Shin'ichiro Yamamoto
| Faculty of Pharmaceutical Sciences,Department of Pharmaceutical Sciences | Associate Professor |
Last Updated :2025/10/07
■Researcher basic information
Field Of Study
■Career
Career
- Apr. 2018 - Present
Teikyo Heisei University, Faculty of Pharmaceutical Sciences - Sep. 2015 - Mar. 2018
Teikyo Heisei University, Faculty of Pharmaceutical Sciences - Apr. 2014 - Aug. 2015
The University of Tokushima, Faculty of Pharmaceutical Sciences - Apr. 2009 - Mar. 2014
Kyoto University, Faculty of Pharmaceutical Sciences
Educational Background
■Research activity information
Paper
- Dynamic remodeling of TRPC5 channel-caveolin-1-eNOS protein assembly potentiates the positive feedback interaction between Ca2+ and NO signals.
Reiko Sakaguchi; Nobuaki Takahashi; Takashi Yoshida; Nozomi Ogawa; Yoshifumi Ueda; Satoshi Hamano; Kaori Yamaguchi; Seishiro Sawamura; Shinichiro Yamamoto; Yuji Hara; Tomoya Kawamoto; Ryosuke Suzuki; Akito Nakao; Masayuki X Mori; Tetsushi Furukawa; Shunichi Shimizu; Ryuji Inoue; Yasuo Mori
The Journal of biological chemistry, 21 Aug. 2024, [Reviewed]
The cell signaling molecules nitric oxide (NO) and Ca2+ regulate diverse biological processes through their closely coordinated activities directed by signaling protein complexes. However, it remains unclear how dynamically the multi-component protein assemblies behave within the signaling complexes upon the interplay between NO and Ca2+ signals. Here we demonstrate that TRPC5 channels activated by stimulation of G-protein-coupled ATP receptors mediate Ca2+ influx, that triggers NO production from endothelial NO synthase (eNOS), inducing secondary activation of TRPC5 via cysteine S-nitrosylation and eNOS in vascular endothelial cells. Mutations in the caveolin-1-binding domains of TRPC5 disrupt its association with caveolin-1 and impair Ca2+ influx and NO production, suggesting that caveolin-1 serves primarily as the scaffold for TRPC5 and eNOS to assemble into the signal complex. Interestingly, during ATP receptor activation, eNOS is dissociated from caveolin-1 and in turn directly associates with TRPC5, which accumulates at the plasma membrane dependently on Ca2+ influx and calmodulin (CaM). This protein reassembly likely results in a relief of eNOS from the inhibitory action of caveolin-1 and an enhanced TRPC5 S-nitrosylation by eNOS localized in the proximity, thereby facilitating the secondary activation of Ca2+ influx and NO production. In isolated rat aorta, vasodilation induced by acetylcholine was significantly suppressed by the TRPC5 inhibitor AC1903. Thus, our study provides evidence that dynamic remodeling of the protein assemblies among TRPC5, eNOS, caveolin-1, and CaM determines the ensemble of Ca2+ mobilization and NO production in vascular endothelial cells. - Mouse transient receptor potential melastatin 2 (TRPM2) isoform 7 attenuates full-length mouse TRPM2 activity through reductions in its expression by targeting it to ER-associated degradation.
Shinichiro Yamamoto; Naoto Kiyatake; Akihiro Kaneko; Masanao Shimamura; Takashi Yoshida; Shunichi Shimizu
Genes to cells : devoted to molecular & cellular mechanisms, Mar. 2024, [Reviewed]
Transient receptor potential melastatin 2 (TRPM2) assembles into tetramers to function as an oxidative stress-sensitive Ca2+ channel at the surface membrane. Limited information is currently available on the 10 protein isoforms of mouse TRPM2 (mTRPM2) identified. This study investigated whether these isoforms function as Ca2+ channels and examined their effects on full-length mTRPM2 activity using the HEK 293 cell exogenous expression system. Only full-length mTRPM2, isoform 1 localized to the surface membrane and was activated by oxidative stress. Isoform 7 was clearly recognized by protein quality control systems and degraded by endoplasmic reticulum-associated degradation after transmembrane proteolysis. In the co-expression system, the activation and expression of full-length mTRPM2 were attenuated by its co-expression with isoform 7, but not with the other isoforms. This decrease in the expression of full-length mTRPM2 was recovered by the proteasomal inhibitor. The present results suggest that isoforms other than isoform 1 did not function as oxidative stress-sensitive channels and also that only isoform 7 attenuated the activation of full-length mTRPM2 by targeting it to endoplasmic reticulum-associated degradation. The present study will provide important information on the functional nature of mTRPM2 isoforms for the elucidation of their roles in physiological and patho-physiological responses in vivo using mouse models. - Possible involvement of TRPM2 activation in 5-fluorouracil-induced myelosuppression in mice
Masaaki Ishibashi; Masakazu Ishii; Shinichiro Yamamoto; Yasuo Mori; Shunichi Shimizu
European Journal of Pharmacology, Jan. 2021, [Reviewed] - Functional maintenance of calcium store by ShcB adaptor protein in cerebellar Purkinje cells.
