Updated on 2025/07/31

写真a

 
UCHIMOTO KAEDE
 
Organization
Academic Assembly Institute of Medicine and Dentistry IGAKU KEIRETU Assistant Professor
Graduate School of Medical and Dental Sciences Center of Nephrology Assistant Professor
Title
Assistant Professor
Homepage
http://www.med.niigata-u.ac.jp/nim/welcomej.html
Other name(s)
ZHANG Ying
External link

Degree

  • 医学博士 ( 2007.3   新潟大学 )

Research Interests

  • 腎臓病学

  • 実験病理学

Research Areas

  • Life Science / Nephrology

Research History (researchmap)

  • Niigata University   Graduate School of Medical and Dental Sciences Center of Nephrology   Assistant Professor

    2016.4

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  • Niigata University   Graduate School of Medical and Dental Sciences Institute of Nephrology   Assistant Professor

    2015.9 - 2016.3

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Research History

  • Niigata University   Faculty of Medicine Institute of Nephrology   Assistant Professor

    2016.4

  • Niigata University   Faculty of Medicine Institute of Nephrology   Assistant Professor

    2015.9 - 2016.3

Education

  • Niigata University   Graduate School, Division of Medical Sciences

    2003.4 - 2007.3

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    Country： Japan

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  • Harbin Medical University, China   Faculty of Medicine

    - 2002.8

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    Country： China

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Qualification acquired

  • International English Language Testing System

 

Papers

  • 14-3-3 Proteins stabilize actin and vimentin filaments to maintain processes in renal glomerular podocyte. International journal

    Hidenori Yasuda, Yoshiyasu Fukusumi, Ying Zhang, Hiroshi Kawachi

    FASEB journal : official publication of the Federation of American Societies for Experimental Biology   37 ( 10 )   e23168   2023.10

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    Language：English   Publishing type：Research paper (scientific journal)  

    14-3-3 proteins are a ubiquitously expressed family of adaptor proteins. Despite exhibiting high sequence homology, several 14-3-3 isoforms have isoform-specific binding partners and roles. We reported that 14-3-3β interacts with FKBP12 and synaptopodin to maintain the structure of actin fibers in podocytes. However, the precise localization and differential role of 14-3-3 isoforms in kidneys are unclear. Herein, we showed that 14-3-3β in glomeruli was restricted in podocytes, and 14-3-3σ in glomeruli was expressed in podocytes and mesangial cells. Although 14-3-3β was dominantly co-localized with FKBP12 in the foot processes, a part of 14-3-3β was co-localized with Par3 at the slit diaphragm. 14-3-3β interacted with Par3, and FKBP12 bound to 14-3-3β competitively with Par3. Deletion of 14-3-3β enhanced the interaction of Par3 with Par6 in podocytes. Gene silencing for 14-3-3β altered the structure of actin fibers and process formation. 14-3-3β and synaptopodin expression was decreased in podocyte injury models. In contrast, 14-3-3σ in podocytes was expressed in the primary processes. 14-3-3σ interacted with vimentin but not with the actin-associated proteins FKBP12 and synaptopodin. Gene silencing for 14-3-3σ altered the structure of vimentin fibers and process formation. 14-3-3σ and vimentin expression was increased in the early phase of podocyte injury models but was decreased in the late stage. Together, the localization of 14-3-3β at actin cytoskeleton plays a role in maintaining the foot processes and the Par complex in podocytes. In contrast, 14-3-3σ at vimentin cytoskeleton is essential for maintaining primary processes.

    DOI： 10.1096/fj.202300865R

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  • Podocyte injury in minimal change nephrotic syndrome

    Hiroshi Kawachi, Yoshiyasu Fukusumi, Kaede Uchimoto

    15 ( 6 )   644 - 651   2022.6

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  • Th17 Cells Participate in Thy1.1 Glomerulonephritis Which Is Ameliorated by Tacrolimus. Reviewed International journal

    Syuhei Watanabe, Ying Zhang, Yoshiyasu Fukusumi, Hidenori Yasuda, Akira Takada, Junichiro J Kazama, Hiroshi Kawachi

    American journal of nephrology   53 ( 5 )   388 - 396   2022

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    INTRODUCTION: Thy1.1 glomerulonephritis (Thy1.1 GN) in rats is widely used as an experimental model of mesangial proliferative glomerulonephritis (GN). We previously reported that T-helper (Th) cells were accumulated in glomeruli from the early phase of this model and that not Th2 cells but Th1 cells play an important role in the development of glomerular alterations. Although Th17 is reported to be involved in the pathogenesis of several autoimmune diseases, the role of Th17 cells in the pathogenesis of mesangial alterations in Thy1.1 GN remains unclear. METHODS: The kinetics of the infiltration of subsets of Th cells and the expression of IL-17 in Thy1.1 GN were analyzed. Next, the localization and the cell types of IL-17 receptor (IL-17R)-positive cells and IL-6-positive cells were analyzed. Then, the effect of tacrolimus on the expressions of Th17-related cytokines in Thy1.1 GN was analyzed. RESULTS: Not only Th1 cells but also Th17 cells were recruited into glomeruli from the early phase of the disease. mRNA expression of IL-17 in glomeruli was elevated. The increased positive expression of IL-17R was detected in the mesangial area, and some of IL-17R-positive cells were co-stained with IL-6. Tacrolimus treatment ameliorated mesangial alterations by suppressing the expressions of Th17-related cytokines such as IL-17 and IL-6. CONCLUSION: Th17 cells participate in the development of Thy1.1 GN, a mimic of mesangial proliferative GN, and Th17 cells and their related cytokines are pertinent therapeutic targets.

    DOI： 10.1159/000524111

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  • Tacrolimus ameliorates podocyte injury by restoring FK506 binding protein 12 (FKBP12) at actin cytoskeleton. Reviewed International journal

    Hidenori Yasuda, Yoshiyasu Fukusumi, Veniamin Ivanov, Ying Zhang, Hiroshi Kawachi

    FASEB journal : official publication of the Federation of American Societies for Experimental Biology   35 ( 11 )   e21983   2021.11

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    Language：English   Publishing type：Research paper (scientific journal)  

    FKBP12 was identified as a binding protein of tacrolimus (Tac). Tac binds to FKBP12 and exhibits immunosuppressive effects in T cells. Although it is reported that Tac treatment directly ameliorates the dysfunction of the podocyte in nephrotic syndrome, the precise pharmacological mechanism of Tac is not well understood yet. It is also known that FKBP12 functions independently of Tac. However, the localization and the physiological function of FKBP12 are not well elucidated. In this study, we observed that FKBP12 is highly expressed in glomeruli, and the FKBP12 in glomeruli is restricted in podocytes. FKBP12 in cultured podocytes was expressed along the actin cytoskeleton and associated with filamentous actin (F-actin). FKBP12 interacted with the actin-associated proteins 14-3-3 and synaptopodin. RNA silencing for FKBP12 reduced 14-3-3 expression, F-actin staining, and process formation in cultured podocytes. FKBP12 expression was decreased in the nephrotic model caused by adriamycin (ADR) and the cultured podocyte treated with ADR. The process formation was deteriorated in the podocytes treated with ADR. Tac treatment ameliorated these decreases. Tac treatment to the normal cells increased the expression of FKBP12 at F-actin in processes and enhanced process formation. Tac enhanced the interaction of FKBP12 with synaptopodin. These observations suggested that FKBP12 at actin cytoskeleton participates in the maintenance of processes, and Tac treatment ameliorates podocyte injury by restoring FKBP12 at actin cytoskeleton.

