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  1. Article ; Online: Temperature-dependent augmentation of ciliary motility by the TRP2 channel in Chlamydomonas reinhardtii.

    Fueki, Shunta / Kaneko, Taro / Matsuki, Haruka / Hashimoto, Yuki / Yoshida, Megumi / Isu, Atsuko / Wakabayashi, Ken-Ichi / Yoshimura, Kenjiro

    Cytoskeleton (Hoboken, N.J.)

    2024  

    Abstract: Temperature is a critical factor for living organisms. Many microorganisms migrate toward preferable temperatures, and this behavior is called thermotaxis. In this study, the molecular and physiological bases for thermotaxis are examined in Chlamydomonas ...

    Abstract Temperature is a critical factor for living organisms. Many microorganisms migrate toward preferable temperatures, and this behavior is called thermotaxis. In this study, the molecular and physiological bases for thermotaxis are examined in Chlamydomonas reinhardtii. A mutant with knockout of a transient receptor potential (TRP) channel, trp2-3, showed defective thermotaxis. The swimming velocity and ciliary beat frequency of wild-type Chlamydomonas increase with temperature; however, this temperature-dependent enhancement of motility was almost absent in the trp2-3 mutant. Wild-type Chlamydomonas showed negative thermotaxis, but mutants deficient in the outer or inner dynein arm showed positive thermotaxis and a defect in temperature-dependent increase in swimming velocity, suggesting involvement of both dynein arms in thermotaxis.
    Language English
    Publishing date 2024-03-01
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2534372-5
    ISSN 1949-3592 ; 1949-3584
    ISSN (online) 1949-3592
    ISSN 1949-3584
    DOI 10.1002/cm.21840
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  2. Article ; Online: MCAs in Arabidopsis are Ca2+-permeable mechanosensitive channels inherently sensitive to membrane tension

    Kenjiro Yoshimura / Kazuko Iida / Hidetoshi Iida

    Nature Communications, Vol 12, Iss 1, Pp 1-

    2021  Volume 9

    Abstract: Mechanosensitive ion channels convert mechanical stimuli into intracellular electric and ionic signals. Here the authors show that Arabidopsis MCA2 is a Ca2+-permeable mechanosensitive channel that is directly activated by membrane tension. ...

    Abstract Mechanosensitive ion channels convert mechanical stimuli into intracellular electric and ionic signals. Here the authors show that Arabidopsis MCA2 is a Ca2+-permeable mechanosensitive channel that is directly activated by membrane tension.
    Keywords Science ; Q
    Language English
    Publishing date 2021-10-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
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  3. Article ; Online: MCAs in Arabidopsis are Ca

    Yoshimura, Kenjiro / Iida, Kazuko / Iida, Hidetoshi

    Nature communications

    2021  Volume 12, Issue 1, Page(s) 6074

    Abstract: Mechanosensitive (MS) ion channels respond to mechanical stress and convert it into intracellular electric and ionic signals. Five MS channel families have been identified in plants, including the Mid1-Complementing Activity (MCA) channel; however, its ... ...

    Abstract Mechanosensitive (MS) ion channels respond to mechanical stress and convert it into intracellular electric and ionic signals. Five MS channel families have been identified in plants, including the Mid1-Complementing Activity (MCA) channel; however, its activation mechanisms have not been elucidated in detail. We herein demonstrate that the MCA2 channel is a Ca
    MeSH term(s) Arabidopsis/chemistry ; Arabidopsis/genetics ; Arabidopsis/metabolism ; Arabidopsis Proteins/genetics ; Arabidopsis Proteins/metabolism ; Biological Transport ; Calcium/metabolism ; Cell Membrane/chemistry ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Cell Membrane Permeability ; Mechanotransduction, Cellular ; Membrane Proteins/genetics ; Membrane Proteins/metabolism
    Chemical Substances Arabidopsis Proteins ; MCA1 protein, Arabidopsis ; MCA2 protein, Arabidopsis ; Membrane Proteins ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2021-10-19
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-021-26363-z
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  4. Article ; Online: Mechanoresponses mediated by the TRP11 channel in cilia of

    Oshima, Daichi / Yoshida, Megumi / Saga, Kosuke / Ito, Neo / Tsuji, Miyu / Isu, Atsuko / Watanabe, Nobuo / Wakabayashi, Ken-Ichi / Yoshimura, Kenjiro

    iScience

    2023  Volume 26, Issue 10, Page(s) 107926

    Abstract: Cilia are organelles involved in motility and sensory transduction, but how these two functions coexist has not been elucidated in depth. Here, the involvement of the ciliary transient receptor potential (TRP) channel TRP11 in mechanoresponses is studied ...