Sho Kakizawa; Yasushi Kishimoto; Shinichiro Yamamoto; Kazuko Onga; Kunihiko Yasuda; Yoshiaki Miyamoto; Masahiko Watanabe; Ryuichi Sakai; Nozomu Mori
Scientific reports, 02 Sep. 2020, [Reviewed]
Intracellular Ca2+ levels are changed by influx from extracellular medium and release from intracellular stores. In the central nervous systems, Ca2+ release is involved in various physiological events, such as neuronal excitability and transmitter release. Although stable Ca2+ release in response to stimulus is critical for proper functions of the nervous systems, regulatory mechanisms relating to Ca2+ release are not fully understood in central neurons. Here, we demonstrate that ShcB, an adaptor protein expressed in central neurons, has an essential role in functional maintenance of Ca2+ store in cerebellar Purkinje cells (PCs). ShcB-knockout (KO) mice showed defects in cerebellar-dependent motor function and long-term depression (LTD) at cerebellar synapse. The reduced LTD was accompanied with an impairment of intracellular Ca2+ release. Although the expression of Ca2+ release channels and morphology of Ca2+ store looked intact, content of intracellular Ca2+ store and activity of sarco/endoplasmic reticular Ca2+-ATPase (SERCA) were largely decreased in the ShcB-deficient cerebellum. Furthermore, when ShcB was ectopically expressed in the ShcB-KO PCs, the Ca2+ release and its SERCA-dependent component were restored. These data indicate that ShcB plays a key role in the functional maintenance of ER Ca2+ store in central neurons through regulation of SERCA activity. - Short TRPM2 prevents the targeting of full-length TRPM2 to the surface transmembrane by hijacking to ER associated degradation.
Shinichiro Yamamoto; Takahiro Ishii; Ryota Mikami; Tomohiro Numata; Shunichi Shimizu
Biochemical and biophysical research communications, Dec. 2019, [Reviewed]
Membrane proteins are targeted to the surface transmembrane after folding and assembling in the endoplasmic reticulum (ER). Misfolded- and unassembled-proteins are degraded by proteasomes following ubiquitination, termed ER-associated degradation (ERAD). Transient receptor potential melastatin 2 (TRPM2) is an oxidative stress-sensitive channel. One of the TRPM2 splicing variants, short TRPM2 (TRPM2-S) having only the N-terminus and first two transmembrane domains, was reported to prevent full-length TRPM2 (TRPM2-L) activation. Although TRPM2-S interacts with TRPM2-L, the inhibitory mechanisms of TRPM2-S are unclear. We found that TRPM2-S prevents transmembrane expression of TRPM2-L by targeting ERAD. TRPM2-S expression was lower than that of TRPM2-L, and was increased by an ERAD inhibitor. TRPM2-S was not expressed at the transmembrane. This suggests that TRPM2-S is a substrate for ERAD. Upon the simultaneous expression of TRPM2-S, the transmembrane expression of TRPM2-L was attenuated and the poly-ubiquitination of TRPM2-L was facilitated. Our study may clarify why TRPM2-S inhibits oxidative stress-induced TRPM2-L activation. - Protective Effects of Duloxetine against Cerebral Ischemia-Reperfusion Injury via Transient Receptor Potential Melastatin 2 Inhibition.