    DOI： 10.1096/fj.202101052R

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  • プライマリ―カルチャー樹立法

    内許玉楓, 河内裕

    腎と透析   91 ( 5 )   965 - 969   2021.11

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  • Synbindin Downregulation Participates in Slit Diaphragm Dysfunction. Reviewed International journal

    Veniamin Ivanov, Yoshiyasu Fukusumi, Ying Zhang, Hidenori Yasuda, Meiko Kitazawa, Hiroshi Kawachi

    American journal of nephrology   52 ( 8 )   1 - 10   2021.8

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    Language：English   Publishing type：Research paper (scientific journal)  

    INTRODUCTION: Synbindin, originally identified as a neuronal cytoplasmic molecule, was found in glomeruli. The cDNA subtractive hybridization technique showed the mRNA expression of synbindin in glomeruli was downregulated in puromycin aminonucleoside (PAN) nephropathy, a mimic of minimal-change nephrotic syndrome. METHODS: The expression of synbindin in podocytes was analyzed in normal rats and 2 types of rat nephrotic models, anti-nephrin antibody-induced nephropathy, a pure slit diaphragm injury model, and PAN nephropathy, by immunohistochemical analysis and RT-PCR techniques. To elucidate the function of synbindin, a gene silencing study with human cultured podocytes was performed. RESULTS: Synbindin was mainly expressed at the slit diaphragm area of glomerular epithelial cells (podocytes). In both nephrotic models, decreased mRNA expression and the altered staining of synbindin were already detected at the early phase when proteinuria and the altered staining of nephrin, a key molecule of slit diaphragm, were not detected yet. Synbindin staining was clearly reduced when severe proteinuria was observed. When the cultured podocytes were treated with siRNA for synbindin, the cell changed to a round shape, and filamentous actin structure was clearly altered. The expression of ephrin-B1, a transmembrane protein at slit diaphragm, was clearly lowered, and synaptic vesicle-associated protein 2B (SV2B) was upregulated in the synbindin knockdown cells. CONCLUSION: Synbindin participates in maintaining foot processes and slit diaphragm as a downstream molecule of SV2B-mediated vesicle transport. Synbindin downregulation participates in slit diaphragm dysfunction. Synbindin can be an early marker to detect podocyte injury.

    DOI： 10.1159/000517975

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  • Nephrin-Ephrin-B1-Na+/H+ Exchanger Regulatory Factor 2-Ezrin-Actin Axis Is Critical in Podocyte Injury. Reviewed International journal

    Yoshiyasu Fukusumi, Hidenori Yasuda, Ying Zhang, Hiroshi Kawachi

    The American journal of pathology   191 ( 7 )   1209 - 1226   2021.7

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    Ephrin-B1 is one of the critical components of the slit diaphragm of kidney glomerular podocyte. However, the precise function of ephrin-B1 is unclear. To clarify the function of ephrin-B1, ephrin-B1-associated molecules were studied. RNA-sequencing analysis suggested that Na+/H+ exchanger regulatory factor 2 (NHERF2), a scaffolding protein, is associated with ephrin-B1. NHERF2 was expressed at the apical area and the slit diaphragm, and interacted with the nephrin-ephrin-B1 complex at the slit diaphragm. The nephrin-ephrin-B1-NHERF2 complex interacted with ezrin bound to F-actin. NHERF2 bound ephrin-B1 via its first postsynaptic density protein-95/disks large/zonula occludens-1 domain, and podocalyxin via its second postsynaptic density protein-95/disks large/zonula occludens-1 domain. Both in vitro analyses with human embryonic kidney 293 cells and in vivo study with rat nephrotic model showed that stimulaiton of the slit diaphragm, phosphorylation of nephrin and ephrin-B1, and dephosphorylation of NHERF2 and ezrin, disrupted the linkages of ephrin-B1-NHERF2 and NHERF2-ezrin. It is conceivable that the linkage of nephrin-ephrin-B1-NHERF2-ezrin-actin is a novel critical axis in the podocytes. Ephrin-B1 phosphorylation also disrupted the linkage of an apical transmembrane protein, podocalyxin, with NHERF2-ezrin-actin. The phosphorylation of ephrin-B1 and the consequent dephosphorylation of NHERF2 are critical initiation events leading to podocyte injury.

    DOI： 10.1016/j.ajpath.2021.04.004

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  • Xanthine oxidoreductase inhibitor topiroxostat ameliorates podocyte injury by inhibiting the reduction of nephrin and podoplanin. Reviewed

    Ying Zhang, Yoshiyasu Fukusumi, Mutsumi Kayaba, Takashi Nakamura, Ryusuke Sakamoto, Naoki Ashizawa, Hiroshi Kawachi

    Nefrologia   41 ( 5 )   539 - 547   2021.3

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    Background
    Topiroxostat, an inhibitor of xanthine oxidoreductase (XOR) was shown to reduce urinary albumin excretion of hyperuricemic patients with chronic kidney disease. However, its pharmacological mechanism is not well understood. In this study, we examined the effects of topiroxostat on glomerular podocytes. Podocyte is characterized by foot process and a unique cell-cell junction slit diaphragm functioning as a final barrier to prevent proteinuria.

    Methods
    The effects of topiroxostat on the expressions of podocyte functional molecules were analysed in db/db mice, a diabetic nephropathy model, anti-nephrin antibody-induced rat podocyte injury model and cultured podocytes treated with adriamycin.

    Results
    Topiroxostat treatment ameliorated albuminuria in db/db mice. The expression of desmin, a podocyte injury marker was increased, and nephrin and podocin, key molecules of slit diaphragm, and podoplanin, an essential molecule in maintaining foot process were downregulated in db/db mice. Topiroxostat treatment prevented the alterations in the expressions of these molecules in db/db mice. XOR activity in kidney was increased in rats with anti-nephrin antibody-induced podocyte injury. Topiroxostat treatment reduced XOR activity and restored the decreased expression of nephrin, podocin and podoplanin in the podocyte injury. Furthermore, topiroxostat enhanced the expression of podoplanin in injured human cultured podocytes.

