Language：English   Publishing type：Research paper (scientific journal)   Publisher：COMPANY OF BIOLOGISTS LTD  

beta-catenin regulates the transcription of genes involved in diverse biological processes, including embryogenesis, tissue homeostasis and regeneration. Endothelial cell (EC)-specific gene-targeting analyses in mice have revealed that Nr2f2-dependent is required for vascular development. However, the precise function of beta-catenin-mediated gene regulation in vascular development is not well understood, since beta-catenin regulates not only gene expression but also the formation of cell-cell junctions. To address this question, we have developed a novel transgenic zebrafish line that allows the visualization of beta-catenin transcriptional activity specifically in ECs and discovered that beta-catenin-dependent transcription is central to the bone morphogenetic protein (Bmp)-mediated formation of venous vessels. During caudal vein (CV) formation, Bmp induces the expression of aggf1, a putative causative gene for Klippel-Trenaunay syndrome, which is characterized by venous malformation and hypertrophy of bones and soft tissues. Subsequently, Aggf1 potentiates beta-catenin transcriptional activity by acting as a transcriptional co-factor, suggesting that Bmp evokes beta-catenin-mediated gene expression through Aggf1 expression. Bmp-mediated activation of beta-catenin induces the expression of Nr2f2 (also known as Coup-TFII), a member of the nuclear receptor superfamily, to promote the differentiation of venous ECs, thereby contributing to CV formation. Furthermore, beta-catenin stimulated by Bmp promotes the survival of venous ECs, but not that of arterial ECs. Collectively, these results indicate that Bmp-induced activation of beta-catenin through Aggf1 regulates CV development by promoting the Nr2f2-dependent differentiation of venous ECs and their survival. This study demonstrates, for the first time, a crucial role of beta-catenin-mediated gene expression in the development of venous vessels.

DOI： 10.1242/dev.115576

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：ACADEMIC PRESS INC ELSEVIER SCIENCE  

The formation of vascular structures requires precisely controlled proliferation of endothelial cells (ECs), which occurs through strict regulation of the cell cycle. However, the mechanism by which EC proliferation is coordinated during vascular formation remains largely unknown, since a method of analyzing cell-cycle progression of ECs in living animals has been lacking. Thus, we devised a novel system allowing the cell-cycle progression of ECs to be visualized in vivo. To achieve this aim, we generated a transgenic zebrafish line that expresses zFucci (zebrafish fluorescent ubiquitination-based cell cycle indicator) specifically in ECs (an EC-zFucci Tg line). We first assessed whether this system works by labeling the S phase ECs with EdU, then performing time-lapse imaging analyses and, finally, examining the effects of cell-cycle inhibitors. Employing the EC-zFucci Tg line, we analyzed the cell-cycle progression of ECs during vascular development in different regions and at different time points and found that ECs proliferate actively in the developing vasculature. The proliferation of ECs also contributes to the elongation of newly formed blood vessels. While ECs divide during elongation in intersegmental vessels, ECs proliferate in the primordial hindbrain channel to serve as an EC reservoir and migrate into basilar and central arteries, thereby contributing to new blood vessel formation. Furthermore, while EC proliferation is not essential for the formation of the basic framework structures of intersegmental and caudal vessels, it appears to be required for full maturation of these vessels. In addition, venous ECs mainly proliferate in the late stage of vascular development, whereas arterial ECs become quiescent at this stage. Thus, we anticipate that the EC-zFucci Tg line can serve as a tool for detailed studies of the proliferation of ECs in various forms of vascular development in vivo. (C) 2014 Elsevier Inc. All rights reserved.

