: Adjust the sails closer to the new wind, 10.1016/j.transci.2016.07.016
  23. Willekens Frans L. A., Werre Jan M., Groenen-Döpp Yvonne A. M., Roerdinkholder-Stoelwinder Bregt, de Pauw Ben, Bosman Giel J. C. G. M., Erythrocyte vesiculation: a self-protective mechanism?, 10.1111/j.1365-2141.2008.07055.x
  24. Stewart Andrew, Urbaniak Stan, Turner Marc, Bessos Hagop, The application of a new quantitative assay for the monitoring of integrin-associated protein CD47 on red blood cells during storage and comparison with the expression of CD47 and phosphatidylserine with flow cytometry, 10.1111/j.1537-2995.2005.00564.x
  25. Bocci Velio, Pessina G.Paolo, Paulesu Luana, Studies of factors regulating the ageing of human erythrocytes—III. Metabolism and fate of erythrocytic vesicles, 10.1016/0020-711x(80)90246-3
  26. Jank Herbert, Salzer Ulrich, Vesicles Generated during Storage of Red Blood Cells Enhance the Generation of Radical Oxygen Speciesin Activated Neutrophils, 10.1100/tsw.2011.25
  27. Donadee Chenell, Raat Nicolaas J.H., Kanias Tamir, Tejero Jesús, Lee Janet S., Kelley Eric E., Zhao Xuejun, Liu Chen, Reynolds Hannah, Azarov Ivan, Frizzell Sheila, Meyer E. Michael, Donnenberg Albert D., Qu Lirong, Triulzi Darrel, Kim-Shapiro Daniel B., Gladwin Mark T., Nitric Oxide Scavenging by Red Blood Cell Microparticles and Cell-Free Hemoglobin as a Mechanism for the Red Cell Storage Lesion, 10.1161/circulationaha.110.008698
  28. Kriebardis, Blood Transfus., 10, S25 (2012)
  29. Burnouf Thierry, Chou Ming-Li, Goubran Hadi, Cognasse Fabrice, Garraud Olivier, Seghatchian Jerard, An overview of the role of microparticles/microvesicles in blood components: Are they clinically beneficial or harmful?, 10.1016/j.transci.2015.10.010
  30. Arraud N., Linares R., Tan S., Gounou C., Pasquet J.-M., Mornet S., Brisson A. R., Extracellular vesicles from blood plasma: determination of their morphology, size, phenotype and concentration, 10.1111/jth.12554
  31. Zwaal Robert F.A, Comfurius Paul, Bevers Edouard M, Scott syndrome, a bleeding disorder caused by defective scrambling of membrane phospholipids, 10.1016/j.bbalip.2003.07.003
  32. Tao Shi-Cong, Guo Shang-Chun, Zhang Chang-Qing, Platelet-derived Extracellular Vesicles: An Emerging Therapeutic Approach, 10.7150/ijbs.19776
  33. Vajen Tanja, Benedikter Birke J., Heinzmann Alexandra C. A., Vasina Elena M., Henskens Yvonne, Parsons Martin, Maguire Patricia B., Stassen Frank R., Heemskerk Johan W. M., Schurgers Leon J., Koenen Rory R., Platelet extracellular vesicles induce a pro-inflammatory smooth muscle cell phenotype, 10.1080/20013078.2017.1322454
  34. Sprague D. L., Elzey B. D., Crist S. A., Waldschmidt T. J., Jensen R. J., Ratliff T. L., Platelet-mediated modulation of adaptive immunity: unique delivery of CD154 signal by platelet-derived membrane vesicles, 10.1182/blood-2007-06-097410
  35. Edelstein Leonard C., The role of platelet microvesicles in intercellular communication, 10.1080/09537104.2016.1257114
  36. Johnson Bobby L., III, Kuethe Josh W., Caldwell Charles C., Neutrophil Derived Microvesicles: Emerging Role of a Key Mediator to the Immune Response, 10.2174/1871530314666140722083717
  37. Halim Ahmad Tarmizi Abdul, Ariffin Nur Azrah Fazera Mohd, Azlan Maryam, Review: the Multiple Roles of Monocytic Microparticles, 10.1007/s10753-016-0381-8
  38. Angelillo-Scherrer Anne, Leukocyte-Derived Microparticles in Vascular Homeostasis, 10.1161/circresaha.110.233403
  39. del Conde I., Tissue-factor-bearing microvesicles arise from lipid rafts and fuse with activated platelets to initiate coagulation, 10.1182/blood-2004-03-1095
  40. Budnik Vivian, Ruiz-Cañada Catalina, Wendler Franz, Extracellular vesicles round off communication in the nervous system, 10.1038/nrn.2015.29
  41. Paolicelli Rosa C., Bergamini Giorgio, Rajendran Lawrence, Cell-to-cell Communication by Extracellular Vesicles: Focus on Microglia, 10.1016/j.neuroscience.2018.04.003
  42. Bianco F., Pravettoni E., Colombo A., Schenk U., Moller T., Matteoli M., Verderio C., Astrocyte-Derived ATP Induces Vesicle Shedding and IL-1  Release from Microglia, 10.4049/jimmunol.174.11.7268
  43. Joshi P, Turola E, Ruiz A, Bergami A, Libera D D, Benussi L, Giussani P, Magnani G, Comi G, Legname G, Ghidoni R, Furlan R, Matteoli M, Verderio C, Microglia convert aggregated amyloid-β into neurotoxic forms through the shedding of microvesicles, 10.1038/cdd.2013.180
  44. Carandini Tiziana, Colombo Federico, Finardi Annamaria, Casella Giacomo, Garzetti Livia, Verderio Claudia, Furlan Roberto, Microvesicles: What is the Role in Multiple Sclerosis?, 10.3389/fneur.2015.00111
  45. Minagar Alireza, Alexander J Steven, Blood-brain barrier disruption in multiple sclerosis, 10.1191/1352458503ms965oa
  46. Raimondo Stefania, Corrado Chiara, Raimondi Lavinia, De Leo Giacomo, Alessandro Riccardo, Role of Extracellular Vesicles in Hematological Malignancies, 10.1155/2015/821613
  47. Gopal S. K., Greening D. W., Rai A., Chen M., Xu R., Shafiq A., Mathias R. A., Zhu H.-J., Simpson R. J., Extracellular vesicles: their role in cancer biology and epithelial-mesenchymal transition, 10.1042/bcj20160006
  48. Coumans Frank A.W., Brisson Alain R., Buzas Edit I., Dignat-George Françoise, Drees Esther E.E., El-Andaloussi Samir, Emanueli Costanza, Gasecka Aleksandra, Hendrix An, Hill Andrew F., Lacroix Romaric, Lee Yi, van Leeuwen Ton G., Mackman Nigel, Mäger Imre, Nolan John P., van der Pol Edwin, Pegtel D. Michiel, Sahoo Susmita, Siljander Pia R.M., Sturk Guus, de Wever Olivier, Nieuwland Rienk, Methodological Guidelines to Study Extracellular Vesicles, 10.1161/circresaha.117.309417
  49. Menck Kerstin, Bleckmann Annalen, Schulz Matthias, Ries Lena, Binder Claudia, Isolation and Characterization of Microvesicles from Peripheral Blood, 10.3791/55057
  50. Konoshenko Maria Yu., Lekchnov Evgeniy A., Vlassov Alexander V., Laktionov Pavel P., Isolation of Extracellular Vesicles: General Methodologies and Latest Trends, 10.1155/2018/8545347
  51. Ramirez Marcel I., Amorim Maria G., Gadelha Catarina, Milic Ivana, Welsh Joshua A., Freitas Vanessa M., Nawaz Muhammad, Akbar Naveed, Couch Yvonne, Makin Laura, Cooke Fiona, Vettore Andre L., Batista Patricia X., Freezor Roberta, Pezuk Julia A., Rosa-Fernandes Lívia, Carreira Ana Claudia O., Devitt Andrew, Jacobs Laura, Silva Israel T., Coakley Gillian, Nunes Diana N., Carter Dave, Palmisano Giuseppe, Dias-Neto Emmanuel, Technical challenges of working with extracellular vesicles, 10.1039/c7nr08360b
  52. Mateescu Bogdan, Kowal Emma J. K., van Balkom Bas W. M., Bartel Sabine, Bhattacharyya Suvendra N., Buzás Edit I., Buck Amy H., de Candia Paola, Chow Franklin W. N., Das Saumya, Driedonks Tom A. P., Fernández-Messina Lola, Haderk Franziska, Hill Andrew F., Jones Jennifer C., Van Keuren-Jensen Kendall R., Lai Charles P., Lässer Cecilia, di Liegro Italia, Lunavat Taral R., Lorenowicz Magdalena J., Maas Sybren L. N., Mäger Imre, Mittelbrunn Maria, Momma Stefan, Mukherjee Kamalika, Nawaz Muhammad, Pegtel D. Michiel, Pfaffl Michael W., Schiffelers Raymond M., Tahara Hidetoshi, Théry Clotilde, Tosar Juan Pablo, Wauben Marca H. M., Witwer Kenneth W., Nolte-‘t Hoen Esther N. M., Obstacles and opportunities in the functional analysis of extracellular vesicle RNA – an ISEV position paper, 10.1080/20013078.2017.1286095
  53. Szatanek Rafal, Baj-Krzyworzeka Monika, Zimoch Jakub, Lekka Malgorzata, Siedlar Maciej, Baran Jarek, The Methods of Choice for Extracellular Vesicles (EVs) Characterization, 10.3390/ijms18061153
