Details of the Researcher

PHOTO

Hiroyuki Satofuka
Section
Graduate School of Medicine
Job title
Assistant Professor
Degree
e-Rad No.
60373312

Research History 8

  • 2024/04 - Present
    Tohoku University

  • 2017/08 - 2024/03
    Tottori University

  • 2017/03 - 2017/07
    Tottori University

  • 2012/11 - 2017/02
    株式会社 オーダーメードメディカルリサーチ　主席研究員

  • 2004/11 - 2012/05
    株式会社 バイオマトリックス研究所　主任研究員 兼 部長代理

  • 2004/04 - 2004/10
    理化学研究所　基礎科学特別研究員

  • 2001/05 - 2004/03
    理化学研究所

  • 2000/04 - 2001/05
    Japan Advanced Institute of Science and Technology　School of Materials Science　Resarcher

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Education 3

  • 京都大学 大学院　工学研究科　合成・生物化学

    1998/04 - 2001/03

  • 大阪大学 大学院　工学研究科　応用生物工学

    1996/04 - 1998/03

  • Hiroshima University　Faculty of Engineering

    1992/04 - 1996/03

Research Interests 2

  • Protein Engineering

  • Antibody Engineering

Research Areas 3

  • Life sciences / Immunology /

  • Life sciences / Applied biochemistry /

  • Life sciences / Cell biology /

Awards 1

  1. Poster Excellence Award

    2022/12　The Antibody Society of Japan　Generation of fully human antibody-producing rats (TC-mAb rats) and analysis of antibody repatoires

Papers 33

  1. Two stress-responsive kinases suppress ferroptosis by activating antioxidant programs under mild oxidative stress. International-journal

    Yumiko Fujikawa, Hirotatsu Imai, Tetsuo Onuki, Kouji Hoshino, Marco A De Velasco, Kazuhiko Matsuo, Hitomi Kurosawa, Kyoko Aoyagi, Hiroko Hirose, Yoshie Nakamura, Akiko Uchiyama, Kae Suzuki, Mariko Mizuguchi, Hidehisa Takahashi, Hiroyuki Osada, Noritaka Kagaya, Kazuo Shin-Ya, Hiroyuki Satofuka, Yukinari Kato, Hidehito Kuroyanagi, Daisuke Utsumi, Kenzo Takahashi, Takashi Nakayama, Hirotsugu Uemura, Hiroji Uemura, Minoru Yoshida, Shigeo Ohno, Akio Yamashita

    Signal transduction and targeted therapy　11　(1)　2026/08/03

    DOI： 10.1038/s41392-026-02892-1 　

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    Cancer cells maintain chronically elevated levels of reactive oxygen species (ROS) while relying on robust antioxidant programs to preserve redox homeostasis and viability. Although therapeutic strategies that disrupt this balance to induce lethal oxidative stress and ferroptosis have emerged as promising anticancer approaches, the upstream signaling mechanisms that constrain ROS accumulation under physiologically relevant stress conditions remain incompletely understood. Here, we identify the stress-responsive kinases SMG1 and DNA-dependent protein kinase (DNA-PK) as functionally redundant regulators of redox homeostasis and ferroptosis resistance. Genetic or pharmacological inhibition of either kinase triggers ferroptotic cell death, accompanied by marked accumulation of total ROS, ferrous iron, and lipid hydroperoxides. Mechanistically, under mild oxidative stress, SMG1 and DNA-PK cooperatively phosphorylate the central antioxidant transcription factor NRF2 at serine 13 and serine 40, weakening its interaction with the negative regulator KEAP1 and promoting NRF2 accumulation and transcriptional activation. Transcriptomic profiling of de novo mRNAs revealed that inhibition of either kinase is sufficient to suppress NRF2-driven antioxidant gene expression. In contrast, excessive oxidative stress overrides this pro-survival pathway and redirects signaling toward anti-survival responses mediated by ATF4, ATM-CHK2, and JNK/p38 pathways. Collectively, these findings uncover a previously unrecognized SMG1/DNA-PK-NRF2 signaling axis that functions as a redox stress-intensity-dependent switch governing cell fate decisions between antioxidant adaptation and ferroptotic death. Targeting this axis may represent a promising therapeutic strategy for cancer treatment.