    Conclusions
    Podocyte injury was evident in db/db mice. Topiroxostat ameliorated albuminuria in diabetic nephropathy model by preventing podocyte injury. Increase of XOR activity in kidney contributes to development of podocyte injury caused by stimulation to slit diaphragm. Topiroxostat has an effect to stabilize slit diaphragm and foot processes by inhibiting the reduction of nephrin, podocin and podoplanin.

    DOI： 10.1016/j.nefroe.2021.11.007

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  • Partitioning-Defective-6-Ephrin-B1 Interaction Is Regulated by Nephrin-Mediated Signal and Is Crucial in Maintaining Slit Diaphragm of Podocyte. Reviewed International journal

    Sayuri Takamura, Yoshiyasu Fukusumi, Ying Zhang, Ichiei Narita, Hiroshi Kawachi

    The American journal of pathology   in press ( 2 )   333 - 346   2020.2

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    Ephrin-B1 plays a critical role at slit diaphragm. Partitioning-defective (Par)-6 is down-regulated in podocyte of ephrin-B1 knockout mouse, suggesting that Par-6 is associated with ephrin-B1. Par polarity complex, consisting of Par-6, Par-3, and atypical protein kinase C, is essential for tight junction formation. In this study, the expression of Par-6 was analyzed in the normal and nephrotic syndrome model rats, and the molecular association of Par-6, Par-3, ephrin-B1, and nephrin was assessed with the human embryonic kidney 293 cell expression system. Par-6 was concentrated at slit diaphragm. Par 6 interacted with ephrin-B1 but not with nephrin, and Par-3 interacted with nephrin but not with ephrin-B1. The complexes of Par-6-ephrin-B1 and Par-3-nephrin were linked via extracellular sites of ephrin-B1 and nephrin. The Par-6-ephrin-B1 complex was delinked from the Par-3-nephrin complex, and Par-6 and ephrin-B1 were clearly down-regulated already at early phase of nephrotic model. The alteration of Par-6/ephrin-B1 advanced that of Par-3/nephrin. Stimulation to nephrin phosphorylated not only nephrin but also ephrin-B1, and consequently inhibited the interaction between ephrin-B1 and Par-6. Par-6 appeared at presumptive podocyte of early developmental stage and moved to basal area at capillary loop stage to participate in slit diaphragm formation at the final stage. Par-6-ephrin-B1 interaction is crucial for formation and maintenance of slit diaphragm of podocyte.

    DOI： 10.1016/j.ajpath.2019.10.015

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  • Nephrin-binding Ephrin-B1 at the slit diaphragm controls podocyte function through the JNK pathway Reviewed International journal

    Yoshiyasu Fukusumi, Ying Zhang, Ryohei Yamagishi, Kanako Oda, Toru Watanabe, Katsuyuki Matsui, Hiroshi Kawachi

    Journal of the American Society of Nephrology   29 ( 5 )   1462 - 1474   2018.5

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：American Society of Nephrology  

    DOI： 10.1681/ASN.2017090993

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  • Cdc42 Activation in Antinephrin Antibody–Induced Nephropathy

    Ying Zhang, Yoshiyasu Fukusumi, Hidenori Yasuda, Guoqing Chang, Mutsumi Kayaba, Hiroshi Kawachi

    Journal of the American Society of Nephrology   2025.6

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1681/ASN.0000000728

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  • Cover Image

    Hidenori Yasuda, Yoshiyasu Fukusumi, Ying Zhang, Hiroshi Kawachi

    The FASEB Journal   2023.10

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    DOI： 10.1096/fsb2.23208

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  • Why are they missing? : Bioinformatics characterization of missing human proteins Reviewed

    Amr Elguoshy, Sameh Magdeldin, Bo Xu, Yoshitoshi Hirao, Ying Zhang, Naohiko Kinoshita, Yusuke Takisawa, Masaaki Nameta, Keiko Yamamoto, Ali El-Refy, Fawzy El-Fiky, Tadashi Yamamoto

    JOURNAL OF PROTEOMICS   149   7 - 14   2016.10

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    DOI： 10.1016/j.jprot.2016.08.005

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  • レニン-アンジオテンシン-アルドステロン系(RAAS)阻害薬 Reviewed

    河内裕, 福住好恭, 張瑩

    腎と透析   81 ( 1 )   2016.7

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  • Comprehensive data analysis of human ureter proteome. Reviewed

    Magdeldin S, Hirao Y, El Guoshy A, Xu B, Zhang Y, Fujinaka H, Yamamoto K, Yates JR, Yamamoto T

    Data Brief.   6   853 - 857   2016.2

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  • Avian Podocytes, Which Lack Nephrin, Use Adherens Junction Proteins at Intercellular Junctions Reviewed International journal

    Eishin Yaoita, Hiroko Nishimura, Masaaki Nameta, Yutaka Yoshida, Hiroki Takimoto, Hidehiko Fujinaka, Hiroshi Kawachi, Sameh Magdeldin, Ying Zhang, Bo Xu, Tomizo Oyama, Fujio Nakamura, Tadashi Yamamoto

    JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY   64 ( 1 )   67 - 76   2016.1

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1369/0022155415611708

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  • A proteomic glimpse into human ureter proteome Reviewed

    Sameh Magdeldin, Yoshitoshi Hirao, Amr Elguoshy, Bo Xu, Ying Zhang, Hidehiko Fujinaka, Keiko Yamamoto, John R. Yates, Tadashi Yamamoto

    PROTEOMICS   16 ( 1 )   80 - 84   2016.1

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1002/pmic.201500214

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  • Datasets from label-free quantitative proteomic analysis of human glomeruli with sclerotic lesions Reviewed

    Ying Zhang, Bo Xu, Naohiko Kinoshita, Yutaka Yoshida, Masayuki Tasaki, Hidehiko Fujinaka, Sameh Magdeldin, Eishin Yaoita, Tadashi Yamamoto

    Data in Brief   4   180 - 185   2015.9

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier Inc.  