  54. Aharon Anat, Brenner Benjamin, Microparticles and pregnancy complications, 10.1016/s0049-3848(11)70019-6
  55. Wilhelm Eurico N., Mourot Laurent, Rakobowchuk Mark, Exercise-Derived Microvesicles: A Review of the Literature, 10.1007/s40279-018-0943-z
  56. Strohacker Kelley, Breslin Whitney L., Carpenter Katie C., Davidson Tiffany R., Agha Nadia H., McFarlin Brian K., Moderate-intensity, premeal cycling blunts postprandial increases in monocyte cell surface CD18 and CD11a and endothelial microparticles following a high-fat meal in young adults, 10.1139/h2012-034
  57. Alijotas-Reig Jaume, Palacio-Garcia Carles, Llurba Elisa, Vilardell-Tarres Miquel, Cell-derived microparticles and vascular pregnancy complications: a systematic and comprehensive review, 10.1016/j.fertnstert.2012.10.009
  58. Gustafson Callie M, Shepherd Alex J, Miller Virginia M, Jayachandran Muthuvel, Age- and sex-specific differences in blood-borne microvesicles from apparently healthy humans, 10.1186/s13293-015-0028-8
  59. BERNIMOULIN M., WATERS E. K., FOY M., STEELE B. M., SULLIVAN M., FALET H., WALSH M. T., BARTENEVA N., GENG J.-G., HARTWIG J. H., MAGUIRE P. B., WAGNER D. D., Differential stimulation of monocytic cells results in distinct populations of microparticles, 10.1111/j.1538-7836.2009.03434.x
  60. Kalra Hina, Simpson Richard J., Ji Hong, Aikawa Elena, Altevogt Peter, Askenase Philip, Bond Vincent C., Borràs Francesc E., Breakefield Xandra, Budnik Vivian, Buzas Edit, Camussi Giovanni, Clayton Aled, Cocucci Emanuele, Falcon-Perez Juan M., Gabrielsson Susanne, Gho Yong Song, Gupta Dwijendra, Harsha H. C., Hendrix An, Hill Andrew F., Inal Jameel M., Jenster Guido, Krämer-Albers Eva-Maria, Lim Sai Kiang, Llorente Alicia, Lötvall Jan, Marcilla Antonio, Mincheva-Nilsson Lucia, Nazarenko Irina, Nieuwland Rienk, Nolte-'t Hoen Esther N. M., Pandey Akhilesh, Patel Tushar, Piper Melissa G., Pluchino Stefano, Prasad T. S. Keshava, Rajendran Lawrence, Raposo Graca, Record Michel, Reid Gavin E., Sánchez-Madrid Francisco, Schiffelers Raymond M., Siljander Pia, Stensballe Allan, Stoorvogel Willem, Taylor Douglas, Thery Clotilde, Valadi Hadi, van Balkom Bas W. M., Vázquez Jesús, Vidal Michel, Wauben Marca H. M., Yáñez-Mó María, Zoeller Margot, Mathivanan Suresh, Vesiclepedia: A Compendium for Extracellular Vesicles with Continuous Community Annotation, 10.1371/journal.pbio.1001450
  61. Kim Dae-Kyum, Kang Byeongsoo, Kim Oh Youn, Choi Dong-sic, Lee Jaewook, Kim Sae Rom, Go Gyeongyun, Yoon Yae Jin, Kim Ji Hyun, Jang Su Chul, Park Kyong-Su, Choi Eun-Jeong, Kim Kwang Pyo, Desiderio Dominic M., Kim Yoon-Keun, Lötvall Jan, Hwang Daehee, Gho Yong Song, EVpedia: an integrated database of high-throughput data for systemic analyses of extracellular vesicles, 10.3402/jev.v2i0.20384
  62. Muralidharan-Chari Vandhana, Clancy James, Plou Carolyn, Romao Maryse, Chavrier Philippe, Raposo Graca, D'Souza-Schorey Crislyn, ARF6-Regulated Shedding of Tumor Cell-Derived Plasma Membrane Microvesicles, 10.1016/j.cub.2009.09.059
  63. Keerthikumar Shivakumar, Gangoda Lahiru, Liem Michael, Fonseka Pamali, Atukorala Ishara, Ozcitti Cemil, Mechler Adam, Adda Christopher G., Ang Ching-Seng, Mathivanan Suresh, Proteogenomic analysis reveals exosomes are more oncogenic than ectosomes, 10.18632/oncotarget.3801
  64. Gasser Olivier, Hess Christoph, Miot Sylvie, Deon Catherine, Sanchez Jean-Charles, Schifferli J.ürg A, Characterisation and properties of ectosomes released by human polymorphonuclear neutrophils, 10.1016/s0014-4827(03)00055-7
  65. Kriebardis Anastasios G., Antonelou Marianna H., Stamoulis Konstantinos E., Economou-Petersen Effrosini, Margaritis Lukas H., Papassideri Issidora S., RBC-derived vesicles during storage: ultrastructure, protein composition, oxidation, and signaling components, 10.1111/j.1537-2995.2008.01794.x
  66. Salzer Ulrich, Zhu Rong, Luten Marleen, Isobe Hirotaka, Pastushenko Vassili, Perkmann Thomas, Hinterdorfer Peter, Bosman Giel J.C.G.M., Vesicles generated during storage of red cells are rich in the lipid raft marker stomatin, 10.1111/j.1537-2995.2007.01549.x
  67. Salzer U., Ca++-dependent vesicle release from erythrocytes involves stomatin-specific lipid rafts, synexin (annexin VII), and sorcin, 10.1182/blood.v99.7.2569
  68. Di Vizio Dolores, Morello Matteo, Dudley Andrew C., Schow Peter W., Adam Rosalyn M., Morley Samantha, Mulholland David, Rotinen Mirja, Hager Martin H., Insabato Luigi, Moses Marsha A., Demichelis Francesca, Lisanti Michael P., Wu Hong, Klagsbrun Michael, Bhowmick Neil A., Rubin Mark A., D'Souza-Schorey Crislyn, Freeman Michael R., Large Oncosomes in Human Prostate Cancer Tissues and in the Circulation of Mice with Metastatic Disease, 10.1016/j.ajpath.2012.07.030
  69. Millimaggi Danilo, Festuccia Claudio, Angelucci Adriano, D'Ascenzo Sandra, Rucci Nadia, Flati Silvio, Bologna Mauro, Teti Anna, Pavan Antonio, Dolo Vincenza, Osteoblast-conditioned media stimulate membrane vesicle shedding in prostate cancer cells, 10.3892/ijo.28.4.909
  70. Taraboletti Giulia, D'Ascenzo Sandra, Borsotti Patrizia, Giavazzi Raffaella, Pavan Antonio, Dolo Vincenza, Shedding of the Matrix Metalloproteinases MMP-2, MMP-9, and MT1-MMP as Membrane Vesicle-Associated Components by Endothelial Cells, 10.1016/s0002-9440(10)64887-0
  71. Shimoda Masayuki, Khokha Rama, Metalloproteinases in extracellular vesicles, 10.1016/j.bbamcr.2017.05.027
  72. Dolo, Cancer Res., 58, 4468 (1998)
  73. Heijnen, Blood, 94, 3791 (1999)
  74. Pluskota E., Woody N. M., Szpak D., Ballantyne C. M., Soloviev D. A., Simon D. I., Plow E. F., Expression, activation, and function of integrin  M 2 (Mac-1) on neutrophil-derived microparticles, 10.1182/blood-2007-12-127183
  75. Mezouar Soraya, Darbousset Roxane, Dignat-George Françoise, Panicot-Dubois Laurence, Dubois Christophe, Inhibition of platelet activation prevents the P-selectin and integrin-dependent accumulation of cancer cell microparticles and reduces tumor growth and metastasisin vivo : Clopidogrel Reduces Thrombosis and MetastasisIn Vivo, 10.1002/ijc.28997
  76. Deregibus M. C., Cantaluppi V., Calogero R., Lo Iacono M., Tetta C., Biancone L., Bruno S., Bussolati B., Camussi G., Endothelial progenitor cell derived microvesicles activate an angiogenic program in endothelial cells by a horizontal transfer of mRNA, 10.1182/blood-2007-03-078709
  77. Al-Nedawi Khalid, Meehan Brian, Micallef Johann, Lhotak Vladimir, May Linda, Guha Abhijit, Rak Janusz, Intercellular transfer of the oncogenic receptor EGFRvIII by microvesicles derived from tumour cells, 10.1038/ncb1725
  78. Kim Kyoung Mi, Abdelmohsen Kotb, Mustapic Maja, Kapogiannis Dimitrios, Gorospe Myriam, RNA in extracellular vesicles : RNA in extracellular vesicles, 10.1002/wrna.1413
  79. Baj-Krzyworzeka Monika, Szatanek Rafał, Węglarczyk Kazimierz, Baran Jarosław, Urbanowicz Barbara, Brański Piotr, Ratajczak Mariusz Z., Zembala Marek, Tumour-derived microvesicles carry several surface determinants and mRNA of tumour cells and transfer some of these determinants to monocytes, 10.1007/s00262-005-0075-9
  80. Fatima Farah, Nawaz Muhammad, Vesiculated Long Non-Coding RNAs: Offshore Packages Deciphering Trans-Regulation between Cells, Cancer Progression and Resistance to Therapies, 10.3390/ncrna3010010