  2. Development of a specific anti-human EphA3 monoclonal antibody, Ea3Mab-20, for flow cytometry International-journal Peer-reviewed

    Hiroyuki Satofuka, Hiroyuki Suzuki, Miu Hirose, Keisuke Shinoda, Takuya Nakamura, Tomohiro Tanaka, Mika K. Kaneko, Yukinari Kato

    Biochemistry and Biophysics Reports　43　102130-102130　2025/09

    DOI： 10.1016/j.bbrep.2025.102130 　

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    Erythropoietin-producing hepatocellular (Eph) receptor A3 (EphA3) is a member of the Eph receptor family, which binds to its respective ligands, ephrins. These interactions are essential for normal development and tissue homeostasis. Dysregulation of EphA3 has been reported to be associated with human hematopoietic malignancies, making it a promising target for therapy and diagnosis. Due to the high similarity of the extracellular domain among Eph receptors (more than 33% amino acid identity), generating highly specific monoclonal antibodies (mAbs) is crucial. We developed anti-human EphA3 mAbs in this study using the Cell-Based Immunization and Screening (CBIS) method. Among them, the clone Ea3Mab-20 (IgG1, kappa) exhibited high affinity and specificity in flow cytometry. The dissociation constant values of Ea3Mab-20 for CHO/EphA3 and Jurkat cells were determined to be 9.0 ± 0.3 × 10-9 M and 1.4 ± 0.1 × 10-9 M, respectively. Ea3Mab-20 showed no cross-reactivity with other Eph receptors in flow cytometry. Furthermore, Ea3Mab-20 demonstrated the suitability for detecting formalin-fixed paraffin-embedded cell samples in immunohistochemistry. Therefore, Ea3Mab-20 is valuable mAb for basic research and is expected to contribute to the clinical application of mAb for cancer therapy and diagnosis.

  3. Development of Anti-Human Cadherin-26 Monoclonal Antibody, Ca26Mab-6, for Flow Cytometry International-journal

    Hiroyuki Satofuka, Hiroyuki Suzuki, Mika K. Kaneko, Yukinari Kato

    Monoclonal antibodies in immunodiagnosis and immunotherapy　45　(3)　25-33　2025/08/12

    DOI： 10.20944/preprints202508.0774.v1 　

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    Cadherin 26 (CDH26) is a recently identified member of the cadherin superfamily. Although CDH26 gene expression has been reported in association with allergic inflammatory responses, the protein expression levels and the signaling pathways mediated through its interactions with other proteins remain poorly understood. This is primarily due to the lack of monoclonal antibodies (mAbs) that can recognize the intact, cell surface-expressed form of CDH26. In this study, we developed an antihuman CDH26 mAb, Ca26Mab-6 (IgM, kappa), using the Cell-Based Immunization and Screening (CBIS) method. Ca26Mab-6 demonstrated high sensitivity and specificity for CDH26 in flow cytometry and did not bind to Chinese hamster ovary (CHO)-K1 cells, which overexpress any of the other type I or type II cadherins. Ca26Mab-6 successfully detected endogenous CDH26 protein expression in HepG2, U-87 MG, MCF7, and 293FT cells. The apparent dissociation constant of Ca26Mab-6 was determined to be 9.8 ± 4.8 × 10-9 M for CDH26-overexpressed CHO-K1 (CHO/CDH26) cells and 3.6 ± 1.0 × 10-7 M for HepG2 cells. The detection of CDH26 expression in cancer cells may offer new insights into the potential relationship between inflammatory responses and malignant transformation. Therefore, Ca26Mab-6, developed using the CBIS method, is expected to facilitate functional studies of CDH26 and contribute to the development of CDH26-targeted antibody-based therapies.