    DOI： 10.1016/j.dib.2015.05.013

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  • Complementary Protein and Peptide OFFGEL Fractionation for High-Throughput Proteomic Analysis Reviewed

    Sameh Magdedin, Amr Elguoshy, Yutaka Yoshida, Yoshitoshi Hirao, Bo Xu, Ying Zhang, Keiko Yamamoto, Hiroki Takimoto, Hidehiko Fujinaka, Naohiko Kinoshita, Tadashi Yamamoto

    ANALYTICAL CHEMISTRY   87 ( 16 )   8481 - 8488   2015.8

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1021/acs.analchem.5b01911

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  • Unrestricted modification search reveals lysine methylation as major modification induced by tissue formalin fixation and paraffin embedding Reviewed

    Ying Zhang, Markus Muller, Bo Xu, Yutaka Yoshida, Oliver Horlacher, Frederic Nikitin, Samuel Garessus, Sameh Magdeldin, Naohiko Kinoshita, Hidehiko Fujinaka, Eishin Yaoita, Miki Hasegawa, Frederique Lisacek, Tadashi Yamamoto

    PROTEOMICS   15 ( 15 )   2568 - 2579   2015.8

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1002/pmic.201400454

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  • Label-free quantitative proteomic analysis reveals strong involvement of complement alternative and terminal pathways in human glomerular sclerotic lesions Reviewed

    Ying Zhang, Bo Xu, Naohiko Kinoshita, Yutaka Yoshida, Masayuki Tasaki, Hidehiko Fujinaka, Sameh Magdeldin, Eishin Yaoita, Tadashi Yamamoto

    JOURNAL OF PROTEOMICS   123   89 - 100   2015.6

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    DOI： 10.1016/j.jprot.2015.03.024

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  • The neXtProt knowledgebase on human proteins: current status Reviewed

    Pascale Gaudet, Pierre-Andre Michel, Monique Zahn-Zabal, Isabelle Cusin, Paula D. Duek, Olivier Evalet, Alain Gateau, Anne Gleizes, Mario Pereira, Daniel Teixeira, Ying Zhang, Lydie Lane, Amos Bairoch

    NUCLEIC ACIDS RESEARCH   43 ( D1 )   D764 - D770   2015.1

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1093/nar/gku1178

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  • Decreased urinary calbindin 1 levels in proteinuric rats and humans with distal nephron segment injuries Reviewed

    Tomoko Iida, Hidehiko Fujinaka, Bo Xu, Ying Zhang, Sameh Magdeldin, Masaaki Nameta, Zan Liu, Yutaka Yoshida, Eishin Yaoita, Shuichi Tomizawa, Akihiko Saito, Tadashi Yamamoto

    CLINICAL AND EXPERIMENTAL NEPHROLOGY   18 ( 3 )   432 - 443   2014.6

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1007/s10157-013-0835-3

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  • Heparin increasing podocyte-specific gene expressions Reviewed

    Eishin Yaoita, Yutaka Yoshida, Masaaki Nameta, Ying Zhang, Hidehiko Fujinaka, Sameh Magdeldin, Bo Xu, Tadashi Yamamoto

    NEPHROLOGY   19 ( 4 )   195 - 201   2014.4

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    DOI： 10.1111/nep.12207

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  • Deep Proteome Mapping of Mouse Kidney Based on OFFGel Prefractionation Reveals Remarkable Protein Post- Translational Modifications Reviewed

    Sameh Magdeldin, Keiko Yamamoto, Yutaka Yoshida, Bo Xu, Ying Zhang, Hidehiko Fujinaka, Eishin Yaoita, John R. Yates, Tadashi Yamamoto

    JOURNAL OF PROTEOME RESEARCH   13 ( 3 )   1636 - 1646   2014.3

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1021/pr401122m

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  • Erratum to: Decreased urinary calbindin 1 levels in proteinuric rats and humans with distal nephron segment injuries (Clinical and Experimental Nephrology DOI: 10.1007/s10157-013-0835-3) Reviewed

    Tomoko Iida, Hidehiko Fujinaka, Bo Xu, Ying Zhang, Sameh Magdeldin, Masaaki Nameta, Zan Liu, Yutaka Yoshida, Eishin Yaoita, Shuichi Tomizawa, Akihiko Saito, Tadashi Yamamoto

    Clinical and Experimental Nephrology   18 ( 3 )   444   2014

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer-Verlag Tokyo  

    DOI： 10.1007/s10157-013-0846-0

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  • Basics and recent advances of two dimensional- polyacrylamide gel electrophoresis.

    Magdeldin Sameh, Enany Shymaa, Yoshida Yutaka, Xu Bo, Zhang Ying, Zureena Zam, Lokamani Ilambarthi, Yaoita Eishin, Yamamoto Tadashi

    Clin Proteomics   11 ( 1 )   16 - 16   2014

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    Gel- based proteomics is one of the most versatile methods for fractionating protein complexes. Among these methods, two dimensional- polyacrylamide gel electrophoresis (2-DE) represents a mainstay orthogonal approach, which is popularly used to simultaneously fractionate, identify, and quantify proteins when coupled with mass spectrometric identification or other immunological tests. Although 2-DE was first introduced more than three decades ago, several challenges and limitations to its utility still exist. This review discusses the principles of 2-DE as well as both recent methodological advances and new applications.

    DOI： 10.1186/1559-0275-11-16,

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  • Two dimensional electrophoresis of the exo-proteome produced from community acquired methicillin resistant Staphylococcus aureus belonging to clonal complex 80

    Shymaa Enany, Yutaka Yoshida, Sameh Magdeldin, Xu Bo, Ying Zhang, Mohamed Enany, Tadashi Yamamoto

    Microbiological Research   168 ( 8 )   504 - 511   2013.10

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    DOI： 10.1016/j.micres.2013.03.004

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  • Profiling of kidney vascular endothelial cell plasma membrane proteins by liquid chromatography-tandem mass spectrometry Reviewed

    Zan Liu, Bo Xu, Masaaki Nameta, Ying Zhang, Sameh Magdeldin, Yutaka Yoshida, Keiko Yamamoto, Hidehiko Fujinaka, Eishin Yaoita, Masayuki Tasaki, Yuki Nakagawa, Kazuhide Saito, Kota Takahashi, Tadashi Yamamoto

    CLINICAL AND EXPERIMENTAL NEPHROLOGY   17 ( 3 )   327 - 337   2013.6

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1007/s10157-012-0708-1

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  • Profiling and annotation of human kidney glomerulus proteome. Reviewed

    Cui Z, Yoshida Y, Xu B, Zhang Y, Nameta M, Magdeldin S, Makiguchi T, Ikoma T, Fujinaka H, Yaoita E, Yamamoto T

    Proteome science   11 ( 1 )   13   2013.4

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  • Extensive proteomic profiling of the secretome of European community acquired methicillin resistant Staphylococcus aureus clone Reviewed

    Shymaa Enany, Yutaka Yoshida, Sameh Magdeldin, Ying Zhang, Xu Bo, Tadashi Yamamoto

    Peptides   37 ( 1 )   128 - 137   2012.9

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    DOI： 10.1016/j.peptides.2012.06.011

