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  1. AU="Suzuki, Kenichi G N"
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  35. AU="Grevtsov K.I."

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  1. Artikel ; Online: Single-Molecule Imaging of Ganglioside Probes in Living Cell Plasma Membranes.

    Suzuki, Kenichi G N

    Methods in molecular biology (Clifton, N.J.)

    2022  Band 2613, Seite(n) 215–227

    Abstract: Gangliosides play a variety of physiological roles and are one of the most important lipid raft constituents. However, their dynamic behaviors have scarcely been investigated in living cells because of the lack of fluorescent probes that behave like ... ...

    Abstract Gangliosides play a variety of physiological roles and are one of the most important lipid raft constituents. However, their dynamic behaviors have scarcely been investigated in living cells because of the lack of fluorescent probes that behave like their parental molecules. Recently, fluorescent ganglioside probes that mimic native ganglioside behaviors have been developed. In this chapter, I discuss the recent advances in research related to the lateral localization and dynamic behaviors of gangliosides in the plasma membranes of living cells.
    Mesh-Begriff(e) Gangliosides/metabolism ; Single Molecule Imaging ; Cell Membrane/metabolism ; Membranes/metabolism ; Nanotechnology
    Chemische Substanzen Gangliosides
    Sprache Englisch
    Erscheinungsdatum 2022-12-10
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-2910-9_17
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Refinement of Singer-Nicolson fluid-mosaic model by microscopy imaging: Lipid rafts and actin-induced membrane compartmentalization.

    Suzuki, Kenichi G N / Kusumi, Akihiro

    Biochimica et biophysica acta. Biomembranes

    2022  Band 1865, Heft 2, Seite(n) 184093

    Abstract: This year celebrates the 50th anniversary of the Singer-Nicolson fluid mosaic model for biological membranes. The next level of sophistication we have achieved for understanding plasma membrane (PM) structures, dynamics, and functions during these 50 ... ...

    Abstract This year celebrates the 50th anniversary of the Singer-Nicolson fluid mosaic model for biological membranes. The next level of sophistication we have achieved for understanding plasma membrane (PM) structures, dynamics, and functions during these 50 years includes the PM interactions with cortical actin filaments and the partial demixing of membrane constituent molecules in the PM, particularly raft domains. Here, first, we summarize our current knowledge of these two structures and emphasize that they are interrelated. Second, we review the structure, molecular dynamics, and function of raft domains, with main focuses on raftophilic glycosylphosphatidylinositol-anchored proteins (GPI-APs) and their signal transduction mechanisms. We pay special attention to the results obtained by single-molecule imaging techniques and other advanced microscopy methods. We also clarify the limitations of present optical microscopy methods for visualizing raft domains, but emphasize that single-molecule imaging techniques can "detect" raft domains associated with molecules of interest in the PM.
    Mesh-Begriff(e) Actins/metabolism ; Microscopy ; Singing ; Membrane Microdomains/chemistry ; Cell Membrane/metabolism
    Chemische Substanzen Actins
    Sprache Englisch
    Erscheinungsdatum 2022-11-21
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamem.2022.184093
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Recently developed glycosphingolipid probes and their dynamic behavior in cell plasma membranes as revealed by single-molecule imaging.

    Suzuki, Kenichi G N / Komura, Naoko / Ando, Hiromune

    Glycoconjugate journal

    2023  Band 40, Heft 3, Seite(n) 305–314

    Abstract: Glycosphingolipids, including gangliosides, are representative lipid raft markers that perform a variety of physiological roles in cell membranes. However, studies aimed at revealing their dynamic behavior in living cells are rare, mostly due to a lack ... ...