  4. Development of an anti-human EphA2 monoclonal antibody Ea2Mab-7 for multiple applications International-journal Peer-reviewed

    Hiroyuki Satofuka, Hiroyuki Suzuki, Tomohiro Tanaka, Guanjie Li, Mika K. Kaneko, Yukinari Kato

    Biochemistry and Biophysics Reports　42　101998-101998　2025/06

    DOI： 10.1016/j.bbrep.2025.101998 　

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    Ephrin type A receptor 2 (EphA2) binds to membrane-bound ligands, ephrin A1, A2, and A5, eliciting bidirectional signaling. This signaling regulates many physiological processes, such as tissue development, homeostasis, and regeneration. The dysregulation of the EphA2-ephrins axis contributes to various diseases, including cancers. The high expression of EphA2 is observed in various cancers, which promotes cancer malignancy, whereas its levels are relatively low in most normal adult tissues. Therefore, EphA2 is a promising target for cancer therapy. We developed anti-human EphA2 monoclonal antibodies in this study using the Cell-Based Immunization and Screening method. Among them, a clone Ea2Mab-7 (IgG1, κ) exhibited a high affinity and sensitivity in flow cytometry. The dissociation constant values of Ea2Mab-7 for CHO/EphA2 and MDA-MB-231 cells were determined as 6.2 ± 1.3 × 10-9 M and 1.6 ± 0.4 × 10-9 M, respectively. Furthermore, Ea2Mab-7 can detect endogenous EphA2 in Western blot and immunohistochemistry. Therefore, the Ea2Mab-7 is highly versatile for basic research and is expected to contribute to clinical applications, such as antibody therapy and tumor diagnosis.

  5. Ea3Mab-20: A Specific Anti-Human EphA3 Monoclonal Antibody for Flow Cytometry

    Hiroyuki Satofuka, Hiroyuki Suzuki, Miu Hirose, Keisuke Shinoda, Takuya Nakamura, Tomohiro Tanaka, Mika K. Kaneko, Yukinari Kato

    2025/04/07

    DOI： 10.20944/preprints202504.0524.v1 　

  6. A novel Anti-Mouse CCR7 Monoclonal Antibody, C7Mab-7, Demonstrates High Sensitivity in Flow Cytometry, Western Blot, and Immunohistochemistry International-journal

    Hiroyuki Satofuka, Hiroyuki Suzuki, Tomohiro Tanaka, Rena Ubukata, Miu Hirose, Haruto Yamamoto, Yu Kaneko, Shiori Fujisawa, Guanjie Li, Mika K Kaneko, Yukinari Kato

    Biochemistry and biophysics reports　41　101948-101948　2024/11/26

    DOI： 10.20944/preprints202411.1959.v1 　

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    C-C chemokine receptor type 7 (CCR7) is a member of the G protein-coupled receptor family and functions as a lymph node-homing receptor for immune cells. Upon ligand binding, CCR7 promotes the migration of immune cells to secondary lymphoid organs. In cancers, CCR7 has been revealed as a critical molecule in lymph node metastasis. Consequently, anti-CCR7 monoclonal antibodies (mAbs) have been developed as cancer therapeutic agents. In this study, we established an anti-mouse CCR7 (mCCR7) mAb, C7Mab-7 (rat IgG1, kappa) using the Cell-Based Immunization and Screening (CBIS) method. C7Mab-7 demonstrated high sensitivity in flow cytometry. The dissociation constant (K D) value of C7Mab-7 was determined to be 2.5 × 10⁻⁹ M for mCCR7-overexpressed Chinese hamster ovary-K1 (CHO/mCCR7) cells. Furthermore, C7Mab-7 detected mCCR7 with high sensitivity in western blot and immunohistochemistry. C7Mab-7, developed by the CBIS method, accelerates the development of CCR7-targeted antibody therapies and cancer diagnostics.