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  • Proteomic approach to human kidney glomerulus prepared by laser microdissection from frozen biopsy specimens: exploration of proteome after removal of blood-derived proteins. Reviewed

    Yoshida Y, Nameta M, Kuwano M, Zhang Y, Bo X, Magdeldin S, Cui Z, Fujinaka H, Yaoita E, Tomonaga T, Yamamoto T

    Proteomics. Clinical applications   6 ( 7月8日 )   412 - 417   2012.8

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  • Murine colon proteome and characterization of the protein pathways Reviewed

    Sameh Magdeldin, Yutaka Yoshida, Huiping Li, Yoshitaka Maeda, Munesuke Yokoyama, Shymaa Enany, Ying Zhang, Bo Xu, Hidehiko Fujinaka, Eishin Yaoita, Sei Sasaki, Tadashi Yamamoto

    BIODATA MINING   5   2012.8

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1186/1756-0381-5-11

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  • Proteomic analysis of glomerulus microdissected from frozen boipsy specimens: removal of blood-derived proteins

    Yoshida Yutaka, Nameta Masaaki, Xu Bo, Zhang Ying, Kuwano Masayosi, Tomonaga Takeshi, Yamamoto Tadashi

    Abstracts for Annual Meeting of Japanese Proteomics Society   2012   91 - 91   2012

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    Language：Japanese   Publisher：Japanese Proteomics Society (Japan Human Proteome Organisation)  

    DOI： 10.14889/jhupo.2012.0.91.0

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  • Reno-protective effects of Eicosapentaenoic Acid (EPA) against PAN induced nephrosis in WKY rats Reviewed

    Ismail Tamer Ahmed, Mohamed Mohamed Soliman, Hossam Fouad Attia, Munoz Cuellar Lino, Xu Bo, Ying Zhang, Tadashi Yamamoto

    Asian Journal of Biochemistry   7 ( 1 )   16 - 26   2012

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    DOI： 10.3923/ajb.2012.16.26

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  • Comparison of human glomerulus proteomic profiles obtained from low quantities of samples by different mass spectrometry with the comprehensive database

    Ying Zhang, Yutaka Yoshida, Bo Xu, Sameh Magdeldin, Hidehiko Fujinaka, Zan Liu, Masahito Miyamoto, Eishin Yaoita, Tadashi Yamamoto

    Proteome Science   9   2011.8

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    DOI： 10.1186/1477-5956-9-47

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  • Usage of electrostatic eliminator reduces human keratin contamination significantly in gel-based proteomics analysis Reviewed

    Bo Xu, Ying Zhang, Zongjiang Zhao, Yutaka Yoshida, Sameh Magdeldin, Hidehiko Fujinaka, Tamer Ahmed Ismail, Eishin Yaoita, Tadashi Yamamoto

    JOURNAL OF PROTEOMICS   74 ( 7 )   1022 - 1029   2011.6

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    DOI： 10.1016/j.jprot.2011.03.001

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  • Novel expression of claudin-5 in glomerular podocytes Reviewed

    Ryo Koda, Linning Zhao, Eishin Yaoita, Yutaka Yoshida, Sachiko Tsukita, Atsushi Tamura, Masaaki Nameta, Ying Zhang, Hidehiko Fujinaka, Sameh Magdeldin, Bo Xu, Ichiei Narita, Tadashi Yamamoto

    CELL AND TISSUE RESEARCH   343 ( 3 )   637 - 648   2011.3

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    DOI： 10.1007/s00441-010-1117-y

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  • "All and None" refining strategy; Fishing your correct protein from proteomics ocean Reviewed

    Sameh Magdeldin, Yutaka Yoshida, Ying Zhang, Bo Xu, Eishin Yaoita, Tadashi Yamamoto

    Journal of Proteomics and Bioinformatics   4 ( 6 )   123 - 124   2011

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    DOI： 10.4172/jpb.1000178

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  • Differential Proteomic Shotgun Analysis Elucidates Involvement of Water Channel Aquaporin 8 in Presence of alpha-Amylase in the Colon Reviewed

    Sameh Magdeldin, Huiping Li, Yutaka Yoshida, Ichiro Satokata, Yoshitaka Maeda, Munesuke Yokoyama, Shymaa Enany, Ying Zhang, Bo Xu, Hidehiko Fujinaka, Eishin Yaoita, Tadashi Yamamoto

    JOURNAL OF PROTEOME RESEARCH   9 ( 12 )   6635 - 6646   2010.12

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    DOI： 10.1021/pr100789v

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  • Comparison of two dimensional electrophoresis mouse colon proteomes before and after knocking out Aquaporin 8 Reviewed

    Sameh Magdeldin, Huiping Li, Yutaka Yoshida, Shymaa Enany, Ying Zhang, Bo Xu, Hidehiko Fujinaka, Eishin Yaoita, Tadashi Yamamoto

    JOURNAL OF PROTEOMICS   73 ( 10 )   2031 - 2040   2010.9

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    DOI： 10.1016/j.jprot.2010.06.010

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  • Glomerular proteins related to slit diaphragm and matrix adhesion in the foot processes are highly tyrosine phosphorylated in the normal rat kidney. Reviewed

    Zhang Y, Yoshida Y, Nameta M, Xu B, Taguchi I, Ikeda T, Fujinaka H, Magdeldin S, Tsukaguchi H, Harita Y, Yaoita E, Yamamoto T

    Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association   25 ( 6 )   1785 - 1795   2010.6

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  • Dietary supplementation with arachidonic acid but not eicosapentaenoic or docosahexaenoic acids alter lipids metabolism in C57BL/6J mice

    Sameh Magdeldin, Yaser Elewa, Takako Ikeda, Junko Ikei, Ying Zhang, Bo Xu, Masaaki Nameta, Hidehiko Fujinaka, Yutaka Yoshida, Eishin Yaoita, Tadashi Yamamoto

    GENERAL PHYSIOLOGY AND BIOPHYSICS   28 ( 3 )   266 - 275   2009.9

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    DOI： 10.4149/gpb_2009_03_266

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  • Identification and characterization of major proteins carrying ABO blood group antigens in the human kidney. International journal

    Masayuki Tasaki, Yutaka Yoshida, Masahito Miyamoto, Masaaki Nameta, Lino M Cuellar, Bo Xu, Ying Zhang, Eishin Yaoita, Yuki Nakagawa, Kazuhide Saito, Tadashi Yamamoto, Kota Takahashi