    Abstract Glycosphingolipids, including gangliosides, are representative lipid raft markers that perform a variety of physiological roles in cell membranes. However, studies aimed at revealing their dynamic behavior in living cells are rare, mostly due to a lack of suitable fluorescent probes. Recently, the ganglio-series, lacto-series, and globo-series glycosphingolipid probes, which mimic the behavior of the parental molecules in terms of partitioning to the raft fraction, were developed by conjugating hydrophilic dyes to the terminal glycans of glycosphingolipids using state-of-art entirely chemical-based synthetic techniques. High-speed, single-molecule observation of these fluorescent probes revealed that gangliosides were scarcely trapped in small domains (100 nm in diameter) for more than 5 ms in steady-state cells, suggesting that rafts including gangliosides were always moving and very small. Furthermore, dual-color, single-molecule observations clearly showed that homodimers and clusters of GPI-anchored proteins were stabilized by transiently recruiting sphingolipids, including gangliosides, to form homodimer rafts and the cluster rafts, respectively. In this review, we briefly summarize recent studies, the development of a variety of glycosphingolipid probes as well as the identification of the raft structures including gangliosides in living cells by single-molecule imaging.
    Mesh-Begriff(e) Glycosphingolipids/metabolism ; Fluorescent Dyes/chemistry ; Single Molecule Imaging ; Gangliosides/metabolism ; Cell Membrane/metabolism ; Membrane Microdomains/metabolism
    Chemische Substanzen Glycosphingolipids ; Fluorescent Dyes ; Gangliosides
    Sprache Englisch
    Erscheinungsdatum 2023-05-03
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 283770-5
    ISSN 1573-4986 ; 0282-0080
    ISSN (online) 1573-4986
    ISSN 0282-0080
    DOI 10.1007/s10719-023-10116-9
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel: [Investigation of raft dynamics by single-molecule observation of ganglioside probes].

    Suzuki, Kenichi G N

    Seikagaku. The Journal of Japanese Biochemical Society

    2018  Band 89, Heft 1, Seite(n) 121–125

    Mesh-Begriff(e) Animals ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Fluorescent Dyes/analysis ; Gangliosides/chemistry ; Gangliosides/metabolism
    Chemische Substanzen Fluorescent Dyes ; Gangliosides
    Sprache Japanisch
    Erscheinungsdatum 2018-04-02
    Erscheinungsland Japan
    Dokumenttyp Journal Article ; Review
    ZDB-ID 282319-6
    ISSN 0037-1017
    ISSN 0037-1017
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Single-Molecule Imaging of Signal Transduction via GPI-Anchored Receptors.

    Suzuki, Kenichi G N

    Methods in molecular biology (Clifton, N.J.)

    2016  Band 1376, Seite(n) 229–238

    Abstract: Lipid rafts have been drawing extensive attention as a signaling platform. To investigate molecular interactions in lipid rafts, we often need to observe molecules in the plasma membranes of living cells because chemical fixation and subsequent ... ...

    Abstract Lipid rafts have been drawing extensive attention as a signaling platform. To investigate molecular interactions in lipid rafts, we often need to observe molecules in the plasma membranes of living cells because chemical fixation and subsequent immunostaining with divalent or multivalent antibodies may change the location of the target molecules. In this chapter, we describe how to examine dynamics of raft-associated glycosylphosphatidylinositol (GPI)-anchored receptors and interactions of the receptors with downstream signaling molecules by single-particle tracking or single-molecule imaging techniques.
    Mesh-Begriff(e) Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/pharmacology ; CD59 Antigens/metabolism ; Calcium/metabolism ; Fluorescent Dyes ; GPI-Linked Proteins/antagonists & inhibitors ; GPI-Linked Proteins/chemistry ; GPI-Linked Proteins/metabolism ; Inositol 1,4,5-Trisphosphate/metabolism ; Metal Nanoparticles ; Molecular Imaging/methods ; Protein Binding ; Receptors, Cell Surface/antagonists & inhibitors ; Receptors, Cell Surface/chemistry ; Receptors, Cell Surface/metabolism ; Signal Transduction ; Staining and Labeling
    Chemische Substanzen Antibodies, Monoclonal ; CD59 Antigens ; Fluorescent Dyes ; GPI-Linked Proteins ; Receptors, Cell Surface ; Inositol 1,4,5-Trisphosphate (85166-31-0) ; Calcium (SY7Q814VUP)
    Sprache Englisch
    Erscheinungsdatum 2016
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-3170-5_19
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: Fluorescence Spectroscopic Analysis of Lateral and Transbilayer Fluidity of Exosome Membranes.

    Yasuda, Tomokazu / Watanabe, Hirofumi / Hirosawa, Koichiro M / Suzuki, Kenichi G N / Suga, Keishi / Hanashima, Shinya

    Langmuir : the ACS journal of surfaces and colloids

    2022  Band 38, Heft 48, Seite(n) 14695–14703

    Abstract: Exosomes are small extracellular vesicles (sEVs) involved in distal cell-cell communication and cancer migration by transferring functional cargo molecules. Membrane domains similar to lipid rafts are assumed to occur in exosome membranes and are ... ...