DOI： 10.1016/j.ydbio.2014.06.015

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：ELSEVIER SCIENCE INC  

Thiamin pyrophosphokinase (TPK) converts thiamin to its active form, thiamin diphosphate. In humans, TPK expression is down-regulated in some thiamin deficiency related syndrome, and enhanced during pregnancy. Rainbow trout are also vulnerable to thiamin deficiency in wild life and are useful models for thiamin metabolism research. We identified the tpk gene transcript including seven splice variants in the rainbow trout. Almost all cell lines and tissues examined showed co-expression of several tpk splice variants including a potentially major one at both mRNA and protein levels. However, relative to other tissues, the longest variant mRNA expression was predominant in the ovary and abundant in embryos. During embryogenesis, total tpk transcripts increased abruptly in early development, and decreased to about half of the peak shortly after hatching. In rainbow trout, the tpk transcript complex is ubiquitously expressed for all tissues and cells examined, and its increase in expression could be important in the early-middle embryonic stages. Moreover, decimated tpk expression in a hepatoma cell line relative to hepatic and gonadal cell lines appears to be consistent with previously reported down-regulation of thiamin metabolism in cancer. (C) 2012 Elsevier Inc. All rights reserved.

DOI： 10.1016/j.cbpb.2012.05.017

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Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：ZOOLOGICAL SOC JAPAN  

Since the gene expression of guanylin peptides and their receptors, guanylyl cyclase Cs, is enhanced in the intestine of seawater (SW)-adapted eels compared with fresh water (FW)-adapted fish, the guanylin family may play an important role in SW adaptation in eels. The present study analyzed the effect of three homologous guanylin peptides, guanylin, uroguanylin and renoguanylin, on ion movement through the eel intestine, and examined the target of guanylin action using Ussing chambers. The middle and posterior parts of the intestine, where water and ion absorption occurs actively in SW eels, exhibited serosa-negative transepithelial potential, while the anterior intestine was serosa-positive. Mucosal application of each guanylin in the middle or posterior intestine reduced the short-circuit current (I-sc) dose dependently and reversed it at high doses, and reduced electric tissue resistance. The effects were greater in the middle intestine than in the posterior intestine. All three guanylins showed similar potency in the middle segment, but guanylin was more potent in the posterior segment. 8-bromo cGMP mimicked the effect of guanylins. The intestinal response to guanylin was smaller in FW eels. The mucosal presence of NPPB utilized as a CFTR blocker, but not of other inhibitors of the channels/transporters localized on the luminal surface in SW fish intestine, inhibited the guanylin-induced decrease in I-sc. In eels, therefore, the guanylin family may be involved in osmoregulation by the intestine by binding to the receptors and activating CFTR-like channels on the mucosal side through cGMP production, perhaps resulting in Cl- and HCO3- secretion into the lumen.

DOI： 10.2108/zsj.24.1222

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Authorship：Last author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：ACADEMIC PRESS INC ELSEVIER SCIENCE  

Guanylin and uroguanylin are principal intestinal hormones secreted into the lumen to regulate ion and water absorption via a specific receptor, guanylyl cyclase-C (GC-C). As the intestine is an essential organ for seawater (SW) adaptation in teleost fishes, the intestinal guanylin system may play a critical role in SW adaptation. Molecular biological studies identified multiple guanylins (guanylin, uroguanylin and renoguanylin) and their receptors (GC-C1 and GC-C2) in eels. The relative potency of the three ligands on cGMP production in transiently expressed receptors was uroguanylin > guanylin >= renoguanylin for CG-C1 and guanylin >= renoguany-fin > uroguanylin for GC-C2. Eel guanylin and GC-C genes are expressed exclusively in the intestine and kidney, and the level of expression is greater in SW eels than in freshwater (FW) eels except for renoguanylin. Physiological studies using Ussing chambers showed that the middle and posterior intestine are major sites of action of guanylins, where they act on the mucosal side to decrease short circuit current (I-sc) in a dose-dependent manner. The ID50 of guanylins for transport inhibition was 50-fold greater than that of atrial natriuretic peptide that acts from the serosal side as an endocrine hormone. However, only guanylins reversed Isc to levels below zero. Pharmacological analyses using various blockers showed that among transporters and channels localized on the intestinal cells of SW teleost fish, the cystic fibrosis transmembrane conductance regulator C-1 channel (CFTR) on the apical membrane is the major target of guanylins. Collectively, guanylins are synthesized locally in the intestine and secreted into the lumen to act on the GC-Cs in the apical membrane of eel intestinal cells. Then, intracellular cGMP production after ligand-receptor interaction activates CFTR and probably induces C-1 and/or HCO3- secretion into the lumen as suggested in mammals. The physiological significance of the anion secretion induced by the luminal guanylin/GC-C system on SW adaptation may rival or exceed that of the serosally derived natriuretic peptides in the euryhaline eel. (c) 2007 Elsevier Inc. All rights reserved.