    Transplantation   87 ( 8 )   1125 - 33   2009.4

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    BACKGROUND: It is generally admitted that ABO(H) blood group antigens are linked to lipids and proteins. Although glycolipids carrying ABO antigens have been well characterized in human kidneys, glycoproteins carrying ABO antigens are largely unknown, and their molecular properties remain to be elucidated. METHODS: All the blood group A antigen-linked proteins in human kidney could be solubilized and captured on immobilized Helix pomatia lectin that recognizes A antigens. These proteins were separated on SDS-PAGE gels. The gel pieces containing protein bands immunoreactive with anti-A antibody were excised, in-gel digested with trypsin, and analyzed by nanoLC tandem mass spectrometer. Protein candidates that carry ABO antigens were confirmed by immunoprecipitation and double-labeled immunofluorescense microscopy. RESULTS: All the glycoproteins carrying ABO antigens were found to be Asn-linked glycoproteins, and presented as multiple bands on SDS-PAGE with molecular masses ranging from 60 to 270 kDa. The protein bands were subjected for mass spectrometric analysis, which identified 121 distinct proteins with high confidence. Of the identified proteins, 55 N-glycosylated, membrane proteins were selected as glycoprotein candidates that carry ABO antigens. Among them, most abundantly expressed proteins as estimated by the number of peptide matches in the MS spectrometric analysis, such as platelet endothelial cell adhesion molecule 1, plasmalemmal vesicle-associated protein, and von Willebrand factor, were further characterized. CONCLUSIONS: Several glycoproteins were identified that represented major glycoproteins carrying ABO antigens in the human kidney, which exhibited distinct features in localization to most of vascular endothelial cells.

    DOI： 10.1097/TP.0b013e31819e0054

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  • ヒト腎組織に発現するABO血液型をもつタンパク質の解析と特性 プロテオミクスを用いて

    田崎 正行, 吉田 豊, 田口 いづみ, 張 瑩, 行田 正晃, 中川 由紀, 斎藤 和英, 高橋 公太, 山本 格

    日本腎臓学会誌   51 ( 3 )   369 - 369   2009.4

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  • Mesangial Cells Connected by the N-Cadherin-Catenin System in the Rat Kidney Reviewed

    Masaaki Nameta, Eishin Yaoita, Nobutaka Kato, Linning Zhao, Ying Zhang, Hidehiko Fujinaka, Bo Xu, Yutaka Yoshida, Tadashi Yamamoto

    NEPHRON EXPERIMENTAL NEPHROLOGY   112 ( 4 )   E92 - E98   2009

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1159/000224797

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  • Claudin-6 localized in tight junctions of rat podocytes Reviewed

    Linning Zhao, Eishin Yaoita, Masaaki Nameta, Ying Zhang, Lino Munoz Cuellar, Hidehiko Fujinaka, Bo Xu, Yutaka Yoshida, Katsuyoshi Hatakeyama, Tadashi Yamamoto

    AMERICAN JOURNAL OF PHYSIOLOGY-REGULATORY INTEGRATIVE AND COMPARATIVE PHYSIOLOGY   294 ( 6 )   R1856 - R1862   2008.6

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    DOI： 10.1152/ajpregu.00862.2007

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  • In-depth proteomic profiling of the normal human kidney glomerulus using two-dimensional protein prefractionation in combination with liquid chromatography-tandem mass spectrometry. International journal

    Masahito Miyamoto, Yutaka Yoshida, Izumi Taguchi, Yoshimi Nagasaka, Masayuki Tasaki, Ying Zhang, Bo Xu, Masaaki Nameta, Hiroshi Sezaki, Lino M Cuellar, Tetsuo Osawa, Hideo Morishita, Shigeki Sekiyama, Eishin Yaoita, Kenjiro Kimura, Tadashi Yamamoto

    Journal of proteome research   6 ( 9 )   3680 - 90   2007.9

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    The kidney glomerulus plays a pivotal role in ultrafiltration of plasma into urine and also is the locus of kidney disease progressing to chronic renal failure. We have focused proteomic analysis on the glomerulus that is most proximal to the disease locus. In the present study, we aimed to provide a confident, in-depth profiling of the glomerulus proteome. The glomeruli were highly purified from the kidney cortex from a male, 68-year-old patient who underwent nephroureterectomy due to ureter carcinoma. The patient was normal in clinical examinations including serum creatinine and urea levels and liver function, and did not receive any chemotherapy and radiotherapy. The cortical tissue was histologically normal, and no significant deposition of immunoglobulins and complement C3 was observed. We employed a novel strategy of protein separation using 1D (SDS-PAGE) and 2D (solution-phase IEF in combination with SDS-PAGE) prefractionation prior to the shotgun analysis with LC-MS/MS. The protein prefractionation produced 90 fractions, and eventually provided a confident set of identified proteins consisting of 6686 unique proteins (3679 proteins with two or more peptide matches and 3007 proteins with one peptide match), representing 2966 distinct genes. All the identified proteins were annotated and classified in terms of molecular function and biological process, compiled into 1D and 2D protein arrays, consisting of 15 and 75 sections, corresponding to the protein fractions which were defined by MW and pI range, and deposited on a Web-based database (http://www.hkupp.org). The most remarkable feature of the glomerulus proteome was a high incidence of identification of cytoskeleton-related proteins, presumably reflecting the well-developed, cytoskeletal organization of glomerular cells related to their physiological functions.

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  • 正常ラットの腎臓におけるチロシンリン酸化タンパク質の局在 Reviewed

    Zhang Y, Yoshida Y, Xu B, Nameta M, Miyamoto M, Yaoita E, Yamamoto T

    2007.3

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  • Localization of tyrosine-phosphorylated proteins in the normal rat kidney

    Ying Zhang, Yutaka Yoshida, Bo Xu, Masaaki Nameta, Masahito Miyamoto, Eishin Yaoita, Tadashi Yamamoto

    Acta Medica et Biologica   55 ( 1 )   1 - 7   2007.3

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  • Two-dimensional electrophoretic profiling of normal human kidney glomerulus proteome and construction of an extensible markup language (XML)-based database

    Yutaka Yoshida, Kenji Miyazaki, Junichi Kamiie, Masao Sato, Seiji Okuizumi, Akihisa Kenmochi, Ken'ichi Kamijo, Takuji Nabetani, Akira Tsugita, Bo Xu, Ying Zhang, Eishin Yaoita, Tetsuo Osawa, Tadashi Yamamoto

    Proteomics   5 ( 4 )   1083 - 1096   2005.3

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    Language：English   Publishing type：Research paper (international conference proceedings)  

    DOI： 10.1002/pmic.200401075

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MISC

  • Discoverry of predictive biomarkers for pre-surgical chemotherapy in ER-positive HER2-negative breast cancer

    Hasegawa Miki, Kanbayashi Chizuko, Wakai Toshifumi, Tomonaga takeshi, Yamamoto tadashi, Yoshida Yutaka, Shiromizu Takashi, Sato Nobuaki, Zhang Ying, Koyama Yu, Makino Haruhiko, Nagahashi Masayuki, Kaneko Kouji