    Abstract Exosomes are small extracellular vesicles (sEVs) involved in distal cell-cell communication and cancer migration by transferring functional cargo molecules. Membrane domains similar to lipid rafts are assumed to occur in exosome membranes and are involved in interactions with target cells. However, the bilayer membrane properties of these small vesicles have not been fully investigated. Therefore, we examined the fluidity, lateral domain separation, and transbilayer asymmetry of exosome membranes using fluorescence spectroscopy. Although there were some differences between the exosomes, TMA-DPH anisotropy showing moderate lipid chain order indicated that ordered phases comprised a significant proportion of exosome membranes. Selective TEMPO quenching of the TMA-DPH fluorescence in the liquid-disordered phase indicated that 40-50% of the exosome membrane area belonged to the ordered phase based on a phase-separated model. Furthermore, NBD-PC in the outer leaflet showed longer fluorescence lifetimes than those in the inner leaflets. Therefore, the exosome membranes maintained transbilayer asymmetry with a topology similar to that of the plasma membranes. In addition, the lateral and transbilayer orders of exosome membranes obtained from different cell lines varied, probably depending on the different membrane lipid components and compositions partially derived from donor cells. As these higher membrane orders and asymmetric topologies are similar to those of cell membranes with lipid rafts, raft-like functional domains are possibly enriched on exosome membranes. These domains likely play key roles in the biological functions and cellular uptake of exosomes by facilitating selective membrane interactions with target organs.
    Mesh-Begriff(e) Spectrometry, Fluorescence ; Membrane Fluidity ; Lipid Bilayers/chemistry ; Exosomes/metabolism ; Cell Membrane/metabolism
    Chemische Substanzen 1-(4-(trimethylamino)phenyl)-6-phenylhexa-1,3,5-triene (71316-28-4) ; Lipid Bilayers
    Sprache Englisch
    Erscheinungsdatum 2022-11-24
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2005937-1
    ISSN 1520-5827 ; 0743-7463
    ISSN (online) 1520-5827
    ISSN 0743-7463
    DOI 10.1021/acs.langmuir.2c02258
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel: New insights into the organization of plasma membrane and its role in signal transduction.

    Suzuki, Kenichi G N

    International review of cell and molecular biology

    2015  Band 317, Seite(n) 67–96

    Abstract: Plasma membranes have heterogeneous structures for efficient signal transduction, required to perform cell functions. Recent evidence indicates that the heterogeneous structures are produced by (1) compartmentalization by actin-based membrane skeleton, ( ... ...

    Abstract Plasma membranes have heterogeneous structures for efficient signal transduction, required to perform cell functions. Recent evidence indicates that the heterogeneous structures are produced by (1) compartmentalization by actin-based membrane skeleton, (2) raft domains, (3) receptor-receptor interactions, and (4) the binding of receptors to cytoskeletal proteins. This chapter provides an overview of recent studies on diffusion, clustering, raft association, actin binding, and signal transduction of membrane receptors, especially glycosylphosphatidylinositol (GPI)-anchored receptors. Studies on diffusion of GPI-anchored receptors suggest that rafts may be small and/or short-lived in plasma membranes. In steady state conditions, GPI-anchored receptors form transient homodimers, which may represent the "standby state" for the stable homodimers and oligomers upon ligation. Furthermore, It is proposed that upon ligation, the binding of GPI-anchored receptor clusters to cytoskeletal actin filaments produces a platform for downstream signaling, and that the pulse-like signaling easily maintains the stability of the overall signaling activity.
    Mesh-Begriff(e) Animals ; Cell Membrane/metabolism ; Humans ; Membrane Microdomains/metabolism ; Membrane Proteins/metabolism ; Signal Transduction
    Chemische Substanzen Membrane Proteins
    Sprache Englisch
    Erscheinungsdatum 2015
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2427220-6
    ISSN 1937-6448 ; 0074-7696
    ISSN 1937-6448 ; 0074-7696
    DOI 10.1016/bs.ircmb.2015.02.004
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  8. Artikel ; Online: Cholesterol- and actin-centered view of the plasma membrane: updating the Singer-Nicolson fluid mosaic model to commemorate its 50th anniversary

    Kusumi, Akihiro / Tsunoyama, Taka A / Tang, Bo / Hirosawa, Koichiro M / Morone, Nobuhiro / Fujiwara, Takahiro K / Suzuki, Kenichi G N

    Molecular biology of the cell

    2023  Band 34, Heft 5

    Abstract: Two very polarized views exist for understanding the cellular plasma membrane (PM). For some, it is the simple fluid described by the original Singer-Nicolson fluid mosaic model. For others, due to the presence of thousands of molecular species that ... ...