  7. Developing a workflow for the isolation of hybridoma cells producing fully human antigen-specific antibodies using a surface IgG detection method. International-journal Peer-reviewed

    Hiroyuki Satofuka, Yayan Wang, Hiroshi Tanaka, Kei Hiramatsu, Kayoko Morimoto, Haruka Takayama, Haochen Tu, Yu Qiao, Satoru Ito, Xu Gao, Mitsuo Oshimura, Yasuhiro Kazuki

    Scientific reports　14　(1)　23138-23138　2024/10/04

    DOI： 10.1038/s41598-024-73770-5 　

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    The antigen-mediated B cell isolation method, based on the detection of surface IgG (sIgG), has increased the efficiency of therapeutic antibody (Ab) discovery. However, the reduction in sIgG expression on B cells during plasma cell differentiation presents challenges as it enables Ab production from only a small subset of B cells (e.g., memory B cells). The present study aimed to addressed this problem by developing a workflow to isolate human-IgG-secreting hybridoma cells produced by cell fusion, the majority of which express sIgG. We showed that our sIgG-based antigen-coated bead separation method efficiently enriched hybridoma cells expressing antigen-specific Abs with a yield of 83.5% (from the cell fusion pool) and a positive rate of 73.2%. Furthermore, because the separation could be performed after only a short (1-2-day) culture period following cell fusion, diverse hybridoma clones could be obtained, minimizing clonal selection and the incidence of duplicates. Given that the expression of membrane-bound IgG and sIgG are regulated by different splicing mechanisms, we speculate that the cell fusion step potentially attenuated the suppression of human sIgG expression. Overall, our proposed method is expected to markedly improve the efficiency of therapeutic Ab candidate production, which will have important clinical implications.

  8. Comparative analysis of trans-chromosomic rodent models reveals improved somatic hypermutation and class-switch recombination in rats

    Hiroyuki Satofuka, Satoshi Abe, Takashi Moriwaki, Akane Okada, Kanako Kazuki, Shusei Hamamichi, Masaharu Hiratsuka, Masumi Hirabayashi, Kazuomi Nakamura, Tetsushi Sakuma, Takashi Yamamoto, Yoshihiro Baba, Kazuma Tomizuka, Yasuhiro Kazuki

    2024/08/26

    DOI： 10.1101/2024.08.26.609625 　

  9. Treatment of CHO cells with Taxol and reversine improves micronucleation and microcell-mediated chromosome transfer efficiency International-journal Peer-reviewed

    Narumi Uno, Hiroyuki Satofuka, Hitomaru Miyamoto, Kazuhisa Honma, Teruhiko Suzuki, Kyotaro Yamazaki, Ryota Ito, Takashi Moriwaki, Shusei Hamamichi, Kazuma Tomizuka, Mitsuo Oshimura, Yasuhiro Kazuki

    Molecular Therapy - Nucleic Acids　33　391-403　2023/07

    Publisher: Elsevier BV

    DOI： 10.1016/j.omtn.2023.07.002 　

    ISSN： 2162-2531

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    Microcell-mediated chromosome transfer is an attractive technique for transferring chromosomes from donor cells to recipient cells and has enabled the generation of cell lines and humanized animal models that contain megabase-sized gene(s). However, improvements in chromosomal transfer efficiency are still needed to accelerate the production of these cells and animals. The chromosomal transfer protocol consists of micronucleation, microcell formation, and fusion of donor cells with recipient cells. We found that the combination of Taxol (paclitaxel) and reversine rather than the conventional reagent colcemid resulted in highly efficient micronucleation and substantially improved chromosomal transfer efficiency from Chinese hamster ovary donor cells to HT1080 and NIH3T3 recipient cells by up to 18.3- and 4.9-fold, respectively. Furthermore, chromosome transfer efficiency to human induced pluripotent stem cells, which rarely occurred with colcemid, was also clearly improved after Taxol and reversine treatment. These results might be related to Taxol increasing the number of spindle poles, leading to multinucleation and delaying mitosis, and reversine inducing mitotic slippage and decreasing the duration of mitosis. Here, we demonstrated that an alternative optimized protocol improved chromosome transfer efficiency into various cell lines. These data advance chromosomal engineering technology and the use of human artificial chromosomes in genetic and regenerative medical research.