    Abstracts for Annual Meeting of Japanese Proteomics Society   2015 ( 0 )   144 - 144   2015

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    Language：Japanese   Publisher：Japanese Proteomics Society (Japan Human Proteome Organisation)  

    DOI： 10.14889/jhupo.2015.0.144.0

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  • Comparative proteomic analysis of the liver in a murine model of non-alcoholic steatohepatitis

    Masaaki Takamura, Bo Xu, Satoshi Yamagiwa, Yasunobu Matsuda, Shuichiro Shimada, Ying Zhang, Yutaka Yoshida, Eishin Yaoita, Minoru Nomoto, Tadashi Yamamoto, Yutaka Aoyagi

    HEPATOLOGY   56   855A - 855A   2012.10

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  • Glomerular proteins related to slit diaphragm and matrix adhesion in the foot processes are highly tyrosine phosphorylated in the normal rat kidney (vol 25, pg 1785, 2010)

    Ying Zhang, Yutaka Yoshida, Masaaki Nameta, Bo Xu, Izumi Taguchi, Takako Ikeda, Hidehiko Fujinaka, Sameh Magdeldin, Hiroyasu Tsukaguchi, Yutaka Harita, Eishin Yaoita, Tadashi Yamamoto

    NEPHROLOGY DIALYSIS TRANSPLANTATION   27 ( 6 )   2606 - 2606   2012.6

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  • 実験的NASHモデルマウス肝組織のプロテオーム解析

    高村 昌昭, 許 波, 嶋田 修一郎, 張 瑩, 吉田 豊, 矢尾板 永信, 山際 訓, 松田 康伸, 野本 実, 山本 格, 青柳 豊

    日本消化器病学会雑誌   109 ( 臨増総会 )   A325 - A325   2012.3

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  • Human kidney glomerulus proteome and biomarker discovery of kidney diseases

    Yutaka Yoshida, Masahito Miyamoto, Izumi Taguchi, Bo Xu, Ying Zhang, Eishin Yaoita, Hidehiko Fujinaka, Tadashi Yamamoto

    PROTEOMICS CLINICAL APPLICATIONS   2 ( 3 )   420 - 427   2008.3

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    Language：English   Publishing type：Book review, literature introduction, etc.  

    DOI： 10.1002/prca.200780016

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Presentations

  • TRPM4の発現、機能低下とその結果生じるTRPC6機能亢進、Ca2+流入の増加はポドサイト傷害の重要な初期変化である

    内許玉楓, 福住好恭, 安田英紀, 常 國慶, 萱場 睦, 河内 裕

    第67回 日本腎臓学会学術総会  2024.6 

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  • 抗ネフリン抗体検出簡便法の確立：免疫組織学 的手法との感度比較

    萱場 睦, 内許玉楓, 永井 隆, 福住好恭, 常 国慶, 河内 裕

    第67回 日本腎臓学会学術総会  2024.6 

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  • 14-3-3 Proteins Stabilize Vimentin and Actin Filaments to Maintain Primary and Foot Processes in Podocyte

    ASN Kidney Week  2023.11 

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  • Downregulation of TRPM4 and Consequent Increase in TRPC6 Activity Are Critical Initiation Events Leading to Podocyte Injury

    Ying Zhang, Yoshiyasu Fukusumi, Hidenori Yasuda, Guoqing Chang, Mutsumi Kayaba, Hiroshi Kawachi

    ASN Kidney Week  2023.11 

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  • Nephrin-Ephrin-B1-Par6 com6plex is crucial for slit diaphragm in podocytes: Ephrin-B1 suppresses tight junction formation by interfering with Par6-Cdc42 binding

    Yoshiyasu Fukusumi, Ying Zhang, Hidenori Yasuda, Hiroshi Kawachi

    2022.11 

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  • Ephrin-B1はPar-6-Cdc42結合と阻害しTJ形成の抑制、スリット膜維持に働く

    福住好恭, 安田英紀, 張瑩(内許玉楓), 河内裕

    第65回日本腎臓学会  2022.6 

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  • Neurexin 1α containing splice site 4 interacts with nephrin and contributes to maintenance of the integrity of podocyte slit diaphragm

    Yoshiyasu Fukusumi, Hidenori Yasuda, Ying Zhang, Hiroshi Kawachi

    Annual Meeting of American Society of Nephrology  2021.11 

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  • NHERF2はスリット膜の分子複合体とポドサイト頂部の分子複合体を連結し、ポドサイトの細胞骨格を維持する

    福住好恭, 安田英紀, 張瑩(内許玉楓, 河内裕

    第64回日本腎臓学会  2021.6 

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  • スプライスサイト4を持つNeurexin 1αバリアントはスリット膜構造の維持に重要な役割を果たす

    福住好恭, 安田英紀, 張瑩(内許玉楓), 河内裕

    第64回日本腎臓学会  2021.6 

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  • PDZ蛋白質NHERF2はEphrin-B1とEzrinを連結させ、スリット膜機能維持に重要な役割を果たす

    福住好恭, 安田英紀, 張瑩(内許玉楓), 河内裕

    第63回日本腎臓学会  2020.6 

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  • メサンギウム増殖性腎炎におけるTh17細胞の関与について

    渡辺秀平, 安田英紀, 張瑩(内許玉楓), 福住好恭, 河内裕

    第62回日本腎臓学会  2019.6 

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  • キサンチン酸化還元酵素阻害薬トピロキソスタットのポドサイト保護作用

    張瑩(内許玉楓), 福住好恭, 中村敬志, 芦澤直樹, 河内裕

    第61回日本腎臓学会  2018.6 

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  • TRPM4 is expressed at the apical surface of podocyte just above slit diaphragm, and its altered expression is involved in podocyte injury

    張瑩(内許玉楓), 福住好恭, 河内裕

    アメリカ腎臓学会（国際学会）  2017.11 

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  • スリット膜特異的障害モデルにおける発現上昇遺伝子の検討:次世代シーケンサを用いたRNA-seq解析

    張瑩(内許玉楓), 福住好恭, 河内裕

    第60回日本腎臓学会  2017.6 

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  • RNA-seq Based Differential Expression Analysis in Rats with Slit Diaphragm Specific Dysfunction: The Glomerular Expression Profiles of Nephropathy Induced by Anti-nephrin Antibody

    張瑩(内許玉楓), 福住好恭, 河内裕

    アメリカ腎臓学会  2016.11 

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  • 次世代シーケンサー解析による新規ネフリン 関連分子、スリット膜機能分子の同定