Takahiro Toda; Shinichiro Yamamoto; Noriko Umehara; Yasuo Mori; Minoru Wakamori; Shunichi Shimizu
The Journal of pharmacology and experimental therapeutics, Feb. 2019, [Reviewed]
Activation of transient receptor potential melastatin 2 (TRPM2), an oxidative stress-sensitive Ca2+-permeable channel, contributes to the aggravation of cerebral ischemia-reperfusion (CIR) injury. Recent studies indicated that treatment with the antidepressant duloxetine for 24 hours (long term) attenuates TRPM2 activation in response to oxidative stress in neuronal cells. To examine the direct effects of antidepressants on TRPM2 activation, we examined their short-term (0-30 minutes) treatment effects on H2O2-induced TRPM2 activation in TRPM2-expressing human embryonic kidney 293 cells using the Ca2+ indicator fura-2. Duloxetine exerted the strongest inhibitory effects on TRPM2 activation among the seven antidepressants tested. These inhibitory effects appeared to be due to the inhibition of H2O2-induced TRPM2 activation via an open-channel blocking-like mechanism, because duloxetine reduced the sustained phase but not the initial phase of increases in intracellular Ca2+ concentrations. In a whole-cell patch-clamp study, duloxetine reduced the TRPM2-mediated inward current during the channel opening state. We also examined the effects of duloxetine in a mouse model of CIR injury. The administration of duloxetine to wild-type mice attenuated CIR injury, similar to that in Trpm2 knockout (KO) mice. The administration of duloxetine did not reduce CIR injury further in Trpm2 KO mice, suggesting that it exerts neuroprotective effects against CIR injury by inhibiting TRPM2 activation. Regarding drug repositioning, duloxetine may be a useful drug in reperfusion therapy for ischemic stroke because it has already been used clinically in therapeutics for several disorders, including depression. - Tyrphostin AG-related compounds attenuate H2O2-induced TRPM2-dependent and -independent cellular responses.
Shinichiro Yamamoto; Takahiro Toda; Ryo Yonezawa; Takaharu Negoro; Shunichi Shimizu
Journal of pharmacological sciences, May 2017, [Reviewed] - Significance of TRP channels in oxidative stress.
Shinichiro Yamamoto; Shunichi Shimizu
European journal of pharmacology, 15 Dec. 2016, [Reviewed] - Targeting TRPM2 in ROS-Coupled Diseases.
Shinichiro Yamamoto; Shunichi Shimizu
Pharmaceuticals (Basel, Switzerland), 07 Sep. 2016, [Reviewed] - Inhibitory effects of Tyrphostin AG-related compounds on oxidative stress-sensitive transient receptor potential channel activation.
Takahiro Toda; Shinichiro Yamamoto; Ryo Yonezawa; Yasuo Mori; Shunichi Shimizu
European journal of pharmacology, 05 Sep. 2016, [Reviewed] - TRPM2 channels in alveolar epithelial cells mediate bleomycin-induced lung inflammation.
Ryo Yonezawa; Shinichiro Yamamoto; Miki Takenaka; Yukiko Kage; Takaharu Negoro; Takahiro Toda; Masayuki Ohbayashi; Tomohiro Numata; Yasuko Nakano; Toshinori Yamamoto; Yasuo Mori; Masakazu Ishii; Shunichi Shimizu
Free radical biology & medicine, Jan. 2016, [Reviewed] - Sensitization of H2O2-induced TRPM2 activation and subsequent interleukin-8 (CXCL8) production by intracellular Fe(2+) in human monocytic U937 cells.
Shunichi Shimizu; Ryo Yonezawa; Takaharu Negoro; Shinichiro Yamamoto; Tomohiro Numata; Masakazu Ishii; Yasuo Mori; Takahiro Toda
The international journal of biochemistry & cell biology, Nov. 2015, [Reviewed] - Prevention of aberrant protein aggregation by anchoring the molecular chaperone αB-crystallin to the endoplasmic reticulum.
Shinichiro Yamamoto; Arisa Yamashita; Naokatu Arakaki; Hisao Nemoto; Tetsuo Yamazaki
Biochemical and biophysical research communications, 12 Dec. 2014, [Reviewed] - Contribution of calumin to embryogenesis through participation in the endoplasmic reticulum-associated degradation activity.