  81. Yuan Alex, Farber Erica L., Rapoport Ana Lia, Tejada Desiree, Deniskin Roman, Akhmedov Novrouz B., Farber Debora B., Transfer of MicroRNAs by Embryonic Stem Cell Microvesicles, 10.1371/journal.pone.0004722
  82. Fonsato Valentina, Collino Federica, Herrera Maria Beatriz, Cavallari Claudia, Deregibus Maria Chiara, Cisterna Barbara, Bruno Stefania, Romagnoli Renato, Salizzoni Mauro, Tetta Ciro, Camussi Giovanni, Human Liver Stem Cell-Derived Microvesicles Inhibit Hepatoma Growth in SCID Mice by Delivering Antitumor MicroRNAs, 10.1002/stem.1161
  83. Crescitelli Rossella, Lässer Cecilia, Szabó Tamas G., Kittel Agnes, Eldh Maria, Dianzani Irma, Buzás Edit I., Lötvall Jan, Distinct RNA profiles in subpopulations of extracellular vesicles: apoptotic bodies, microvesicles and exosomes, 10.3402/jev.v2i0.20677
  84. Dong L., Lin W., Qi P., Xu M.-d., Wu X., Ni S., Huang D., Weng W.-w., Tan C., Sheng W., Zhou X., Du X., Circulating Long RNAs in Serum Extracellular Vesicles: Their Characterization and Potential Application as Biomarkers for Diagnosis of Colorectal Cancer, 10.1158/1055-9965.epi-16-0006
  85. Kawamura Yumi, Yamamoto Yusuke, Sato Taka-Aki, Ochiya Takahiro, Extracellular vesicles as trans-genomic agents: Emerging roles in disease and evolution, 10.1111/cas.13222
  86. Kanada Masamitsu, Bachmann Michael H., Hardy Jonathan W., Frimannson Daniel Omar, Bronsart Laura, Wang Andrew, Sylvester Matthew D., Schmidt Tobi L., Kaspar Roger L., Butte Manish J., Matin A. C., Contag Christopher H., Differential fates of biomolecules delivered to target cells via extracellular vesicles, 10.1073/pnas.1418401112
  87. Osteikoetxea Xabier, Balogh Andrea, Szabó-Taylor Katalin, Németh Andrea, Szabó Tamás Géza, Pálóczi Krisztina, Sódar Barbara, Kittel Ágnes, György Bence, Pállinger Éva, Matkó János, Buzás Edit Irén, Improved Characterization of EV Preparations Based on Protein to Lipid Ratio and Lipid Properties, 10.1371/journal.pone.0121184
  88. Haraszti Reka A., Didiot Marie-Cecile, Sapp Ellen, Leszyk John, Shaffer Scott A., Rockwell Hannah E., Gao Fei, Narain Niven R., DiFiglia Marian, Kiebish Michael A., Aronin Neil, Khvorova Anastasia, High-resolution proteomic and lipidomic analysis of exosomes and microvesicles from different cell sources, 10.3402/jev.v5.32570
  89. Baig S., Lim J.Y., Fernandis A.Z., Wenk M.R., Kale A., Su L.L., Biswas A., Vasoo S., Shui G., Choolani M., Lipidomic analysis of human placental Syncytiotrophoblast microvesicles in adverse pregnancy outcomes, 10.1016/j.placenta.2013.02.004
  90. Weerheim A.M., Kolb A.M., Sturk A., Nieuwland R., Phospholipid Composition of Cell-Derived Microparticles Determined by One-Dimensional High-Performance Thin-Layer Chromatography, 10.1006/abio.2001.5552
  91. Bicalho Beatriz, Holovati, Jelena L., Acker Jason P., Phospholipidomics reveals differences in glycerophosphoserine profiles of hypothermically stored red blood cells and microvesicles, 10.1016/j.bbamem.2012.10.026
  92. Laurén Eva, Tigistu-Sahle Feven, Valkonen Sami, Westberg Melissa, Valkeajärvi Anne, Eronen Juha, Siljander Pia, Pettilä Ville, Käkelä Reijo, Laitinen Saara, Kerkelä Erja, Phospholipid composition of packed red blood cells and that of extracellular vesicles show a high resemblance and stability during storage, 10.1016/j.bbalip.2017.09.012
  93. Lutz H., Release of spectrin-free vesicles from human erythrocytes during ATP depletion: 1. characterization of spectrin-free vesicles, 10.1083/jcb.73.3.548
  94. Hu Qianghua, Wang Miao, Cho Min Soon, Wang Chunyan, Nick Alpa M., Thiagarajan Perumal, Aung Fleur M., Han Xianlin, Sood Anil K., Afshar-Kharghan Vahid, Lipid profile of platelets and platelet-derived microparticles in ovarian cancer, 10.1016/j.bbacli.2016.06.003
  95. BIRO E., AKKERMAN J. W. N., HOEK F. J., GORTER G., PRONK L. M., STURK A., NIEUWLAND R., The phospholipid composition and cholesterol content of platelet-derived microparticles: a comparison with platelet membrane fractions, 10.1111/j.1538-7836.2005.01646.x
  96. Exner Thomas, Ma David Dang Fung, Joseph Joanne Emily, Connor David Ewan, The majority of circulating platelet-derived microparticles fail to bind annexin V, lack phospholipid-dependent procoagulant activity and demonstrate greater expression of glycoprotein Ib, 10.1160/th09-09-0644
  97. Cluitmans Judith C. A., Gevi Federica, Siciliano Angela, Matte Alessandro, Leal Joames K. F., De Franceschi Lucia, Zolla Lello, Brock Roland, Adjobo-Hermans Merel J. W., Bosman Giel J. G. C. M., Red Blood Cell Homeostasis: Pharmacological Interventions to Explore Biochemical, Morphological and Mechanical Properties, 10.3389/fmolb.2016.00010
  98. Dinkla S, Wessels K, Verdurmen W P R, Tomelleri C, Cluitmans J C A, Fransen J, Fuchs B, Schiller J, Joosten I, Brock R, Bosman G J C G M, Functional consequences of sphingomyelinase-induced changes in erythrocyte membrane structure, 10.1038/cddis.2012.143
  99. Boilard Eric, Extracellular vesicles and their content in bioactive lipid mediators: more than a sack of microRNA, 10.1194/jlr.r084640
  100. Rousseau Matthieu, Belleannee Clemence, Duchez Anne-Claire, Cloutier Nathalie, Levesque Tania, Jacques Frederic, Perron Jean, Nigrovic Peter A., Dieude Melanie, Hebert Marie-Josee, Gelb Michael H., Boilard Eric, Detection and Quantification of Microparticles from Different Cellular Lineages Using Flow Cytometry. Evaluation of the Impact of Secreted Phospholipase A2 on Microparticle Assessment, 10.1371/journal.pone.0116812
  101. Duchez Anne-Claire, Boudreau Luc H., Naika Gajendra S., Bollinger James, Belleannée Clémence, Cloutier Nathalie, Laffont Benoit, Mendoza-Villarroel Raifish E., Lévesque Tania, Rollet-Labelle Emmanuelle, Rousseau Matthieu, Allaeys Isabelle, Tremblay Jacques J., Poubelle Patrice E., Lambeau Gérard, Pouliot Marc, Provost Patrick, Soulet Denis, Gelb Michael H., Boilard Eric, Platelet microparticles are internalized in neutrophils via the concerted activity of 12-lipoxygenase and secreted phospholipase A2-IIA, 10.1073/pnas.1507905112
  102. Lux S. E., Anatomy of the red cell membrane skeleton: unanswered questions, 10.1182/blood-2014-12-512772
  103. Manno Sumie, Takakuwa Yuichi, Mohandas Narla, Modulation of Erythrocyte Membrane Mechanical Function by Protein 4.1 Phosphorylation, 10.1074/jbc.m410650200
  104. Picas Laura, Rico Félix, Deforet Maxime, Scheuring Simon, Structural and Mechanical Heterogeneity of the Erythrocyte Membrane Reveals Hallmarks of Membrane Stability, 10.1021/nn303824j
  105. Muravyov, Clin. Hemorheol. Microcirc., 53, 45 (2013)
  106. An Xiuli, Zhang Xihui, Debnath Gargi, Baines Anthony J., Mohandas Narla, Phosphatidylinositol-4,5-Biphosphate (PIP2) Differentially Regulates the Interaction of Human Erythrocyte Protein 4.1 (4.1R) with Membrane Proteins†, 10.1021/bi060015v
  107. Kapus, Compr. Physiol., 3, 1231 (2013)
  108. Bogdanova Anna, Makhro Asya, Wang Jue, Lipp Peter, Kaestner Lars, Calcium in Red Blood Cells—A Perilous Balance, 10.3390/ijms14059848
  109. Huisjes Rick, Bogdanova Anna, van Solinge Wouter W., Schiffelers Raymond M., Kaestner Lars, van Wijk Richard, Squeezing for Life – Properties of Red Blood Cell Deformability, 10.3389/fphys.2018.00656
  110. Evans E, Mohandas N, Leung A, Static and dynamic rigidities of normal and sickle erythrocytes. Major influence of cell hemoglobin concentration., 10.1172/jci111234
  111. Lew Virgilio L., Tiffert Teresa, On the Mechanism of Human Red Blood Cell Longevity: Roles of Calcium, the Sodium Pump, PIEZO1, and Gardos Channels, 10.3389/fphys.2017.00977