    張 瑩(内許玉楓), 福住 好恭, 河内 裕

    第59回日本腎臓学会  2016.6 

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Research Projects

  • スリット膜機能維持におけるNeurexin-シナプス小胞関連分子相互作用の役割

    Grant number：24K11405

    2024.4 - 2028.3

    System name：科学研究費助成事業

    Research category：基盤研究(C)

    Awarding organization：日本学術振興会

    福住好恭, 内許玉楓, 永井 隆, 河内 裕

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    Grant amount：\4680000 （ Direct Cost: \3600000 、 Indirect Cost：\1080000 ）

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  • Role of Ephrin-Nephrin-Neurexin complex in maintaining slit diaphragm function

    Grant number：22H03086

    2022.4 - 2025.3

    System name：Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (B)

    Research category：Grant-in-Aid for Scientific Research (B)

    Awarding organization：Japan Society for the Promotion of Science

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    Grant amount：\17290000 （ Direct Cost: \13300000 、 Indirect Cost：\3990000 ）

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  • 腎糸球体上皮細胞スリット膜におけるNeurexinの役割の解明

    Grant number：20K08587

    2020.4 - 2024.3

    System name：科学研究費助成事業 基盤研究(C)

    Research category：基盤研究(C)

    Awarding organization：日本学術振興会

    福住 好恭, 内許 玉楓, 安田 英紀, 河内 裕

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    Grant amount：\4160000 （ Direct Cost: \3200000 、 Indirect Cost：\960000 ）

    我々はシナプス前末端に存在するneurexin1がポドサイトスリット膜部に発現していること、ポドサイトで発現しているneurexin1は神経組織と異なる特異的なバリアント(splice site (SS)4(+))であることを示した。しかし、neurexin1のスリット膜での役割の詳細は不明である。
    Neurexin1のスリット膜のバリア維持機能における役割を明らかにするため、本年度（令和2年度）はneurexin1αKOマウスを作製し、ポドサイト病変、スリット膜機能分子の発現を解析した。また、neurexin1αとスリット膜機能分子nephrinとの相互作用解析を行った。
    まず、ラット糸球体可溶化材料を用いたウエスタンブロット解析から、ポドサイトで発現しているneurexin1は主に長鎖のneurexin1αであることを示した。
    次に、neurexin1αKOマウスの解析で、若齢期の10週齢では野生型マウスと比較して顕著な変化は観察されなかったが、成体期の20週齢でnephrin、podocinの著明な発現低下、及び有意な病的蛋白尿を観察した。
    相互作用解析では、ラット糸球体可溶化材料を用いた免疫沈降解析によりneurexin1αとnephrinの結合性を認めた。また、HEK293細胞を用いた強制発現系の解析で、神経組織で発現しているneurexin1α-SS4(-)はnephrinとの結合性が認められなかったが、ポドサイトでの発現型であるneurexin1α-SS４(+)はnephrinと結合性を有した。
    以上より、neurexin1αはnephrinと結合性を有するスリット膜構成分子であること、neurexin1αの発現低下により病的蛋白尿が誘導されることが示され、ポドサイト特異的neurexin1α-SS４(+)はスリット膜の機能維持に重要であることを明らかにした。

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  • Function of TRPM4 on podocyte

    Grant number：19K08720

    2019.4 - 2023.3

    System name：Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)

    Research category：Grant-in-Aid for Scientific Research (C)

    Awarding organization：Japan Society for the Promotion of Science

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    Grant amount：\4160000 （ Direct Cost: \3200000 、 Indirect Cost：\960000 ）

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  • Novel therapy for nephotic syndrome targetting synapse associated molecules in podocyte

    Grant number：19H03673

    2019.4 - 2022.3

    System name：Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (B)

    Research category：Grant-in-Aid for Scientific Research (B)

    Awarding organization：Japan Society for the Promotion of Science

    Kawachi Hiroshi

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    Grant amount：\17160000 （ Direct Cost: \13200000 、 Indirect Cost：\3960000 ）

    It was demonstrated that synapse associated molecules, SV2B, Neurexin, Ephrin-B1 were expressed in podocyte, and dysfunction of these molecules lead proteinuria. The present study revealed that a unique variant of Neurexin (Neurexin 1a, splice site #4(+)) was expressed in podocyte and interacted with nephrin and CD2AP, critical molecules of slit diaphragm. The interactions played a key role in maintaining the barrier function of slit diaphragm. Ephrin-B, a transmembrane protein was connected to cytoskeletal actin via NHERF2 and Ezrin. The linkage is essential for maintaining barrier function of sit diaphragm. These synapse-associated molecules could be targets for a novel therapy.

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  • 次世代シーケンサー解析によるネフローゼ症候群の新規治療標的分子の探索

    2016.4 - 2019.3

    System name：科学研究費助成事業

    Research category：若手研究(B)

    Awarding organization：日本学術振興会

    張 瑩

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    Authorship：Principal investigator  Grant type：Competitive

    ネフローゼ症候群の蛋白尿発症に関わる分子機構の全体像は未解明で、現在まで蛋白尿に対する有効な治療法がない。本研究の目的は、ネフローゼ症候群の病態モデルを用い、次世代シーケンサー解析による腎臓糸球体のすべてのmRNA 配列の解読と発現量の測定を行った上で、ネフローゼ症候群の糸球体における発現変動遺伝子を同定し、ネフローゼ症候群に対する新規治療の標的候補分子を決定することである。

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  • 糸球体と尿のプロテオーム解析による糖尿病性腎症のバイオマーカーの探索

    2015.4 - 2015.8

    System name：科学研究費助成事業

    Research category：若手研究(B)

    Awarding organization：日本学術振興会

    張 瑩

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    Authorship：Principal investigator  Grant type：Competitive

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  • Identification of antigen of IgA and Membranous Nephropathy by On -site proteomics

    Grant number：22659165

    2010 - 2012

    System name：Grants-in-Aid for Scientific Research

    Research category：Grant-in-Aid for Challenging Exploratory Research

    Awarding organization：Japan Society for the Promotion of Science

    XU Bo, YAMAMOTO Tadashi, ZHANG Ying

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    Grant amount：\3300000 （ Direct Cost: \3000000 、 Indirect Cost：\300000 ）

    Formation of immune complexes were recognized as key rule involved with IgA nephropathy and membranous nephropathy deeply, but it is still unclear in many cases of antigen of these diseases. In this study, 10 μm thickness sections of kidney biopsy samples were pretreated, and glomeruli were dissected by using laser micro dissection (LMD). Peptides were extracted from collected glomeruli followed by On-Site proteomics method followed LC-MS/MS analysis. Proteins with significant changesbetween the IgA・membranous nephropathy and normal glomerulus were analyzed by bioinformatics tool and pathway analysis of diseases to be explored their pathogenesis of IgA・membranous nephropathy

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