Shinichiro Yamamoto; Tetsuo Yamazaki; Shinji Komazaki; Takeshi Yamashita; Masako Osaki; Masaya Matsubayashi; Hiroyasu Kidoya; Nobuyuki Takakura; Daiju Yamazaki; Sho Kakizawa
Developmental biology, 01 Sep. 2014, [Reviewed] - TRIM50 protein regulates vesicular trafficking for acid secretion in gastric parietal cells.
Miyuki Nishi; Fumiyo Aoyama; Fumihiko Kisa; Hua Zhu; Mingzhai Sun; Peihui Lin; Hiroya Ohta; Bo Van; Shinichiro Yamamoto; Sho Kakizawa; Hideki Sakai; Jianjie Ma; Akira Sawaguchi; Hiroshi Takeshima
The Journal of biological chemistry, 28 Sep. 2012, [Reviewed] - The juvenile myoclonic epilepsy-related protein EFHC1 interacts with the redox-sensitive TRPM2 channel linked to cell death.
Masahiro Katano; Tomohiro Numata; Kripamoy Aguan; Yuji Hara; Shigeki Kiyonaka; Shinichiro Yamamoto; Takafumi Miki; Seishiro Sawamura; Toshimitsu Suzuki; Kazuhiro Yamakawa; Yasuo Mori
Cell calcium, Feb. 2012, [Reviewed] - TRPA1 underlies a sensing mechanism for O2.
Nobuaki Takahashi; Tomoyuki Kuwaki; Shigeki Kiyonaka; Tomohiro Numata; Daisuke Kozai; Yusuke Mizuno; Shinichiro Yamamoto; Shinji Naito; Ellen Knevels; Peter Carmeliet; Toru Oga; Shuji Kaneko; Seiji Suga; Toshiki Nokami; Jun-ichi Yoshida; Yasuo Mori
Nature chemical biology, 28 Aug. 2011, [Reviewed] - TRIC-A channels in vascular smooth muscle contribute to blood pressure maintenance.
Daiju Yamazaki; Yasuharu Tabara; Satomi Kita; Hironori Hanada; Shinji Komazaki; Daisuke Naitou; Aya Mishima; Miyuki Nishi; Hisao Yamamura; Shinichiro Yamamoto; Sho Kakizawa; Hitoshi Miyachi; Shintaro Yamamoto; Toshiyuki Miyata; Yuhei Kawano; Kei Kamide; Toshio Ogihara; Akira Hata; Satoshi Umemura; Masayoshi Soma; Norio Takahashi; Yuji Imaizumi; Tetsuro Miki; Takahiro Iwamoto; Hiroshi Takeshima
Cell metabolism, 03 Aug. 2011, [Reviewed] - [Function of TRPM2 as a Ca(2+)-release channel in β cells].
Yamamoto S; Mori Y
Nihon yakurigaku zasshi. Folia pharmacologica Japonica, May 2011, [Invited] - Chemical physiology of oxidative stress-activated TRPM2 and TRPC5 channels
Shinichiro Yamamoto; Nobuaki Takahashi; Yasuo Mori
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, Sep. 2010, [Reviewed] - [TRIC (trimeric intracellular cation)-channel functions during Ca(2+) release from the sarco/endoplasmic reticulum].
Yamazaki D; Yamamoto S; Takeshima H
Nihon yakurigaku zasshi. Folia pharmacologica Japonica, Mar. 2010, [Invited] - Involvement of TRPM2 channel in amplification of reactive oxygen species-induced signaling and chronic inflammation.
Yamamoto S; Shimizu S; Mori Y
Nihon yakurigaku zasshi. Folia pharmacologica Japonica, Sep. 2009, [Invited] - TRPM2 functions as a lysosomal Ca2+-release channel in β cells
Ingo Lange; Shinichiro Yamamoto; Santiago Partida-Sanchez; Yasuo Mori; Andrea Fleig; Reinhold Penner
Science Signaling, 19 May 2009, [Reviewed] - [Ion channels responsible for environmental response: molecular function of TRP channels activated by reactive chemical species].