  112. Betz T., Lenz M., Joanny J.-F., Sykes C., ATP-dependent mechanics of red blood cells, 10.1073/pnas.0904614106
  113. Park Y., Best C. A., Auth T., Gov N. S., Safran S. A., Popescu G., Suresh S., Feld M. S., Metabolic remodeling of the human red blood cell membrane, 10.1073/pnas.0910785107
  114. Yoon Young-Zoon, Kotar Jurij, Yoon Gilwon, Cicuta Pietro, The nonlinear mechanical response of the red blood cell, 10.1088/1478-3975/5/3/036007
  115. Rifkind Joseph M., Nagababu Enika, Hemoglobin Redox Reactions and Red Blood Cell Aging, 10.1089/ars.2012.4867
  116. Rubin O., Crettaz D., Canellini G., Tissot J.-D., Lion N., Microparticles in stored red blood cells: an approach using flow cytometry and proteomic tools, 10.1111/j.1423-0410.2008.01101.x
  117. Kriebardis Anastasios G., Antonelou Marianna H., Stamoulis Konstantinos E., Economou-Petersen Effrosini, Margaritis Lukas H., Papassideri Issidora S., Storage-dependent remodeling of the red blood cell membrane is associated with increased immunoglobulin G binding, lipid raft rearrangement, and caspase activation : RBC MEMBRANE REMODELING IN STORAGE, 10.1111/j.1537-2995.2007.01254.x
  118. Bosman G.J.C.G.M., Lasonder E., Groenen-Döpp Y.A.M., Willekens F.L.A., Werre J.M., Novotný V.M.J., Comparative proteomics of erythrocyte aging in vivo and in vitro, 10.1016/j.jprot.2009.07.010
  119. Zhu Qiang, Salehyar Sara, Cabrales Pedro, Asaro Robert J., Prospects for Human Erythrocyte Skeleton-Bilayer Dissociation during Splenic Flow, 10.1016/j.bpj.2017.05.052
  120. Fricke K., Sackmann E., Variation of frequency spectrum of the erythrocyte flickering caused by aging, osmolarity, temperature and pathological changes, 10.1016/0167-4889(84)90004-1
  121. Gov N.S., Safran S.A., Red Blood Cell Membrane Fluctuations and Shape Controlled by ATP-Induced Cytoskeletal Defects, 10.1529/biophysj.104.045328
  122. Edwards Christopher L., Scales Mischca T., Loughlin Charles, Bennett Gary G., Harris-Peterson Shani, Castro Laura M. De, Whitworth Elaine, Abrams Mary, Feliu Miriam, Johnson Stephanie, Wood Mary, Harrison Ojinga, Killough Alvin, A brief review of the pathophysiology, associated pain, and psychosocial issues in sickle cell disease, 10.1207/s15327558ijbm1203_6
  123. Bartosz Grzegorz, Gaczyńska Maria, Grzelińska Ewa, Soszyński Mirosklaw, Michalak Wklodzimierz, Gondko Roman, Aged erythrocytes exhibit decreased anion exchange, 10.1016/0047-6374(87)90064-9
  124. Bartosz G., Tannert Ch., Fried R., Leyko W., Superoxide dismutase activity decreases during erythrocyte aging, 10.1007/bf01932355
  125. Fornaini Giorgio, Magnani Mauro, Fazi Antonio, Accorsi Augusto, Stocchi Vilberto, Dachà Marina, Regulatory properties of human erythrocyte hexokinase during cell ageing, 10.1016/0003-9861(85)90698-8
  126. Azouzi Slim, Romana Marc, Arashiki Nobuto, Takakuwa Yuichi, El Nemer Wassim, Peyrard Thierry, Colin Yves, Amireault Pascal, Le Van Kim Caroline, Band 3 phosphorylation induces irreversible alterations of stored red blood cells, 10.1002/ajh.25044
  127. Szigyártó Imola Cs., Deák Róbert, Mihály Judith, Rocha Sandra, Zsila Ferenc, Varga Zoltán, Beke-Somfai Tamás, Flow Alignment of Extracellular Vesicles: Structure and Orientation of Membrane-Associated Bio-macromolecules Studied with Polarized Light, 10.1002/cbic.201700378
  128. Wither Matthew, Dzieciatkowska Monika, Nemkov Travis, Strop Pavel, D'Alessandro Angelo, Hansen Kirk C., Hemoglobin oxidation at functional amino acid residues during routine storage of red blood cells : Hb OXIDATION IN STORED RBCs AND VESICLES, 10.1111/trf.13363
  129. Arashiki Nobuto, Kimata Naoki, Manno Sumie, Mohandas Narla, Takakuwa Yuichi, Membrane Peroxidation and Methemoglobin Formation Are Both Necessary for Band 3 Clustering: Mechanistic Insights into Human Erythrocyte Senescence, 10.1021/bi400405p
  130. Lutz, J. Immunol., 133, 2610 (1984)
  131. Stowell Sean R., Smith Nicole H., Zimring James C., Fu Xiaoyun, Palmer Andre F., Fontes Jorge, Banerjee Uddyalok, Yazer Mark H., Addition of ascorbic acid solution to stored murine red blood cells increases posttransfusion recovery and decreases microparticles and alloimmunization : Ascorbic Acid Improves Mouse RBC Storage, 10.1111/trf.12106
  132. Freikman Inna, Fibach Eitan, Distribution and shedding of the membrane phosphatidylserine during maturation and aging of erythroid cells, 10.1016/j.bbamem.2011.08.014
  133. Repsold Lisa, Joubert Anna Margaretha, Eryptosis: An Erythrocyte’s Suicidal Type of Cell Death, 10.1155/2018/9405617
  134. Allan D, Thomas P, Limbrick A R, The isolation and characterization of 60 nm vesicles (‘nanovesicles’) produced during ionophore A23187-induced budding of human erythrocytes, 10.1042/bj1880881
  135. Butikofer, Blood, 74, 1481 (1989)
  136. Nguyen Duc Bach, Thuy Ly Thi Bich, Wesseling Mauro Carlos, Hittinger Marius, Torge Afra, Devitt Andrew, Perrie Yvonne, Bernhardt Ingolf, Characterization of Microvesicles Released from Human Red Blood Cells, 10.1159/000443059
  137. Allan D, Michell R H, Calcium ion-dependent diacylglycerol accumulation in erythrocytes is associated with microvesiculation but not with efflux of potassium ions, 10.1042/bj1660495
  138. Nguyen Duc Bach, Wagner-Britz Lisa, Maia Sara, Steffen Patrick, Wagner Christian, Kaestner Lars, Bernhardt Ingolf, Regulation of Phosphatidylserine Exposure in Red Blood Cells, 10.1159/000335798
  139. Morel Olivier, Jesel Laurence, Freyssinet Jean-Marie, Toti Florence, Cellular Mechanisms Underlying the Formation of Circulating Microparticles, 10.1161/atvbaha.109.200956
  140. Westerman Maxwell, Porter John B., Red blood cell-derived microparticles: An overview, 10.1016/j.bcmd.2016.04.003
  141. Rachmilewitz, Blood, 39, 794 (1972)
  142. Ferru E., Pantaleo A., Carta F., Mannu F., Khadjavi A., Gallo V., Ronzoni L., Graziadei G., Cappellini M. D., Turrini F., Thalassemic erythrocytes release microparticles loaded with hemichromes by redox activation of p72Syk kinase, 10.3324/haematol.2013.084533
  143. George A., Pushkaran S., Konstantinidis D. G., Koochaki S., Malik P., Mohandas N., Zheng Y., Joiner C. H., Kalfa T. A., Erythrocyte NADPH oxidase activity modulated by Rac GTPases, PKC, and plasma cytokines contributes to oxidative stress in sickle cell disease, 10.1182/blood-2012-07-441188
  144. Camus S. M., De Moraes J. A., Bonnin P., Abbyad P., Le Jeune S., Lionnet F., Loufrani L., Grimaud L., Lambry J.-C., Charue D., Kiger L., Renard J.-M., Larroque C., Le Clesiau H., Tedgui A., Bruneval P., Barja-Fidalgo C., Alexandrou A., Tharaux P.-L., Boulanger C. M., Blanc-Brude O. P., Circulating cell membrane microparticles transfer heme to endothelial cells and trigger vasoocclusions in sickle cell disease, 10.1182/blood-2014-07-589283
  145. Eber Stefan, Lux Samuel E, Hereditary spherocytosis—defects in proteins that connect the membrane skeleton to the lipid bilayer, 10.1053/j.seminhematol.2004.01.002
  146. Perrotta Silverio, Gallagher Patrick G, Mohandas Narla, Hereditary spherocytosis, 10.1016/s0140-6736(08)61588-3
  147. Diez-Silva Monica, Dao Ming, Han Jongyoon, Lim Chwee-Teck, Suresh Subra, Shape and Biomechanical Characteristics of Human Red Blood Cells in Health and Disease, 10.1557/mrs2010.571
  148. Li He, Lykotrafitis George, Vesiculation of healthy and defective red blood cells, 10.1103/physreve.92.012715
  149. Alaarg Amr, Schiffelers Raymond M., van Solinge Wouter W., van Wijk Richard, Red blood cell vesiculation in hereditary hemolytic anemia, 10.3389/fphys.2013.00365