  10. Characterization of human anti-EpCAM antibodies for developing an antibody–drug conjugate International-journal Peer-reviewed

    Hiroyuki Satofuka, Yayan Wang, Kyotaro Yamazaki, Shusei Hamamichi, Takeshi Fukuhara, Abdur Rafique, Nana Osako, Iori Kanazawa, Takeshi Endo, Naomi Miyake, Kazuhisa Honma, Yuichi Nagashima, Genki Hichiwa, Kazuto Shimoya, Satoshi Abe, Takashi Moriwaki, Yasufumi Murakami, Xu Gao, Hiroyuki Kugoh, Mitsuo Oshimura, Yuji Ito, Yasuhiro Kazuki

    Scientific Reports　13　(1)　4225-4225　2023/03/14

    Publisher: Springer Science and Business Media LLC

    DOI： 10.1038/s41598-023-31263-x 　

    eISSN： 2045-2322

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    Abstract We previously generated fully human antibody-producing TC-mAb mice for obtaining potential therapeutic monoclonal antibodies (mAbs). In this study, we investigated 377 clones of fully human mAbs against a tumor antigen, epithelial cell adhesion molecule (EpCAM), to determine their antigen binding properties. We revealed that a wide variety of mAbs against EpCAM can be obtained from TC-mAb mice by the combination of epitope mapping analysis of mAbs to EpCAM and native conformational recognition analysis. Analysis of 72 mAbs reacting with the native form of EpCAM indicated that the EpCL region (amino acids 24–80) is more antigenic than the EpRE region (81–265), consistent with numerous previous studies. To evaluate the potential of mAbs against antibody–drug conjugates, mAbs were directly labeled with DM1, a maytansine derivative, using an affinity peptide-based chemical conjugation (CCAP) method. The cytotoxicity of the conjugates against a human colon cancer cell line could be clearly detected with high-affinity as well as low-affinity mAbs by the CCAP method, suggesting the advantage of this method. Thus, this study demonstrated that TC-mAb mice can provide a wide variety of antibodies and revealed an effective way of identifying candidates for fully human ADC therapeutics.

  11. Efficient human-like antibody repertoire and hybridoma production in trans-chromosomic mice carrying megabase-sized human immunoglobulin loci International-journal Peer-reviewed

    Hiroyuki Satofuka, Satoshi Abe, Takashi Moriwaki, Akane Okada, Kanako Kazuki, Hiroshi Tanaka, Kyotaro Yamazaki, Genki Hichiwa, Kayoko Morimoto, Haruka Takayama, Yuji Nakayama, Shinya Hatano, Yutaro Yada, Yasufumi Murakami, Yoshihiro Baba, Mitsuo Oshimura, Kazuma Tomizuka, Yasuhiro Kazuki

    Nature Communications　13　(1)　1841-1841　2022/04

    Publisher: Springer Science and Business Media LLC

    DOI： 10.1038/s41467-022-29421-2 　

    eISSN： 2041-1723

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    Abstract Trans-chromosomic (Tc) mice carrying mini-chromosomes with megabase-sized human immunoglobulin (Ig) loci have contributed to the development of fully human therapeutic monoclonal antibodies, but mitotic instability of human mini-chromosomes in mice may limit the efficiency of hybridoma production. Here, we establish human antibody-producing Tc mice (TC-mAb mice) that stably maintain a mouse-derived, engineered chromosome containing the entire human Ig heavy and kappa chain loci in a mouse Ig-knockout background. Comprehensive, high-throughput DNA sequencing shows that the human Ig repertoire, including variable gene usage, is well recapitulated in TC-mAb mice. Despite slightly altered B cell development and a delayed immune response, TC-mAb mice have more subsets of antigen-specific plasmablast and plasma cells than wild-type mice, leading to efficient hybridoma production. Our results thus suggest that TC-mAb mice offer a valuable platform for obtaining fully human therapeutic antibodies, and a useful model for elucidating the regulation of human Ig repertoire formation.