Yamamoto S; Takahashi N; Kiyonaka S; Mori Y
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, Mar. 2009, [Invited] - Reactive oxygen species-induced signal amplification and chronic inflammation mediated by TRPM2 channels
Yasuo Mori; Shinichiro Yamamoto; Shigeki Kiyonaka; Nobuaki Takahashi; Yuji Kiuchi; Shunichi Shimizu
JOURNAL OF PHARMACOLOGICAL SCIENCES, 2009, [Invited] - Structures and variable functions of TRP channels
Tomohiro Numata; Daisuke Kozai; Nobuaki Takahashj; Kenta Kato; Yoshitsugu Uriu; Shinichiro Yamamoto; Takeshi Kaneko; Tatsuo Shinmoto; Yasuo Mori
Seikagaku, 2009, [Reviewed] - TRPM2-mediated Ca(2+) influx induces chemokine production in monocytes that aggravates inflammatory neutrophil infiltration
Shinichiro Yamamoto; Shunichi Shimizu; Shigeki Kiyonaka; Nobuaki Takahashi; Teruaki Wajima; Yuji Hara; Takaharu Negoro; Toshihito Hiroi; Yuji Kiuchi; Takaharu Okada; Shuji Kaneko; Ingo Lange; Andrea Fleig; Reinhold Penner; Miyuki Nishi; Hiroshi Takeshima; Yasuo Mori
NATURE MEDICINE, Jul. 2008, [Reviewed] - Molecular characterization of TRPA1 channel activation by cysteine-reactive inflammatory mediators
Nobuaki Takahashi; Yusuke Mizuno; Daisuke Kozai; Shinichiro Yamamoto; Shigeki Kiyonaka; Takahiro Shibata; Koji Uchida; Yasuo Mori
CHANNELS, Jul. 2008, [Reviewed] - Physiological role of the oxidative stress-sensitive activation of TRPM2 Ca2+ channels
Shinichiro Yamamoto; Shigeki Kiyonaka; Nobuaki Takahashi; Yasuo Mori
YAKUGAKU ZASSHI-JOURNAL OF THE PHARMACEUTICAL SOCIETY OF JAPAN, 2008 - Transient receptor potential channels in Alzheimer's disease.
Yamamoto S; Wajima T; Hara Y; Nishida M; Mori Y
Biochimica et biophysica acta, Aug. 2007, [Reviewed], [Invited] - Nitric oxide activates TRP channels by cysteine S-nitrosylation
Takashi Yoshida; Ryuji Inoue; Takashi Morii; Nobuaki Takahashi; Shinichiro Yamamoto; Yuji Hara; Makoto Tominaga; Shunichi Shimizu; Yoji Sato; Yasuo Mori
NATURE CHEMICAL BIOLOGY, Nov. 2006, [Reviewed] - Hydrogen peroxide stimulates tetrahydrobiopterin synthesis through the induction of GTP-cyclohydrolase I and increases nitric oxidesynthase activity in vascular endothelial cells
S Shimizu; K Shiota; S Yamamoto; Y Miyasaka; M Ishii; T Watabe; M Nishida; Y Mori; T Yamamoto; Y Kiuchi
FREE RADICAL BIOLOGY AND MEDICINE, May 2003, [Reviewed] - Stimulation of tetrahydrobioptenin synthesis by basic fibroblast growth factor in vascular endothelial cells
S Shimizu; Y Miyasaka; S Yamamoto; M Ishii; Y Kiuchi
PTERIDINES, Mar. 2003, [Reviewed] - Stimulation of tetrahydrobiopterin synthesis by cyclosporin A during lipopolysaccharide treatment in vascular endothelial cells
M Ishii; S Shimizu; K Shiota; S Yamamoto; Y Kiuchi; T Yamamoto
PTERIDINES, Sep. 2002, [Reviewed] - Stimulation of tetrahydrobiopterin synthesis by cyclosporin A in mouse brain microvascular endothelial cells
M Ishii; S Shimizu; K Shiota; S Yamamoto; Y Kiuchi; T Yamamoto
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, Sep. 2002, [Reviewed] - Hydrogen peroxide stimulates the LPS-induced tetrahydrobiopterin synthesis in mouse brain microvascular endothelial cells
K Shiota; S Shimizu; M Ishii; S Yamamoto; M Iwasaki; T Yamamoto; Y Kiuchi
PTERIDINES, Mar. 2002, [Reviewed]
MISC
- 肛門手術における塩酸キニーネ注射薬の検討