DOI： 10.1016/j.ygcen.2007.05.005

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Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：ACADEMIC PRESS INC ELSEVIER SCIENCE  

Guanylyl cyclase C (GC-C) is a single transmembrane receptor for a family of intestinal hormones, guanylins. In the eel, we previously identified three guanylins, whose gene expression was enhanced in the intestine after transfer from fresh water to seawater. However, only limited information is available about the structure and function of their receptor(s). In the present study, we cloned full-length cDNAs encoding two isoforms of GC-C, named GC-C1 and GC-C2, from eel intestine, The predicted GC-C proteins consisted of extracellular ligand-binding domain, membrane-spanning domain, kinase-like domain and cyclase catalytic domain, in which GC-C-specific sequences were largely conserved. Phylogenetic analyses showed that the cloned membrane GCs are grouped with the GC-C of other vertebrates but not with GC-A and GC-B. However, eel GC-Cs appear to have undergone unique structural evolution compared with other GC-Cs. The three eel guanylins (guanylin, uroguanylin and renoguanylin), but not eel atrial natriuretic peptide, stimulated cGMP production dose-dependently in COS cells expressing either of the cloned cDNAs, providing functional support for assignment as eel guanylin receptors. The potency order for cGMP production was uroguanylin > guanylin >= renoguanylin for GC-C1; guanylin >= renoguanylin > uroguanylin for GC-C2. The distinctive ligand selectivity was consistent with the low homology (53%) of the extracellular domain of the two GC-Cs compared with that observed for other domains (74-90%). Both GC-C genes were expressed in the alimentary tract (esophagus, stomach and intestine) and kidney, and their expression was higher in the intestine of seawater-adapted eels than that of freshwater eels just as observed with the guanylin genes. However, the expression of the receptor genes was unchanged for 24 h after transfer of eels from fresh water to seawater or vice versa, showing slower response of the receptors to salinity changes than their ligands. Collectively, the multiple guanylin-GC-C system may be involved as a paracrine factor in seawater adaptation at the intestine and kidney of the eel. (c) 2006 Elsevier Inc. All rights reserved.

DOI： 10.1016/j.ygcen.2006.04.012

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Language：English  

The structure of ghrelin has been determined in the Japanese eel, Anguilla japonica. In this study, we identified immunoreactive ghrelin in extracts from plasma and stomach of the eel by radioimmunoassay (RIA) using an antiserum against octanoylated rat ghrelin [1-11]. Using the antiserum, we examined localization of ghrelin-immunopositive cells in the eel stomach. Detection of ghrelin mRNA-expressing cells was also attempted in the eel stomach using a cRNA probe specific for the eel ghrelin gene. Furthermore, we examined ghrelin expression patterns in plasma and stomach after transfer of freshwater (FW) eels to seawater (SW). Multiple types of immunoreactive ghrelin were detected using RIA. These were octanoylated eel ghrelin and other ghrelins that may have different fatty acid modifications, suggesting that this RIA can detect acylated ghrelin of eels as seen previously in the case of rat. Ghrelin-immunopositive cells were observed in the mucosal layer of the stomach, especially in the neck of the fundic gland. Ghrelin mRNA-expressing cells showed similar distribution and characteristics to the immunopositive cells. Plasma ghrelin levels in FW eels starved for one week before experimentation were approximately 40 fmol/ml. Plasma ghrelin levels in control-transferred FW eels did not change for 7 days, but significantly increased on day 14. Plasma ghrelin levels transiently increased fivefold 6h after SW transfer and then declined to the FW level by 24h after transfer. Ghrelin content and ghrelin mRNA levels in the stomach did not change after SW transfer, except for a transient decrease in ghrelin content seen 24h after transfer. The present results suggest that ghrelin may participate in osmoregulation in eels.