  150. Reliene, Blood, 100, 2208 (2002)
  151. Peters Luanne L, Shivdasani Ramesh A, Liu Shih-Chun, Hanspal Manjit, John Kathryn M, Gonzalez Jennifer M, Brugnara Carlo, Gwynn Babette, Mohandas Narla, Alper Seth L, Orkin Stuart H, Lux Samuel E, Anion Exchanger 1 (Band 3) Is Required to Prevent Erythrocyte Membrane Surface Loss but Not to Form the Membrane Skeleton, 10.1016/s0092-8674(00)80167-1
  152. Tricarico Christopher, Clancy James, D'Souza-Schorey Crislyn, Biology and biogenesis of shed microvesicles, 10.1080/21541248.2016.1215283
  153. Nawaz Muhammad, Camussi Giovanni, Valadi Hadi, Nazarenko Irina, Ekström Karin, Wang Xiaoqin, Principe Simona, Shah Neelam, Ashraf Naeem M., Fatima Farah, Neder Luciano, Kislinger Thomas, The emerging role of extracellular vesicles as biomarkers for urogenital cancers, 10.1038/nrurol.2014.301
  154. Hugel Bénédicte, Martínez M. Carmen, Kunzelmann Corinne, Freyssinet Jean-Marie, Membrane Microparticles: Two Sides of the Coin, 10.1152/physiol.00029.2004
  155. Muhsin-Sharafaldine Morad-Remy, McLellan Alexander D., Tumor-Derived Apoptotic Vesicles: With Death They Do Part, 10.3389/fimmu.2018.00957
  156. McMahon H. T., Boucrot E., Membrane curvature at a glance, 10.1242/jcs.114454
  157. Yáñez-Mó María, Barreiro Olga, Gordon-Alonso Mónica, Sala-Valdés Mónica, Sánchez-Madrid Francisco, Tetraspanin-enriched microdomains: a functional unit in cell plasma membranes, 10.1016/j.tcb.2009.06.004
  158. Bari Rafijul, Guo Qiusha, Xia Bing, Zhang Yanhui H., Giesert Eldon E., Levy Shoshana, Zheng Jie J., Zhang Xin A., Tetraspanins regulate the protrusive activities of cell membrane, 10.1016/j.bbrc.2011.10.121
  159. Clancy James W., Sedgwick Alanna, Rosse Carine, Muralidharan-Chari Vandhana, Raposo Graca, Method Michael, Chavrier Philippe, D’Souza-Schorey Crislyn, Regulated delivery of molecular cargo to invasive tumour-derived microvesicles, 10.1038/ncomms7919
  160. D'Souza-Schorey Crislyn, Chavrier Philippe, ARF proteins: roles in membrane traffic and beyond, 10.1038/nrm1910
  161. Li B, Antonyak M A, Zhang J, Cerione R A, RhoA triggers a specific signaling pathway that generates transforming microvesicles in cancer cells, 10.1038/onc.2011.636
  162. Wang T., Gilkes D. M., Takano N., Xiang L., Luo W., Bishop C. J., Chaturvedi P., Green J. J., Semenza G. L., Hypoxia-inducible factors and RAB22A mediate formation of microvesicles that stimulate breast cancer invasion and metastasis, 10.1073/pnas.1410041111
  163. Verderio Claudia, Gabrielli Martina, Giussani Paola, Role of sphingolipids in the biogenesis and biological activity of extracellular vesicles, 10.1194/jlr.r083915
  164. Pfrieger Frank W., Vitale Nicolas, Cholesterol and the journey of extracellular vesicles, 10.1194/jlr.r084210
  165. Morad Samy A. F., Cabot Myles C., Ceramide-orchestrated signalling in cancer cells, 10.1038/nrc3398
  166. VELDMAN Robert J., MAESTRE Nicolas, ADUIB Osama M., MEDIN Jeffrey A., SALVAYRE Robert, LEVADE Thierry, A neutral sphingomyelinase resides in sphingolipid-enriched microdomains and is inhibited by the caveolin-scaffolding domain: potential implications in tumour necrosis factor signalling, 10.1042/bj3550859
  167. Menck Kerstin, Sönmezer Can, Worst Thomas Stefan, Schulz Matthias, Dihazi Gry Helene, Streit Frank, Erdmann Gerrit, Kling Simon, Boutros Michael, Binder Claudia, Gross Julia Christina, Neutral sphingomyelinases control extracellular vesicles budding from the plasma membrane, 10.1080/20013078.2017.1378056
  168. Bianco Fabio, Perrotta Cristiana, Novellino Luisa, Francolini Maura, Riganti Loredana, Menna Elisabetta, Saglietti Laura, Schuchman Edward H, Furlan Roberto, Clementi Emilio, Matteoli Michela, Verderio Claudia, Acid sphingomyelinase activity triggers microparticle release from glial cells, 10.1038/emboj.2009.45
  169. Henry Brian, Ziobro Regan, Becker Katrin Anne, Kolesnick Richard, Gulbins Erich, Acid Sphingomyelinase, Sphingolipids: Basic Science and Drug Development (2013) ISBN:9783709113677 p.77-88, 10.1007/978-3-7091-1368-4_4
  170. Xu Ming, Xia Min, Li Xiao-Xue, Han Wei-Qing, Boini Krishna M., Zhang Fan, Zhang Yang, Ritter Joseph K, Li Pin-Lan, Requirement of translocated lysosomal V1 H+-ATPase for activation of membrane acid sphingomyelinase and raft clustering in coronary endothelial cells, 10.1091/mbc.e11-09-0821
  171. Awojoodu A. O., Keegan P. M., Lane A. R., Zhang Y., Lynch K. R., Platt M. O., Botchwey E. A., Acid sphingomyelinase is activated in sickle cell erythrocytes and contributes to inflammatory microparticle generation in SCD, 10.1182/blood-2014-01-543652
  172. Hoehn Richard S., Jernigan Peter L., Japtok Lukasz, Chang Alex L., Midura Emily F., Caldwell Charles C., Kleuser Burkhard, Lentsch Alex B., Edwards Michael J., Gulbins Erich, Pritts Timothy A., Acid Sphingomyelinase Inhibition in Stored Erythrocytes Reduces Transfusion-Associated Lung Inflammation : , 10.1097/sla.0000000000001648
  173. Wang Jue, Pendurthi Usha R., Rao L. Vijaya Mohan, Sphingomyelin encrypts tissue factor: ATP-induced activation of A-SMase leads to tissue factor decryption and microvesicle shedding, 10.1182/bloodadvances.2016003947
  174. López-Montero Iván, Rodriguez Nicolas, Cribier Sophie, Pohl Antje, Vélez Marisela, Devaux Philippe F., Rapid Transbilayer Movement of Ceramides in Phospholipid Vesicles and in Human Erythrocytes, 10.1074/jbc.m412052200
  175. Slotte J. Peter, Hedström Gun, Rannström Stina, Ekman Stig, Effects of sphingomyelin degradation on cell cholesterol oxidizability and steady-state distribution between the cell surface and the cell interior, 10.1016/0005-2736(89)90108-9
  176. Fanani Maria Laura, De Tullio Luisina, Hartel Steffen, Jara Jorge, Maggio Bruno, Sphingomyelinase-Induced Domain Shape Relaxation Driven by Out-of-Equilibrium Changes of Composition, 10.1529/biophysj.108.141499
  177. Castro Bruno M., Prieto Manuel, Silva Liana C., Ceramide: A simple sphingolipid with unique biophysical properties, 10.1016/j.plipres.2014.01.004
  178. Goñi Félix M., Alonso Alicia, Effects of ceramide and other simple sphingolipids on membrane lateral structure, 10.1016/j.bbamem.2008.09.002
  179. White A. B., Givogri M. I., Lopez-Rosas A., Cao H., van Breemen R., Thinakaran G., Bongarzone E. R., Psychosine Accumulates in Membrane Microdomains in the Brain of Krabbe Patients, Disrupting the Raft Architecture, 10.1523/jneurosci.5597-08.2009
  180. D’Auria Ludovic, Reiter Cory, Ward Emma, Moyano Ana Lis, Marshall Michael S., Nguyen Duc, Scesa Giuseppe, Hauck Zane, van Breemen Richard, Givogri Maria I., Bongarzone Ernesto R., Psychosine enhances the shedding of membrane microvesicles: Implications in demyelination in Krabbe’s disease, 10.1371/journal.pone.0178103
  181. Vind-Kezunovic Dina, Nielsen Claus Hélix, Wojewodzka Urszula, Gniadecki Robert, Line tension at lipid phase boundaries regulates formation of membrane vesicles in living cells, 10.1016/j.bbamem.2008.05.015
  182. Liu Ming-Lin, Reilly Michael P., Casasanto Peter, McKenzie Steven E., Williams Kevin Jon, Cholesterol Enrichment of Human Monocyte/Macrophages Induces Surface Exposure of Phosphatidylserine and the Release of Biologically-Active Tissue Factor–Positive Microvesicles, 10.1161/01.atv.0000254674.47693.e8
  183. Carquin Mélanie, D’Auria Ludovic, Pollet Hélène, Bongarzone Ernesto R., Tyteca Donatienne, Recent progress on lipid lateral heterogeneity in plasma membranes: From rafts to submicrometric domains, 10.1016/j.plipres.2015.12.004