Jun. 2021 - Spatio-temporal regulation of intracellular Ca2+ and NO signaling by the TRPC5 channel complex
Nobuaki Takahashi; Takashi Yoshida; Shinichiro Yamamoto; Yoshifumi Ueda; Yasuo Mori
JOURNAL OF PHYSIOLOGICAL SCIENCES, 2013 - TRIC channel function in sarco/endoplasmic reticulum
Daiju Yamazaki; Shinichiro Yamamoto; Miyuki Nishi; Hiroshi Takeshima
JOURNAL OF PHYSIOLOGICAL SCIENCES, 2010 - FACILITATION OF TRPC5 CHANNEL BY CALCIUM
Minoru Wakamori; Takashi Yoshida; Shinichiro Yamamoto; Yasuo Mori
JOURNAL OF PHYSIOLOGICAL SCIENCES, 2009 - 15d-PGJ2, an inflammatory compound, activates TRPA1 channel via cysteine modification
Takahashi Nobuaki; Mizuno Yusuke; Yamamoto Shinichiro; Shibata Takahiro; Mori Yasuo
Proceedings of Annual Meeting of the Physiological Society of Japan, 2008
TRPA1 is a member of the Transient Receptor Potential (TRP) family of ion channels, and is expressed in sensory nerve endings of the pain pathway. It has been reported that TRPA1 is activated by a variety of noxious stimuli including pungent natural compounds and environmental irritants. However, it has been poorly reported that high-affinity endogenous ligands directly activate TRPA1. Here, we show that 15-deoxy-delta <SUP>12,14</SUP>-Prostaglandin J<SUB>2</SUB> (15d-PGJ<SUB>2</SUB>), an endogenous α, β-unsaturated ketone that is produced in inflammation, activates TRPA1. Ca<SUP>2+</SUP> imaging showed that 15d-PGJ<SUB>2</SUB> activates heterologously expressed TRPA1 in HEK293 cells with an apparent EC<SUB>50</SUB> of 890 nM. Site-directed mutagenesis studies and binding assay indicate that cytoplasmic N-terminal cysteines of the channel is involved in 15d-PGJ<SUB>2</SUB> activity on TRPA1. Our results indicate that 15d-PGJ<SUB>2</SUB>, an inflammatory compound, may directly activate TRPA1 in nervous system. <b>[J Physiol Sci. 2008;58 Suppl:S78]</b>, PHYSIOLOGICAL SOCIETY OF JAPAN - Physiological role of the oxidative stress-sensitive TRPM2 Ca2+ channel in immunocytes
Shinichiro Yamamoto; Shunichi Shimizu; Teruaki Wajima; Yasuo Mori
JOURNAL OF PHARMACOLOGICAL SCIENCES, 2007 - Nitric oxide activates TRP channels by cysteine S-nitrosylation
Takahashi Nobuaki; Yoshida Takashi; Yamamoto Shinichiro; Mori Yasuo
Proceedings of Annual Meeting of the Physiological Society of Japan, 2007
Intracellular Ca<SUP>2+</SUP> concentration elevation is essential for activation of Ca<SUP>2+</SUP>-dependent NO synthases (NOSs). However, molecular components eliciting this mechanism remain unclear. Here, we report a novel activation mechanism mediated by cysteine S-nitrosylation in transient receptor potential (TRP) channels. Recombinant TRPC5 and TRPV1, which are commonly classified as receptor-activated channel and thermosensor channel respectively, induce entry of Ca<SUP>2+</SUP> into cells in response to nitric oxide (NO). Labeling and functional assays using cysteine mutants, together with membrane sidedness in activating reactive disulfides, show that cytoplasmically accessible Cys553 and nearby Cys558 are nitrosylation sites mediating NO sensitivity in TRPC5. The responsive TRP proteins have conserved cysteines on the same N-terminal side of the pore region. Notably, nitrosylation of native TRPC5 upon G protein-coupled ATP receptor stimulation elicits entry of Ca<SUP>2+</SUP> into endothelial