DOI： 10.1016/j.ygcen.2006.04.010

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：WILEY-BLACKWELL  

Fish endocrinologists are commonly motivated to pursue their research driven by their own interests in these aquatic animals. However, the data obtained in fish studies not only satisfy their own interests but often contribute more generally to the studies of other vertebrates, including mammals. The life of fishes is characterized by the aquatic habitat, which demands many physiological adjustments distinct from the terrestrial life. Among them, body fluid regulation is of particular importance as the body fluids are exposed to media of varying salinities only across the thin respiratory epithelia of the gills. Endocrine systems play pivotal roles in the homeostatic control of body fluid balance. Judging from the habitat-dependent control mechanisms, some osmoregulatory hormones of fish should have undergone functional. and molecular evolution during the ecological transition to the terrestrial life. In fact, water-regulating hormones such as vasopressin are essential for survival on the land, whereas ion-regulating hormones such as natriuretic peptides, guanylins and adrenomedullins are diversified and exhibit more critical functions in aquatic species. In this short review, we introduce some examples illustrating how comparative fish studies contribute to general endocrinology by taking advantage of such differences between fishes and tetrapods. In a functional context, fish studies often afford a deeper understanding of the essential actions of a hormone across vertebrate taxa. Using the natriuretic peptide family as an example, we suggest that more functional studies on fishes will bring similar rewards of understanding. At the molecular level, recent establishment of genome databases in fishes and mammals brings clues to the evolutionary history of hormone molecules via a comparative genomic approach. Because of the functional and molecular diversification of ion-regulating hormones in fishes, this approach sometimes leads to the discovery of new hormones in tetrapods as exemplified by adrenomedullin 2.

DOI： 10.1002/jez.a.309

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：OXFORD UNIV PRESS  

Natriuretic peptides (NPs) are a group of hormones playing important roles in cardiovascular and osmoregulatory systems in vertebrates. Among the NP subtypes, atrial NP (ANP), B-type NP (BNP), and ventricular NP (VNP) are circulating hormones expressed exclusively in the heart (cardiac NPs). The constitution of cardiac NPs is variable among species of vertebrates. In order to understand the evolutionary and functional significance of such variation, we performed a systematic survey of cardiac NP cDNAs in nine taxonomically diverse teleosts inhabiting environments of varying salinity. The discovery of the coexistence of the ANP, BNP, and VNP genes in the eel and rainbow trout suggested that the ancestral teleost had all three cardiac NPs. As the VNP cDNA was undetectable in ayu and six species of Neoteleostei, it is possible that VNP was lost before the divergence of Osmeroidei. The ANP gene was also undetectable in the medaka. Thus, only the BNP gene is universal in species examined in the present study. Synthetic medaka BNP preferentially activated two medaka GC-A-type receptors, suggesting that the three cardiac NPs share the same receptor. However, the regulation of BNP expression may be the most strict because ATTTA repeats in the 3'-untranslated region and the dibasic motif in the ring are conserved among teleosts and tetrapods. Linkage analyses in the rainbow trout located ANP, BNP, and VNP genes on the same chromosome, which suggested the generation of the VNP gene by tandem duplication as observed with ANP and BNP genes. If the duplication occurred before the divergence of tetrapods and teleosts, VNP may exist in the tetrapod lineage.