    Abstract Cilia are organelles involved in motility and sensory transduction, but how these two functions coexist has not been elucidated in depth. Here, the involvement of the ciliary transient receptor potential (TRP) channel TRP11 in mechanoresponses is studied in
    Language English
    Publishing date 2023-09-15
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2023.107926
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  5. Article: Transgenic

    Yoshida, Megumi / Yamamiya, Ryodai / Shimizu, Yuto / Yoshimura, Kenjiro

    Frontiers in pharmacology

    2020  Volume 11, Page(s) 578955

    Abstract: Transient receptor potential ankyrin 1 (TRPA1) channel is an ion channel whose gating is controlled by agonists, such as allyl isothiocyanate (AITC), and temperature. Since TRPA1 is associated with various disease symptoms and chemotherapeutic side ... ...

    Abstract Transient receptor potential ankyrin 1 (TRPA1) channel is an ion channel whose gating is controlled by agonists, such as allyl isothiocyanate (AITC), and temperature. Since TRPA1 is associated with various disease symptoms and chemotherapeutic side effects, it is a frequent target of drug development. To facilitate the screening of TRPA1 agonists and antagonists, this study aimed to develop a simple bioassay for TRPA1 activity. To this end, transgenic
    Language English
    Publishing date 2020-09-29
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587355-6
    ISSN 1663-9812
    ISSN 1663-9812
    DOI 10.3389/fphar.2020.578955
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  6. Article ; Online: Responses to transient receptor potential (TRP) channel agonists in

    Wada, Mamoru / Kaizuka, Itaru / Yoshimura, Kenjiro

    Biology open

    2020  Volume 9, Issue 7

    Abstract: Pungent substances, such as capsaicin and gingerol, activate the transient receptor potential (TRP)-V1 channel and affect the feeding behaviors of animals. To gain insight into how living organisms have acquired a sense for pungent substances, we ... ...

    Abstract Pungent substances, such as capsaicin and gingerol, activate the transient receptor potential (TRP)-V1 channel and affect the feeding behaviors of animals. To gain insight into how living organisms have acquired a sense for pungent substances, we explored the response to TRP agonists in a protist,
    MeSH term(s) Capsaicin/pharmacology ; Catechols/pharmacology ; Chlamydomonas reinhardtii/drug effects ; Chlamydomonas reinhardtii/metabolism ; Fatty Alcohols/pharmacology ; Flagella/drug effects ; Flagella/metabolism ; Hydrogen-Ion Concentration ; Signal Transduction ; Transient Receptor Potential Channels/agonists ; Transient Receptor Potential Channels/antagonists & inhibitors ; Transient Receptor Potential Channels/genetics ; Transient Receptor Potential Channels/metabolism
    Chemical Substances Catechols ; Fatty Alcohols ; Transient Receptor Potential Channels ; gingerol (925QK2Z900) ; Capsaicin (S07O44R1ZM)
    Language English
    Publishing date 2020-07-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2632264-X
    ISSN 2046-6390 ; 2046-6390
    ISSN (online) 2046-6390
    ISSN 2046-6390
    DOI 10.1242/bio.053140
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  7. Article ; Online: Responses to transient receptor potential (TRP) channel agonists in Chlamydomonas reinhardtii

    Mamoru Wada / Itaru Kaizuka / Kenjiro Yoshimura

    Biology Open, Vol 9, Iss

    2020  Volume 7

    Abstract: Pungent substances, such as capsaicin and gingerol, activate the transient receptor potential (TRP)-V1 channel and affect the feeding behaviors of animals. To gain insight into how living organisms have acquired a sense for pungent substances, we ... ...

    Abstract Pungent substances, such as capsaicin and gingerol, activate the transient receptor potential (TRP)-V1 channel and affect the feeding behaviors of animals. To gain insight into how living organisms have acquired a sense for pungent substances, we explored the response to TRP agonists in a protist, Chlamydomonas reinhardtii. When capsaicin or gingerol was applied to wild-type cells, they became immotile, with flagella detaching from the cell body. The degree of deflagellation was nearly halved in a mutant defective in the TRP channel ADF1. Deflagellation in the adf1 mutant was inhibited further by Ruthenium Red, indicating ADF1 and another TRP channel are involved in the deflagellation response. The response to capsaicin and gingerol was not inhibited by TRPV1-specific blockers such as 4-(3-Chloro-2-pyridinyl)-N-[4-(1,1-dimethylethyl)phenyl]-1-piperazinecarboxamide (BCTC) and capsazepine. When capsaicin or gingerol was applied to wild-type cells in the presence of Ruthenium Red, a large proportion lost motility while flagella remained attached, suggesting that flagella stop contributing to motility, at least in part, through a TRP-channel-independent pathway. These results indicate that pungent compounds such as capsaicin and gingerol induce loss of flagellar motility and flagellar detachment in C. reinhardtii cells.
    Keywords trp channel ; cilia and flagella ; chlamydomonas ; motility ; capsaicin ; gingerol ; Science ; Q ; Biology (General) ; QH301-705.5
    Subject code 572
    Language English
    Publishing date 2020-07-01T00:00:00Z
    Publisher The Company of Biologists
    Document type Article ; Online
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  8. Article: Is the exosome a potential target for cancer immunotherapy?