  184. Lipowsky Reinhard, Budding of membranes induced by intramembrane domains, 10.1051/jp2:1992238
  185. Baumgart Tobias, Hess Samuel T., Webb Watt W., Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension, 10.1038/nature02013
  186. Yang Sung-Tae, Kiessling Volker, Tamm Lukas K., Line tension at lipid phase boundaries as driving force for HIV fusion peptide-mediated fusion, 10.1038/ncomms11401
  187. Bretscher Mark S., Phosphatidyl-ethanolamine: Differential labelling in intact cells and cell ghosts of human erythrocytes by a membrane-impermeable reagent, 10.1016/s0022-2836(72)80020-2
  188. Yeung Tony, Grinstein Sergio, Lipid signaling and the modulation of surface charge during phagocytosis, 10.1111/j.1600-065x.2007.00546.x
  189. BEVERS Edouard M., COMFURIUS Paul, VAN RIJN Jan L. M. L., HEMKER H. Coenraad, Generation of Prothrombin-Converting Activity and the Exposure of Phosphatidylserine at the Outer Surface of Platelets, 10.1111/j.1432-1033.1982.tb05898.x
  190. Lentz Barry R, Exposure of platelet membrane phosphatidylserine regulates blood coagulation, 10.1016/s0163-7827(03)00025-0
  191. Larson M. C., Karafin M. S., Hillery C. A., Hogg N., Phosphatidylethanolamine is progressively exposed in RBCs during storage : Phosphatidylethanolamine and red cell storage, 10.1111/tme.12382
  192. Nagata S, Suzuki J, Segawa K, Fujii T, Exposure of phosphatidylserine on the cell surface, 10.1038/cdd.2016.7
  193. Stratton Dan, Moore Colin, Zheng Lei, Lange Sigrun, Inal Jameel, Prostate cancer cells stimulated by calcium-mediated activation of protein kinase C undergo a refractory period before re-releasing calcium-bearing microvesicles, 10.1016/j.bbrc.2015.03.061
  194. Tepper Annemiek D., Ruurs Paula, Wiedmer Therese, Sims Peter J., Borst Jannie, van Blitterswijk Wim J., Sphingomyelin Hydrolysis to Ceramide during the Execution Phase of Apoptosis Results from Phospholipid Scrambling and Alters Cell-Surface Morphology, 10.1083/jcb.150.1.155
  195. Simons Kai, Ikonen Elina, Functional rafts in cell membranes, 10.1038/42408
  196. Lingwood D., Simons K., Lipid Rafts As a Membrane-Organizing Principle, 10.1126/science.1174621
  197. Parton Robert G., del Pozo Miguel A., Caveolae as plasma membrane sensors, protectors and organizers, 10.1038/nrm3512
  198. Pike Linda J., Rafts defined: a report on the Keystone symposium on lipid rafts and cell function, 10.1194/jlr.e600002-jlr200
  199. Baumgart T., Hammond A. T., Sengupta P., Hess S. T., Holowka D. A., Baird B. A., Webb W. W., Large-scale fluid/fluid phase separation of proteins and lipids in giant plasma membrane vesicles, 10.1073/pnas.0611357104
  200. Bernardino de la Serna Jorge, Perez-Gil Jesus, Simonsen Adam C., Bagatolli Luis A., Cholesterol Rules : DIRECT OBSERVATION OF THE COEXISTENCE OF TWO FLUID PHASES IN NATIVE PULMONARY SURFACTANT MEMBRANES AT PHYSIOLOGICAL TEMPERATURES, 10.1074/jbc.m404648200
  201. Kahya Nicoletta, Scherfeld Dag, Bacia Kirsten, Poolman Bert, Schwille Petra, Probing Lipid Mobility of Raft-exhibiting Model Membranes by Fluorescence Correlation Spectroscopy, 10.1074/jbc.m302969200
  202. Plasencia I., Norlén L., Bagatolli L.A., Direct Visualization of Lipid Domains in Human Skin Stratum Corneum's Lipid Membranes: Effect of pH and Temperature, 10.1529/biophysj.106.096164
  203. Carquin Mélanie, Pollet Hélène, Veiga-da-Cunha Maria, Cominelli Antoine, Van Der Smissen Patrick, N’kuli Francisca, Emonard Hervé, Henriet Patrick, Mizuno Hideaki, Courtoy Pierre J., Tyteca Donatienne, Endogenous sphingomyelin segregates into submicrometric domains in the living erythrocyte membrane, 10.1194/jlr.m048538
  204. D'Auria Ludovic, Fenaux Marisa, Aleksandrowicz Paulina, Van Der Smissen Patrick, Chantrain Christophe, Vermylen Christiane, Vikkula Miikka, Courtoy Pierre J., Tyteca Donatienne, Micrometric segregation of fluorescent membrane lipids: relevance for endogenous lipids and biogenesis in erythrocytes, 10.1194/jlr.m034314
  205. Sanchez S. A., Tricerri M. A., Gratton E., Laurdan generalized polarization fluctuations measures membrane packing micro-heterogeneity in vivo, 10.1073/pnas.1118288109
  206. Carquin Mélanie, Conrard Louise, Pollet Hélène, Van Der Smissen Patrick, Cominelli Antoine, Veiga-da-Cunha Maria, Courtoy Pierre J., Tyteca Donatienne, Cholesterol segregates into submicrometric domains at the living erythrocyte membrane: evidence and regulation, 10.1007/s00018-015-1951-x
  207. Tyteca D., D'Auria L., Der Smissen P. Van, Medts T., Carpentier S., Monbaliu J.C., de Diesbach P., Courtoy P.J., Three unrelated sphingomyelin analogs spontaneously cluster into plasma membrane micrometric domains, 10.1016/j.bbamem.2010.01.021
  208. Bach Juri Niño, Bramkamp Marc, Flotillins functionally organize the bacterial membrane : Flotillin-mediated membrane organization, 10.1111/mmi.12252
  209. Grossmann Guido, Opekarová Miroslava, Malinsky Jan, Weig-Meckl Ina, Tanner Widmar, Membrane potential governs lateral segregation of plasma membrane proteins and lipids in yeast, 10.1038/sj.emboj.7601466
  210. Leonard, Volume 19, 121 (2017)
  211. Grassmé H., Jendrossek V., Riehle A., von Kürthy G., Berger J., Schwarz H., Weller M., Kolesnick R., Gulbins E., Host defense against Pseudomonas aeruginosa requires ceramide-rich membrane rafts, 10.1038/nm823
  212. Stancevic Branka, Kolesnick Richard, Ceramide-rich platforms in transmembrane signaling, 10.1016/j.febslet.2010.02.026
  213. Dietrich C., Bagatolli L.A., Volovyk Z.N., Thompson N.L., Levi M., Jacobson K., Gratton E., Lipid Rafts Reconstituted in Model Membranes, 10.1016/s0006-3495(01)76114-0
  214. Jacobson Ken, Mouritsen Ole G., Anderson Richard G. W., Lipid rafts: at a crossroad between cell biology and physics, 10.1038/ncb0107-7
  215. Sezgin Erdinc, Gutmann Theresia, Buhl Tomasz, Dirkx Ron, Grzybek Michal, Coskun Ünal, Solimena Michele, Simons Kai, Levental Ilya, Schwille Petra, Adaptive Lipid Packing and Bioactivity in Membrane Domains, 10.1371/journal.pone.0123930
  216. Stone Matthew B, Shelby Sarah A, Núñez Marcos F, Wisser Kathleen, Veatch Sarah L, Protein sorting by lipid phase-like domains supports emergent signaling function in B lymphocyte plasma membranes, 10.7554/elife.19891
  217. Owen Dylan M., Oddos Stephane, Kumar Sunil, Davis Daniel M., Neil Mark A. A., French Paul M. W., Dustin Michael L., Magee Anthony I., Cebecauer Marek, High plasma membrane lipid order imaged at the immunological synapse periphery in live T cells, 10.3109/09687688.2010.495353
  218. Rentero Carles, Zech Tobias, Quinn Carmel M., Engelhardt Karin, Williamson David, Grewal Thomas, Jessup Wendy, Harder Thomas, Gaus Katharina, Functional Implications of Plasma Membrane Condensation for T Cell Activation, 10.1371/journal.pone.0002262
  219. Gaus Katharina, Chklovskaia Elena, Fazekas de St. Groth Barbara, Jessup Wendy, Harder Thomas, Condensation of the plasma membrane at the site of T lymphocyte activation, 10.1083/jcb.200505047
  220. Leonard Catherine, Pollet Hélène, Vermylen Christiane, Gov Nir, Tyteca Donatienne, Mingeot-Leclercq Marie-Paule, Tuning of Differential Lipid Order Between Submicrometric Domains and Surrounding Membrane Upon Erythrocyte Reshaping, 10.1159/000492700
  221. Ursell T. S., Klug W. S., Phillips R., Morphology and interaction between lipid domains, 10.1073/pnas.0903825106