DOI： 10.1093/molbev/msi243

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：ELSEVIER SCIENCE INC  

Atrial and B-type natriuretic peptide (ANP and BNP) are cardiac hormones synthesized and secreted by the myoendocrine cells of the heart. They exert potent actions on body fluid balance. Since various body organs including the heart are under high physiological stress during water and food deprivation in the desert nomads, we intended to perform molecular biological and histological studies of ANP in the heart of the dromedary camel Camelus dronzedarius. Initially, we isolated cDNAs encoding ANP from the atrium and BNP from the atrium and ventricle of the dromedary camel. Putative mature ANP, deduced from the cDNA sequence, was identical to that of human and pig ANP, but the putative mature BNP was more diverse and was most similar to pig BNP (94% identity). Thus, we used antisera raised against human ANP that did not cross-react with pig BNP in the subsequent immunohistochemical studies. The ANP-expressing myoendocrine cells are most concentrated in the right atrium, to a lesser extent in the left atrium, and almost absent in the left ventricle. The immuno-positive cells are scattered uniformly in each region and are characterized by the presence of immunoreactive granular deposits around the nucleus. The left atrium comprises some ramifications of conductive cells (Purkinje fibers), some of which also contained ANP-immunoreactive granules. At the electron microscopic level, myoendocrine cells possessed secretory granules primarily in the perinuclear zone and a well-developed Golgi apparatus. The present study is the first comprehensive report dealing with the molecular cloning and immunohistochemical localization of ANP in the heart of a desert dwelling mammal. (C) 2004 Elsevier Inc. All rights reserved.

DOI： 10.1016/j.cbpb.2004.05.009

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Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC  

As the intestine is an essential organ for fish osmoregulation, the intestinal hormone guanylins may perform major functions, especially in euryhaline fish such as eels and salmonids. From the intestine of an eel, we identified cDNAs encoding three distinct guanylin- like peptides. Based on the sequence of mature peptide and sites of production, we named them guanylin, uroguanylin, and renoguanylin. Renoguanylin is a novel peptide that possesses the characteristics of both guanylin and uroguanylin and was abundantly expressed in the kidney. By immunohistochemistry, guanylin was localized exclusively in goblet cells, but not enterochromaffin cells, of the intestine. After transfer of eels from fresh water to seawater, mRNA expression of guanylin and uroguanylin did not change for 3 h, but it increased after 24 h. The increase was profound ( 2 - 6- fold) after adaptation to seawater. The expression of uroguanylin was also up- regulated in the kidney of seawater- adapted eels, but that of renoguanylin was not so prominent as other guanylins in both intestine and kidney. Collectively, the novel eel guanylin family appears to have important functions for seawater adaptation, particularly long- term adaptation. Eel guanylin may be secreted from goblet cells into the lumen with mucus in response to increased luminal osmolality and act on the epithelium to regulate water and salt absorption.

DOI： 10.1074/jbc.M303111200

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Authorship：Lead author   Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

CiNii Books

J-GLOBAL

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Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

J-GLOBAL

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Event date： 2020.9

Language：Japanese   Presentation type：Symposium, workshop panel (nominated)  

Venue：Web   Country：Japan  

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Event date： 2019.12

Language：Japanese   Presentation type：Symposium, workshop panel (nominated)  

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Language：English   Presentation type：Oral presentation (general)  

Venue：Boston Park Plaza Hotel, Boston, USA  

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Language：Japanese   Presentation type：Oral presentation (invited, special)  

Venue：Pacifico Yokohama, Yokohama, Japan  

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Language：Japanese   Presentation type：Poster presentation  

Venue：東京（日本医科大学 橘桜会館）  

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Language：Japanese   Presentation type：Oral presentation (invited, special)  

Venue：Osaka International House Foundation, Osaka, Japan  

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Language：English   Presentation type：Oral presentation (general)  

Venue：Hilton San Francisco Union Square, San Francisco, CA, USA  

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Event date： 2023.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：Korimoto campus in Kagoshima University (Kagoshima)   Country：Japan  

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Event date： 2022.10

Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

Venue：Michigan State University in East Lansing, MI, USA   Country：United States  

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Event date： 2022.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：Sendagi in Nippon Medical School   Country：Japan  

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Event date： 2022.7

Language：Japanese   Presentation type：Oral presentation (general)  

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Event date： 2022.7

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：Web   Country：Japan  

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Event date： 2021.9

Language：English   Presentation type：Oral presentation (general)  

Venue：Web (Osaka)   Country：Japan  

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Event date： 2019.12

Language：Japanese   Presentation type：Poster presentation  

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Language：Japanese   Presentation type：Poster presentation  

Venue：Epochal Tsukuba, Ibaragi, Japan  

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Language：Japanese   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