    Yoshimura, Akihiko / Sawada, Kenjiro / Kimura, Tadashi

    Annals of translational medicine

    2017  Volume 5, Issue 5, Page(s) 117

    Language English
    Publishing date 2017-03-16
    Publishing country China
    Document type Editorial ; Comment
    ZDB-ID 2893931-1
    ISSN 2305-5847 ; 2305-5839
    ISSN (online) 2305-5847
    ISSN 2305-5839
    DOI 10.21037/atm.2017.01.47
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  9. Article ; Online: Temperature-sensitive mutants of MscL mechanosensitive channel.

    Owada, Naoto / Yoshida, Megumi / Morita, Kohei / Yoshimura, Kenjiro

    Journal of biochemistry

    2019  Volume 166, Issue 3, Page(s) 281–288

    Abstract: MscL is a mechanosensitive channel that undergoes a global conformational change upon application of membrane stretching. To elucidate how the structural stability and flexibility occur, we isolated temperature-sensitive (Ts) mutants of Escherichia coli ... ...

    Abstract MscL is a mechanosensitive channel that undergoes a global conformational change upon application of membrane stretching. To elucidate how the structural stability and flexibility occur, we isolated temperature-sensitive (Ts) mutants of Escherichia coli MscL that allowed cell growth at 32°C but not at 42°C. Two Ts mutants, L86P and D127V, were identified. The L86P mutation occurred in the second transmembrane helix, TM2. Substitution of residues neighbouring L86 with proline also led to a Ts mutation, but the substitution of L86 with other amino acids did not result in a Ts phenotype, indicating that the Ts phenotype was due to a structural change of TM2 helix by the introduction of a proline residue. The D127V mutation was localized in the electrostatic belt of the bundle of cytoplasmic helices, indicating that stability of the pentameric bundle of the cytoplasmic helix affects MscL structure. Together, this study described a novel class of MscL mutations that were correlated with the thermodynamic stability of the MscL structure.
    MeSH term(s) Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Ion Channels/chemistry ; Ion Channels/genetics ; Ion Channels/metabolism ; Models, Molecular ; Mutation ; Temperature
    Chemical Substances Escherichia coli Proteins ; Ion Channels ; MscL protein, E coli
    Language English
    Publishing date 2019-05-29
    Publishing country England
    Document type Journal Article
    ZDB-ID 218073-x
    ISSN 1756-2651 ; 0021-924X
    ISSN (online) 1756-2651
    ISSN 0021-924X
    DOI 10.1093/jb/mvz035
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  10. Article ; Online: The impact of crystal phase transition on the hardness and structure of kidney stones.

    Michibata, Uta / Maruyama, Mihoko / Tanaka, Yutaro / Yoshimura, Masashi / Yoshikawa, Hiroshi Y / Takano, Kazufumi / Furukawa, Yoshihiro / Momma, Koichi / Tajiri, Rie / Taguchi, Kazumi / Hamamoto, Shuzo / Okada, Atsushi / Kohri, Kenjiro / Yasui, Takahiro / Usami, Shigeyoshi / Imanishi, Masayuki / Mori, Yusuke

    Urolithiasis

    2024  Volume 52, Issue 1, Page(s) 57

    Abstract: Calcium oxalate kidney stones, the most prevalent type of kidney stones, undergo a multi-step process of crystal nucleation, growth, aggregation, and secondary transition. The secondary transition has been rather overlooked, and thus, the effects on the ... ...

    Abstract Calcium oxalate kidney stones, the most prevalent type of kidney stones, undergo a multi-step process of crystal nucleation, growth, aggregation, and secondary transition. The secondary transition has been rather overlooked, and thus, the effects on the disease and the underlying mechanism remain unclear. Here, we show, by periodic micro-CT images of human kidney stones in an ex vivo incubation experiment, that the growth of porous aggregates of calcium oxalate dihydrate (COD) crystals triggers the hardening of the kidney stones that causes difficulty in lithotripsy of kidney stone disease in the secondary transition. This hardening was caused by the internal nucleation and growth of precise calcium oxalate monohydrate (COM) crystals from isolated urine in which the calcium oxalate concentrations decreased by the growth of COD in closed grain boundaries of COD aggregate kidney stones. Reducing the calcium oxalate concentrations in urine is regarded as a typical approach for avoiding the recurrence. However, our results revealed that the decrease of the concentrations in closed microenvironments conversely promotes the transition of the COD aggregates into hard COM aggregates. We anticipate that the suppression of the secondary transition has the potential to manage the deterioration of kidney stone disease.
    MeSH term(s) Humans ; Calcium Oxalate ; Hardness ; Kidney Calculi ; Body Fluids ; Lithotripsy
    Chemical Substances Calcium Oxalate (2612HC57YE)
    Language English
    Publishing date 2024-04-02
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2703553-0
    ISSN 2194-7236 ; 2194-7228
    ISSN (online) 2194-7236
    ISSN 2194-7228
    DOI 10.1007/s00240-024-01556-5
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    Zs.A 928: Show issues Location:
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