  222. Skočaj Matej, Yu Yang, Grundner Maja, Resnik Nataša, Bedina Zavec Apolonija, Leonardi Adrijana, Križaj Igor, Guella Graziano, Maček Peter, Kreft Mateja Erdani, Frangež Robert, Veranič Peter, Sepčić Kristina, Characterisation of plasmalemmal shedding of vesicles induced by the cholesterol/sphingomyelin binding protein, ostreolysin A-mCherry, 10.1016/j.bbamem.2016.08.015
  223. D′auria Ludovic, Van Der Smissen Patrick, Bruyneel Frédéric, Courtoy Pierre J., Tyteca Donatienne, Segregation of Fluorescent Membrane Lipids into Distinct Micrometric Domains: Evidence for Phase Compartmentation of Natural Lipids?, 10.1371/journal.pone.0017021
  224. Leonard C., Conrard L., Guthmann M., Pollet H., Carquin M., Vermylen C., Gailly P., Van Der Smissen P., Mingeot-Leclercq M. P., Tyteca D., Contribution of plasma membrane lipid domains to red blood cell (re)shaping, 10.1038/s41598-017-04388-z
  225. Mikhalyov Ilya, Samsonov Andrey, Lipid raft detecting in membranes of live erythrocytes, 10.1016/j.bbamem.2011.04.002
  226. Murate M., Abe M., Kasahara K., Iwabuchi K., Umeda M., Kobayashi T., Transbilayer distribution of lipids at nano scale, 10.1242/jcs.163105
  227. Montes L.-Ruth, López David J., Sot Jesús, Bagatolli Luis A., Stonehouse Martin J., Vasil Michael L., Wu Bill X., Hannun Yusuf A., Goñi Félix M., Alonso Alicia, Ceramide-Enriched Membrane Domains in Red Blood Cells and the Mechanism of Sphingomyelinase-Induced Hot−Cold Hemolysis†, 10.1021/bi801139z
  228. Gousset Karine, Wolkers Willem F., Tsvetkova Nelly M., Oliver Ann E., Field Cara L., Walker Naomi J., Crowe John H., Tablin Fern, Evidence for a physiological role for membrane rafts in human platelets, 10.1002/jcp.10039
  229. Gaus K., Gratton E., Kable E. P. W., Jones A. S., Gelissen I., Kritharides L., Jessup W., Visualizing lipid structure and raft domains in living cells with two-photon microscopy, 10.1073/pnas.2534386100
  230. Gomez-Mouton C., Abad J. L., Mira E., Lacalle R. A., Gallardo E., Jimenez-Baranda S., Illa I., Bernad A., Manes S., Martinez-A. C., Segregation of leading-edge and uropod components into specific lipid rafts during T cell polarization, 10.1073/pnas.171160298
  231. Ekyalongo Roudy C., Nakayama Hitoshi, Kina Katsunari, Kaga Naoko, Iwabuchi Kazuhisa, Organization and functions of glycolipid-enriched microdomains in phagocytes, 10.1016/j.bbalip.2014.06.009
  232. Mizuno Hideaki, Abe Mitsuhiro, Dedecker Peter, Makino Asami, Rocha Susana, Ohno-Iwashita Yoshiko, Hofkens Johan, Kobayashi Toshihide, Miyawaki Atsushi, Fluorescent probes for superresolution imaging of lipid domains on the plasma membrane, 10.1039/c1sc00169h
  233. Rungaldier Stefanie, Oberwagner Walter, Salzer Ulrich, Csaszar Edina, Prohaska Rainer, Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains, 10.1016/j.bbamem.2012.11.030
  234. Salzer U., Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts, 10.1182/blood.v97.4.1141
  235. Murphy S. C., Erythrocyte detergent-resistant membrane proteins: their characterization and selective uptake during malarial infection, 10.1182/blood-2003-09-3165
  236. Cai Mingjun, Zhao Weidong, Shang Xin, Jiang Junguang, Ji Hongbin, Tang Zhiyong, Wang Hongda, Direct Evidence of Lipid Rafts by in situ Atomic Force Microscopy, 10.1002/smll.201102183
  237. Dumitru Andra C., Poncin Mégane A., Conrard Louise, Dufrêne Yves F., Tyteca Donatienne, Alsteens David, Nanoscale membrane architecture of healthy and pathological red blood cells, 10.1039/c7nh00187h
  238. Lutz, J. Biol. Chem., 251, 3500 (1976)
  239. Salzer Ulrich, Hunger Ursula, Prohaska Rainer, Chapter Three Insights in the Organization and Dynamics of Erythrocyte Lipid Rafts, Advances in Planar Lipid Bilayers and Liposomes (2008) ISBN:9780123739025 p.49-259, 10.1016/s1554-4516(07)06003-6
  240. Civenni, Blood, 91, 1784 (1998)
  241. Whitlow, Blood, 81, 510 (1993)
  242. Wilkinson D. Katie, Turner E. Jane, Parkin Edward T., Garner Ashley E., Harrison Penny J., Crawford Mark, Stewart Gordon W., Hooper Nigel M., Membrane raft actin deficiency and altered Ca2+-induced vesiculation in stomatin-deficient overhydrated hereditary stomatocytosis, 10.1016/j.bbamem.2007.09.016
  243. Santos Nuno C., Martins-Silva J., Saldanha Carlota, Gramicidin D and Dithiothreitol Effects on Erythrocyte Exovesiculation, 10.1385/cbb:43:3:419
  244. Kunzelmann-Marche Corinne, Freyssinet Jean-Marie, Martı́nez M. Carmen, Loss of Plasma Membrane Phospholipid Asymmetry Requires Raft Integrity : ROLE OF TRANSIENT RECEPTOR POTENTIAL CHANNELS AND ERK PATHWAY, 10.1074/jbc.m200324200
  245. Gonzalez Laurie J, Gibbons Elizabeth, Bailey Rachel W, Fairbourn Jeremy, Nguyen Thaothanh, Smith Samantha K, Best Katrina B, Nelson Jennifer, Judd Allan M, Bell John D, The influence of membrane physical properties on microvesicle release in human erythrocytes, 10.1186/1757-5036-2-7
  246. DORAHY Douglas J, LINCZ Lisa F, MELDRUM Clifford J, BURNS Gordon F, Biochemical isolation of a membrane microdomain from resting platelets highly enriched in the plasma membrane glycoprotein CD36, 10.1042/bj3190067
  247. Bali Rachna, Savino Laura, Ramirez Diego A., Tsvetkova Nelly M., Bagatolli Luis, Tablin Fern, Crowe John H., Leidy Chad, Macroscopic domain formation during cooling in the platelet plasma membrane: An issue of low cholesterol content, 10.1016/j.bbamem.2009.03.017
  248. Bodin Stéphane, Tronchère Hélène, Payrastre Bernard, Lipid rafts are critical membrane domains in blood platelet activation processes, 10.1016/s0005-2736(03)00022-1
  249. Bodin Stéphane, Giuriato Sylvie, Ragab Jeannie, Humbel Bruno M., Viala Cécile, Vieu Claude, Chap Hugues, Payrastre Bernard, Production of Phosphatidylinositol 3,4,5-Trisphosphate and Phosphatidic Acid in Platelet Rafts:  Evidence for a Critical Role of Cholesterol-Enriched Domains in Human Platelet Activation†, 10.1021/bi0109313
  250. Caroni P., NEW EMBO MEMBERS' REVIEW: Actin cytoskeleton regulation through modulation of PI(4,5)P2 rafts, 10.1093/emboj/20.16.4332
  251. Flaumenhaft Robert, Formation and fate of platelet microparticles, 10.1016/j.bcmd.2005.12.019
  252. Mairhofer M., Stomatin is a major lipid-raft component of platelet alpha granules, 10.1182/blood.v100.3.897
  253. Wei Hao, Malcor Jean-Daniel M., Harper Matthew T., Lipid rafts are essential for release of phosphatidylserine-exposing extracellular vesicles from platelets, 10.1038/s41598-018-28363-4
  254. Larive Romain M., Baisamy Laurent, Urbach Serge, Coopman Peter, Bettache Nadir, Cell membrane extensions, generated by mechanical constraint, are associated with a sustained lipid raft patching and an increased cell signaling, 10.1016/j.bbamem.2009.11.016
  255. Heijnen H. F. G., Van Lier M., Waaijenborg S., Ohno-Iwashita Y., Waheed A. A., Inomata M., Gorter G., Möbius W., Akkerman J. W. N., Slot J. W., Concentration of rafts in platelet filopodia correlates with recruitment of c-Src and CD63 to these domains : Cholesterol and platelet adhesion, 10.1046/j.1538-7836.2003.00316.x
  256. O'Connell Daniel J., Rozenvayn Nataliya, Flaumenhaft Robert, Phosphatidylinositol 4,5-Bisphosphate Regulates Activation-Induced Platelet Microparticle Formation†, 10.1021/bi047344c
  257. Gómez-Moutón Concepción, Lacalle Rosa Ana, Mira Emilia, Jiménez-Baranda Sonia, Barber Domingo F., Carrera Ana C., Martínez-A. Carlos, Mañes Santos, Dynamic redistribution of raft domains as an organizing platform for signaling during cell chemotaxis, 10.1083/jcb.200309101