cells. These findings suggest that native TRPC5 is essential for Ca<SUP>2+</SUP> influx activated by NO via eNOS upon receptor stimulation in endothelial cells. Forthermore, the group of native S-nitrosylation-sensitive TRP channels mediates a ubiquitous mechanism that is critical for feedback regulation of Ca<SUP>2+</SUP> signals by NO. <b>[J Physiol Sci. 2007;57 Suppl:S224]</b>, PHYSIOLOGICAL SOCIETY OF JAPAN - Physiological role and activation mechanism of the oxidative stress-susceptible TRPM2 Ca2+ channel in immunocytes
S Yamamoto; S Shimizu; M Ishii; Y Hara; T Hagiwara; T Negoro; M Nishida; T Tobe; Y Kiuchi; Y Mori
JOURNAL OF PHARMACOLOGICAL SCIENCES, 2006 - Physiological role and activation mechanism of the oxidative stress-susceptible TRPM2 Ca2+ channel in immunocytes
S Yamamoto; S Shimizu; M Ishii; T Hagiwara; Y Hara; T Negoro; M Nishida; T Tobe; Y Kiuchi; Y Mori
JOURNAL OF PHARMACOLOGICAL SCIENCES, 2005 - U937におけるH2O2刺激によるTRPM2を介したCa2+流入のサイトカイン産生及びアポトーシス誘導に及ぼす影響
山本 伸一郎; 清水 俊一; 根来 孝治; 石井 正和; 原 雄二; 西田 基宏; 戸部 敞; 森 泰生; 木内 祐二
日本薬学会年会要旨集, Mar. 2004
(公社)日本薬学会 - Possible involvement of hydroxyl radical in H2O2-induced calcium influx through TRPM2 channel
M Ishii; Y Hara; S Yamamoto; Y Mori; S Shimizu; Y Kiuchi
JOURNAL OF PHARMACOLOGICAL SCIENCES, 2004 - Implication of Ca2+ entry through oxidative stress sensitive TRPM2 channel on IL-8 production by H2O2 in U937 cells
S Yamamoto; S Shimizu; T Negoro; M Ishii; Y Hara; M Nishida; T Tobe; Y Mori; Y Kiuchi
JOURNAL OF PHARMACOLOGICAL SCIENCES, 2004 - 血管内皮細胞におけるbFGFによるBH4合成の促進
宮坂 善之; 山本 伸一郎; 新本 里香; 石井 正和; 清水 俊一; 木内 祐二
日本薬学会年会要旨集, Mar. 2003
(公社)日本薬学会
Research Themes
- 糖尿病発症における小胞体ストレス誘導性カルシウムシグナリングの関与の解明
Apr. 2017 - Mar. 2020 - Conditional TRIC-B knockout mice production and functional analysis
Grant-in-Aid for Scientific Research (B)
National Institute of Health Sciences
Apr. 2015 - Mar. 2019
To investigate the TRIC-B function in various cells and tissues, we generated conditional TRIC-B deficient mice instead of conventional TRIC-B knockout mice which died immediately after birth due to impairement of pulmonary alveolous. First, we generated heart-specific TRIC-B deficient mice. Second, we generated mTRIC-B deficient ES cells and differntiated to the central nervous system cell lineage using with the neurosphere method. In heart-specific TRIC-B deficient mice, treatment of tamoxifen decreased gene expression of Tric-b in the heart. In addition, it was suggested that lack of TRIC-B may contribute to the differentiation process to the central nervous system cell lineage. - 極性細胞の脂質輸送におけるカルミンの役割の解明
Feb. 2012 - Mar. 2014 - Analysis for physiological role of the Ca2+-binding ER protein calumin
Grant-in-Aid for Young Scientists (B)
Kyoto University
Apr. 2010 - Mar. 2011
Calumin is transmembrane protein on endoplasmic reticulum. Although calumin knockout in mice is embryonic lethal around E10. 5-11. 5, the physiological role is no clear. Thus, we investigated the physiological role of calumin. Calumin is specifically expressed in yolk sac endoderm cells which are the principal nutrient-transporting cells. Additionally, lipid droplets are accumulated in calumin knockout yolk sac endoderm cells. Therefore, it was suggested that calumin was involved in lipid transport in endoderm cells.