  12. A SARS-CoV-2 Antibody Broadly Neutralizes SARS-related Coronaviruses and Variants by Coordinated Recognition of a Virus Vulnerable Site International-journal Peer-reviewed

    Taishi Onodera, Shunsuke Kita, Yu Adachi, Saya Moriyama, Akihiko Sato, Takao Nomura, Shuhei Sakakibara, Takeshi Inoue, Takashi Tadokoro, Yuki Anraku, Kohei Yumoto, Cong Tian, Hideo Fukuhara, Michihito Sasaki, Yasuko Orba, Nozomi Shiwa, Naoko Iwata, Noriyo Nagata, Tateki Suzuki, Jiei Sasaki, Tsuyoshi Sekizuka, Keisuke Tonouchi, Lin Sun, Shuetsu Fukushi, Hiroyuki Satofuka, Yasuhiro Kazuki, Mitsuo Oshimura, Tomohiro Kurosaki, Makoto Kuroda, Yoshiharu Matsuura, Tadaki Suzuki, Hirofumi Sawa, Takao Hashiguchi, Katsumi Maenaka, Yoshimasa Takahashi

    Immunity　54　(10)　2385-2398　2021/08

    Publisher: Elsevier BV

    DOI： 10.1016/j.immuni.2021.08.025 　

    ISSN： 1074-7613

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    Potent neutralizing SARS-CoV-2 antibodies often target the spike protein receptor-binding site (RBS), but the variability of RBS epitopes hampers broad neutralization of multiple sarbecoviruses and drifted viruses. Here, using humanized mice, we identified an RBS antibody with a germline VH gene that potently neutralized SARS-related coronaviruses, including SARS-CoV and SARS-CoV-2 variants. X-ray crystallography revealed coordinated recognition by the heavy chain of non-RBS conserved sites and the light chain of RBS with a binding angle mimicking the angiotensin-converting enzyme 2 (ACE2) receptor. The minimum footprints in the hypervariable region of RBS contributed to the breadth of neutralization, which was enhanced by immunoglobulin G3 (IgG3) class switching. The coordinated binding resulted in broad neutralization of SARS-CoV and emerging SARS-CoV-2 variants of concern. Low-dose therapeutic antibody treatment in hamsters reduced the virus titers and morbidity during SARS-CoV-2 challenge. The structural basis for broad neutralizing activity may inform the design of a broad spectrum of therapeutics and vaccines.

  13. Immunization method for multi-pass membrane proteins using highly metastatic cell lines International-journal Peer-reviewed

    Hiroyuki Satofuka, Yoko Okabe, Yuki Takano, Takahiko Utsugi, Masaya Ohtsu, Yasufumi Murakami

    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS　450　(1)　99-104　2014/07

    DOI： 10.1016/j.bbrc.2014.05.065 　

    ISSN： 0006-291X

    eISSN： 1090-2104

  14. Ea10Mab-3: A Novel Anti-EphA10 Monoclonal Antibody for Flow Cytometry

    Keisuke Shinoda, Hiroyuki Suzuki, Takuya Nakamura, Yukari Ogura, Reina Ito, Hiroyuki Satofuka, Tomohiro Tanaka, Mika K. Kaneko, Yukinari Kato

    2026/06/04

    DOI： 10.20944/preprints202606.0383.v1 　

  15. Chimeric Anti-Glypican 1 Antibodies Exert Antitumor Activities in Xenograft Models of Lung and Pancreatic Cancers International-journal

    Haruto Yamamoto, Hiroyuki Suzuki, Tomokazu Ohishi, Hiroyuki Satofuka, Mika K. Kaneko, Yukinari Kato