  258. Seveau Stéphanie, Eddy Robert J., Maxfield Frederick R., Pierini Lynda M., Cytoskeleton-dependent Membrane Domain Segregation during Neutrophil Polarization, 10.1091/mbc.12.11.3550
  259. Millan J., Lipid rafts mediate biosynthetic transport to the T lymphocyte uropod subdomain and are necessary for uropod integrity and function, 10.1182/blood.v99.3.978
  260. Pierini Lynda M., Eddy Robert J., Fuortes Michele, Seveau Stéphanie, Casulo Carlo, Maxfield Frederick R., Membrane Lipid Organization Is Critical for Human Neutrophil Polarization, 10.1074/jbc.m212386200
  261. Nakayama Hitoshi, Yoshizaki Fumiko, Prinetti Alessandro, Sonnino Sandro, Mauri Laura, Takamori Kenji, Ogawa Hideoki, Iwabuchi Kazuhisa, Lyn-coupled LacCer-enriched lipid rafts are required for CD11b/CD18-mediated neutrophil phagocytosis of nonopsonized microorganisms, 10.1189/jlb.0707478
  262. Saha Amit K., Dallo Shatha F., Detmar Ariana L., Osmulski Pawel, Gaczynska Maria, Huang Tim Hui-Ming, Ramasubramanian Anand K., Cellular cholesterol regulates monocyte deformation, 10.1016/j.jbiomech.2016.12.033
  263. Rothmeier Andrea S., Marchese Patrizia, Petrich Brian G., Furlan-Freguia Christian, Ginsberg Mark H., Ruggeri Zaverio M., Ruf Wolfram, Caspase-1–mediated pathway promotes generation of thromboinflammatory microparticles, 10.1172/jci79329
  264. Roduit Charles, van der Goot F. Gisou, De Los Rios Paolo, Yersin Alexandre, Steiner Pascal, Dietler Giovanni, Catsicas Stefan, Lafont Frank, Kasas Sandor, Elastic Membrane Heterogeneity of Living Cells Revealed by Stiff Nanoscale Membrane Domains, 10.1529/biophysj.107.112862
  265. Boggs Joan M., Wang Huimin, Co-clustering of galactosylceramide and membrane proteins in oligodendrocyte membranes on interaction with polyvalent carbohydrate and prevention by an intact cytoskeleton, 10.1002/jnr.20080
  266. Boggs Joan M., Gao Wen, Zhao Jingsha, Park Hyun-Joo, Liu Yuanfang, Basu Amit, Participation of galactosylceramide and sulfatide in glycosynapses between oligodendrocyte or myelin membranes, 10.1016/j.febslet.2009.11.074
  267. Gonnord P., Delarasse C., Auger R., Benihoud K., Prigent M., Cuif M. H., Lamaze C., Kanellopoulos J. M., Palmitoylation of the P2X7 receptor, an ATP-gated channel, controls its expression and association with lipid rafts, 10.1096/fj.08-114637
  268. Ohmi Yuhsuke, Ohkawa Yuki, Yamauchi Yoshio, Tajima Orie, Furukawa Keiko, Furukawa Koichi, Essential Roles of Gangliosides in the Formation and Maintenance of Membrane Microdomains in Brain Tissues, 10.1007/s11064-012-0764-7
  269. Schilling Tom, Eder Claudia, Importance of lipid rafts for lysophosphatidylcholine-induced caspase-1 activation and reactive oxygen species generation, 10.1016/j.cellimm.2010.08.003
  270. Allen John A., Halverson-Tamboli Robyn A., Rasenick Mark M., Lipid raft microdomains and neurotransmitter signalling, 10.1038/nrn2059
  271. Decker L., Lipid Rafts and Integrin Activation Regulate Oligodendrocyte Survival, 10.1523/jneurosci.5725-03.2004
  272. Martín Virginia, Fabelo Noemí, Santpere Gabriel, Puig Berta, Marín Raquel, Ferrer Isidre, Díaz Mario, Lipid Alterations in Lipid Rafts from Alzheimer's Disease Human Brain Cortex, 10.3233/jad-2010-1242
  273. Yuyama Kohei, Mitsutake Susumu, Igarashi Yasuyuki, Pathological roles of ceramide and its metabolites in metabolic syndrome and Alzheimer's disease, 10.1016/j.bbalip.2013.08.002
  274. Booth Heather D.E., Hirst Warren D., Wade-Martins Richard, The Role of Astrocyte Dysfunction in Parkinson’s Disease Pathogenesis, 10.1016/j.tins.2017.04.001
  275. Hein Leanne K., Rozaklis Tina, Adams Melissa K., Hopwood John J., Karageorgos Litsa, Lipid composition of microdomains is altered in neuronopathic Gaucher disease sheep brain and spleen, 10.1016/j.ymgme.2017.05.010
  276. Al-Nedawi K., Meehan B., Kerbel R. S., Allison A. C., Rak J., Endothelial expression of autocrine VEGF upon the uptake of tumor-derived microvesicles containing oncogenic EGFR, 10.1073/pnas.0804543106
  277. Orsini F., Cremona A., Arosio P., Corsetto P.A., Montorfano G., Lascialfari A., Rizzo A.M., Atomic force microscopy imaging of lipid rafts of human breast cancer cells, 10.1016/j.bbamem.2012.07.024
  278. Kiyokawa Etsuko, Baba Takeshi, Otsuka Naomi, Makino Asami, Ohno Shinichi, Kobayashi Toshihide, Spatial and Functional Heterogeneity of Sphingolipid-rich Membrane Domains, 10.1074/jbc.m502244200
  279. Kokkonen Nina, Khosrowabadi Elham, Hassinen Antti, Harrus Deborah, Glumoff Tuomo, Kietzmann Thomas, Kellokumpu Sakari, Abnormal Golgi pH Homeostasis in Cancer Cells Impairs Apical Targeting of Carcinoembryonic Antigen by Inhibiting Its Glycosyl-Phosphatidylinositol Anchor-Mediated Association with Lipid Rafts, 10.1089/ars.2017.7389
  280. Hirpara Jayshree L., Loh Thomas, Ng Siok Bian, Chng Wee Joo, Pervaiz Shazib, Aberrant localization of apoptosis protease activating factor-1 in lipid raft sub-domains of diffuse large B cell lymphomas, 10.18632/oncotarget.13336
  281. Lavie Yaakov, Fiucci Giusy, Czarny Malgorzata, Liscovitch Mordechai, Changes in membrane microdomains and caveolae constituents in multidrug-resistant cancer cells, 10.1007/bf02562229
  282. Ausili Alessio, Martínez-Valera Pablo, Torrecillas Alejandro, Gómez-Murcia Victoria, de Godos Ana M., Corbalán-García Senena, Teruel José A., Gómez Fernández Juan C., Anticancer Agent Edelfosine Exhibits a High Affinity for Cholesterol and Disorganizes Liquid-Ordered Membrane Structures, 10.1021/acs.langmuir.8b01539
  283. Mollinedo Faustino, Gajate Consuelo, Lipid rafts as major platforms for signaling regulation in cancer, 10.1016/j.jbior.2014.10.003
  284. Lorent Joseph H., Quetin-Leclercq Joëlle, Mingeot-Leclercq Marie-Paule, The amphiphilic nature of saponins and their effects on artificial and biological membranes and potential consequences for red blood and cancer cells, 10.1039/c4ob01652a
  285. Park E-K, Lee EJ, Lee S-H, Koo KH, Sung JY, Hwang EH, Park JH, Kim C-W, Jeong K-C, Park B-K, Kim Y-N, Induction of apoptosis by the ginsenoside Rh2 by internalization of lipid rafts and caveolae and inactivation of Akt : Rh2 affects raft internalization and Akt, 10.1111/j.1476-5381.2010.00768.x
  286. Yi Jae-Sung, Choo Hyo-Jung, Cho Bong-Rae, Kim Hwan-Myung, Kim Yong-Nyun, Ham Young-Mi, Ko Young-Gyu, Ginsenoside Rh2 induces ligand-independent Fas activation via lipid raft disruption, 10.1016/j.bbrc.2009.05.028
  287. Verstraeten Sandrine L., Albert Marie, Paquot Adrien, Muccioli Giulio G., Tyteca Donatienne, Mingeot-Leclercq Marie-Paule, Membrane cholesterol delays cellular apoptosis induced by ginsenoside Rh2, a steroid saponin, 10.1016/j.taap.2018.05.014
  288. van Blitterswijk W. J., Emmelot P., Hilkmann H. A. M., Hilgers J., Feltkamp C. A., Rigid plasma-membrane-derived vesicles, enriched in tumour-associated surface antigens (MLr), occurring in the ascites fluid of a murine leukaemia (GRSL), 10.1002/ijc.2910230112
  289. Lamprecht Constanze, Gehrmann Mathias, Madl Josef, Römer Winfried, Multhoff Gabriele, Ebner Andreas, Molecular AFM imaging of Hsp70-1A association with dipalmitoyl phosphatidylserine reveals membrane blebbing in the presence of cholesterol, 10.1007/s12192-018-0879-0
Bibliographic reference Pollet, Hélène ; Conrard, Louise ; Cloos, Anne-Sophie ; Tyteca, Donatienne. Plasma Membrane Lipid Domains as Platforms for Vesicle Biogenesis and Shedding?. In: Biomolecules, Vol. 8, no.3, p. 94 [1-38] (2018)
Permanent URL http://hdl.handle.net/2078.1/212395