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-->   Masanao Kinoshita Last modified date：2024.04.24 Assistant Professor / Bioanalitical Chemistry Department of Chemistry Faculty of Sciences 1 Research Interests 2 Academic Activities 2.1 Papers 2.2 Presentations Graduate School Department of Chemistry Graduate School of Sciences Department of Chemistry Graduate School of Sciences Homepage https://kyushu-u.elsevierpure.com/en/persons/masanao-kinoshita　Reseacher Profiling Tool　Kyushu University Pure Academic Degree Science Country of degree conferring institution (Overseas) No Field of Specialization Biophysics Total Priod of education and research career in the foreign country 00years00months Research Research Interests Influence of local anesthetics on cell membraneskeyword : local anesthetics2017.06～2022.06. membrane structures and propertieskeyword : lipid rafts2019.06～2019.06. membrane sructures, properties and dynamics keyword : membrane sructures, properties, dynamics 2015.10～2015.10. Academic Activities Papers  Show All Papers >> 1. Masanao Kinoshita, Kenichi G. N. Suzuki, Nobuaki Matsumori, Misa Takada, Hikaru Ano, Kenichi Morigaki, Mitsuhiro Abe, Asami Makino, Toshihide Kobayashi, Koichiro M. Hirosawa, Takahiro K. Fujiwara, Akihiro Kusumi, Michio Murata, Raft-based sphingomyelin interactions revealed by new fluorescent sphingomyelin analogs, JOURNAL OF CELL BIOLOGY, 10.1083/jcb.201607086, 216, 4, 1183-1204, 2017.04, Sphingomyelin (SM) has been proposed to form cholesterol-dependent raft domains and sphingolipid domains in the plasma membrane (PM). How SM contributes to the formation and function of these domains remains unknown, primarily because of the scarcity of suitable fluorescent SM analogs. We developed new fluorescent SM analogs by conjugating a hydrophilic fluorophore to the SM choline headgroup without eliminating its positive charge, via a hydrophilic nonaethylene glycol linker. The new analogs behaved similarly to the native SM in terms of their partitioning behaviors in artificial liquid order-disorder phase-separated membranes and detergent-resistant PM preparations. Single fluorescent molecule tracking in the live-cell PM revealed that they indirectly interact with each other in cholesterol-and sphingosine backbone-dependent manners, and that, for similar to 10-50 ms, they undergo transient colocalization-codiffusion with a glycosylphosphatidylinositol (GPI)-anchored protein, CD59 (in monomers, transient-dimer rafts, and clusters), in CD59-oligomer size-, cholesterol-, and GPI anchoring-dependent manners. These results suggest that SM continually and rapidly exchanges between CD59-associated raft domains and the bulk PM.. Presentations  Show All Presentations >> Unauthorized reprint of the contents of this database is prohibited. Copyright © 2006, Kyushu University. All rights reserved.