Venue：I-AMS in Nippon Medical School, Kawasaki, Japan  

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Language：Japanese   Presentation type：Oral presentation (general)  

Venue：Toyama Prefectural Civic Center, Toyama, Japan  

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Language：Japanese   Presentation type：Poster presentation  

Venue：Sheraton Kobe Bay Hotel & Towers, Kobe, Japan  

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Language：Japanese   Presentation type：Poster presentation  

Venue：Sendai International Center, Sendai, Japan  

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Language：Japanese   Presentation type：Oral presentation (general)  

Venue：Ishikawa Ongakudo and others, Kanazawa, Japan  

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Language：Japanese   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

Venue：I-AMS in Nippon Medical School, Kawasaki, Japan  

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Language：English   Presentation type：Poster presentation  

Venue：Kumamoto Kenmin Koryu Kaikan-Parea, Kumamoto, Japan  

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Language：Japanese   Presentation type：Symposium, workshop panel (nominated)  

Venue：Tokyo Medical and Dental University, Tokyo, Japan  

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Language：Japanese   Presentation type：Oral presentation (invited, special)  

Venue：Tokyo Dome Hotel, Tokyo, Japan  

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Language：Japanese   Presentation type：Poster presentation  

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Language：Japanese   Presentation type：Poster presentation  

Venue：岡山  

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Language：English   Presentation type：Poster presentation  

Venue：Salve Regina University, Newport, RI, USA  

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Language：English   Presentation type：Poster presentation  

Venue：Hyatt Regency Baltimore Inner Harbor, Baltimore, MD, USA  

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Language：Japanese   Presentation type：Poster presentation  

Venue：川崎（日本医科大学先端医学研究所）  

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Language：Japanese   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

Venue：Hongo Campus, University of Tokyo, Tokyo, Japan  

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Language：English   Presentation type：Poster presentation  

Venue：Miyazaki Convention Center Summit, Miyazaki, Japan  

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Language：English   Presentation type：Oral presentation (general)  

Venue：Nara-ken New Public Hall, Nara, Japan  

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Language：English   Presentation type：Poster presentation  

Venue：Institute of Zoology, Academia Sinica, Taipei, Taiwan  

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Language：Japanese   Presentation type：Oral presentation (general)  

Venue：Nakano Sunplaza, Nakano, Tokyo, Japan  

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Language：English   Presentation type：Poster presentation  

Venue：Yayoi Auditorium, University of Tokyo, Tokyo, Japan  

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Language：English   Presentation type：Poster presentation  

Venue：La Trobe University, Mt. Buller, Australia  

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Language：Japanese   Presentation type：Poster presentation  

Venue：Okayama Civic Hall, Okayama, Japan  

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Language：English   Presentation type：Poster presentation  

Venue：Zhongshan University, Guangzhou, China  

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Language：Japanese   Presentation type：Poster presentation  

Venue：Waseda University, Tokyo, Japan  

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Language：Japanese   Presentation type：Poster presentation  

Venue：Kyushu Sangyo University, Hukuoka, Japan  

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Language：English   Presentation type：Oral presentation (general)  

Venue：Weber’s Inn, Ann Arbor, MI, USA  

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Language：Japanese   Presentation type：Oral presentation (general)  

Venue：Osaka University at Toyonaka, Osaka, Japan  

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Language：English   Presentation type：Oral presentation (general)  

Venue：Monona Terrace Community and Convention Center, Madison, WI, USA  

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Language：English   Presentation type：Oral presentation (general)  

Venue：Weber’s Inn, Ann Arbor, MI, USA  

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Language：English   Presentation type：Symposium, workshop panel (nominated)  

Venue：University of Calgary, Calgary, Alberta, Canada  

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Language：English   Presentation type：Symposium, workshop panel (nominated)  

Venue：The administrative building, National Taiwan Ocean University (NTOU), Keelung, Taiwan  

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Language：English   Presentation type：Poster presentation  

Venue：the Renold Building, University of Manchester, Manchester, UK  

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Language：English   Presentation type：Oral presentation (general)  

Venue：National Museum of Emerging Science and Innovation, Tokyo, Japan  

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