    Abstract Two very polarized views exist for understanding the cellular plasma membrane (PM). For some, it is the simple fluid described by the original Singer-Nicolson fluid mosaic model. For others, due to the presence of thousands of molecular species that extensively interact with each other, the PM forms various clusters and domains that are constantly changing and therefore, no simple rules exist that can explain the structure and molecular dynamics of the PM. In this article, we propose that viewing the PM from its two predominant components, cholesterol and actin filaments, provides an excellent and transparent perspective of PM organization, dynamics, and mechanisms for its functions. We focus on the actin-induced membrane compartmentalization and lipid raft domains coexisting in the PM and how they interact with each other to perform PM functions. This view provides an important update of the fluid mosaic model.
    Mesh-Begriff(e) Actins/metabolism ; Anniversaries and Special Events ; Singing ; Cell Membrane/metabolism ; Cholesterol/metabolism
    Chemische Substanzen Actins ; Cholesterol (97C5T2UQ7J)
    Sprache Englisch
    Erscheinungsdatum 2023-04-11
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E20-12-0809
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  9. Artikel: [Mechanisms for signal transduction in lipid rafts of cell plasma membranes].

    Suzuki, Kenichi G N

    Seikagaku. The Journal of Japanese Biochemical Society

    2013  Band 85, Heft 1, Seite(n) 34–37

    Mesh-Begriff(e) Animals ; CD59 Antigens/metabolism ; Humans ; Membrane Microdomains/metabolism ; Signal Transduction/physiology ; Time Factors
    Chemische Substanzen CD59 Antigens
    Sprache Japanisch
    Erscheinungsdatum 2013-01
    Erscheinungsland Japan
    Dokumenttyp Journal Article ; Review
    ZDB-ID 282319-6
    ISSN 0037-1017
    ISSN 0037-1017
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  10. Artikel ; Online: Formation of Supramolecular Nanostructures through in Situ Self-Assembly and Post-Assembly Modification of a Biocatalytically Constructed Dipeptide Hydrazide.

    Shintani, Yuki / Ohtomi, Taku / Shibata, Aya / Kitamura, Yoshiaki / Hirosawa, Koichiro M / Suzuki, Kenichi G N / Ikeda, Masato

    Chemistry (Weinheim an der Bergstrasse, Germany)

    2022  Band 28, Heft 8, Seite(n) e202104421

    Abstract: Aqueous self-assembly of short peptides has attracted growing attention for the construction of supramolecular materials for various bioapplications. Herein, we describe how the thermolysin-assisted biocatalytic construction of a dipeptide hydrazide from ...

    Abstract Aqueous self-assembly of short peptides has attracted growing attention for the construction of supramolecular materials for various bioapplications. Herein, we describe how the thermolysin-assisted biocatalytic construction of a dipeptide hydrazide from an N-protected amino acid and an amino acid hydrazide leads to the formation of thermally stable supramolecular hydrogels. In addition, we demonstrate the post-assembly modification of the supramolecular architectures constructed in situ tethering hydrazide groups as a chemical handle by means of fluorescence imaging.
    Mesh-Begriff(e) Dipeptides ; Hydrazines ; Hydrogels ; Nanostructures ; Peptides
    Chemische Substanzen Dipeptides ; Hydrazines ; Hydrogels ; Peptides
    Sprache Englisch
    Erscheinungsdatum 2022-01-27
    Erscheinungsland Germany
    Dokumenttyp Journal Article
    ZDB-ID 1478547-X
    ISSN 1521-3765 ; 0947-6539
    ISSN (online) 1521-3765
    ISSN 0947-6539
    DOI 10.1002/chem.202104421
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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