    International Journal of Molecular Sciences　27　(10)　2026/05/08

    DOI： 10.3390/ijms27104181 　

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    Glypican-1 (GPC1) has emerged as a critical mediator of malignant tumor progression. GPC1 plays essential roles in regulating various signaling pathways involved in tumor cell proliferation, invasiveness, and tumorigenesis. Overexpression of GPC1 in tumors mediates oncogenic transformation, epithelial-to-mesenchymal transition, metastatic dissemination, and therapeutic resistance. Accordingly, GPC1-targeted therapeutic strategies have been investigated in clinical and preclinical studies. However, clinical efficacy has been limited. We previously developed an anti-GPC1 monoclonal antibody (mAb), G1Mab-28 (mouse IgG1, κ), which exhibits high affinity and specificity for GPC1. In the present study, we generated recombinant isotype-converted G1Mab-28, including G1Mab-28-mG2a (mouse IgG2a) and G1Mab-28-hG1 (human IgG1). Both mAbs recognized GPC1-expressing human tumor cell lines, including lung squamous cell carcinoma PC-10 and pancreatic ductal adenocarcinoma PK-45H, by flow cytometry. Moreover, both mAbs exerted antibody-dependent cellular cytotoxicity and complement-dependent cytotoxicity against those cell lines. In mouse xenograft models, treatment with the mAbs resulted in potent antitumor efficacy against PC-10 and PK-45H tumors. Collectively, these findings support the therapeutic potential of G1Mab-28 for the treatment of GPC1-positive tumors.

  16. Antitumor Activities of Chimeric Anti-EphA2 Antibodies in Xenograft Models of Breast, Pancreatic, and Colorectal Cancers International-journal

    Guanjie Li, Hiroyuki Suzuki, Tomokazu Ohishi, Hiroyuki Satofuka, Kenichiro Ishikawa, Kai Shimizu, Airi Nomura, Haruto Araki, Naoki Kojo, Kaito Suzuki, Saori Handa, Takuro Nakamura, Miyuki Yanaka, Tomohiro Tanaka, Mika K. Kaneko, Yukinari Kato

    International Journal of Molecular Sciences　27　(7)　2026/04/02

    DOI： 10.3390/ijms27073221 　

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    Erythropoietin-producing hepatocellular receptor A2 (EphA2) has emerged as a key mediator that promotes tumor malignant progression. EphA2 overexpression and its non-canonical signaling lead to oncogenic transformation, metabolic reprogramming, resistance to treatments, and metastasis. Therefore, strategies targeting EphA2 have been evaluated in clinical trials. However, the clinical effects were not sufficient. An anti-EphA2 monoclonal antibody (mAb), Ea2Mab-7 (mouse IgG1, κ), demonstrated high affinity and specificity among Eph receptors. In this study, we produced recombinant class-switched Ea2Mab-7 variants, including Ea2Mab-7-mG2a (mouse IgG2a) and Ea2Mab-7-hG1 (human IgG1). Both Ea2Mab-7-mG2a and Ea2Mab-7-hG1 recognized human triple-negative breast cancer MDA-MB-231, pancreatic cancer MIA PaCa-2, and colorectal cancer HCT-15 in flow cytometry. Furthermore, both Ea2Mab-7-mG2a and Ea2Mab-7-hG1 exerted significant antibody-dependent cellular cytotoxicity and complement-dependent cytotoxicity against these tumors. In mouse xenograft models of breast, pancreatic, and colorectal cancers, both mAbs demonstrated antitumor activity. These results indicate the potential of Ea2Mab-7 variants for the treatment of EphA2-positive cancers.

  17. Development of a novel anti-human glypican 5 monoclonal antibody (G5Mab-1) for multiple applications International-journal Peer-reviewed

    Yu Kaneko, Tomohiro Tanaka, Shiori Fujisawa, Guanjie Li, Hiroyuki Satofuka, Mika K. Kaneko, Hiroyuki Suzuki, Yukinari Kato

    Biochemistry and Biophysics Reports　43　102140-102140　2025/09

    DOI： 10.1016/j.bbrep.2025.102140 　

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    Glypican 5 (GPC5) is a member of heparan sulfate proteoglycans and is anchored to the plasma membrane via glycosylphosphatidylinositol. GPC5 plays an essential role in kidney, limb, and brain development. Furthermore, GPC5 is expressed in some cancers, but whether it functions as a cancer-promoting or -suppressing factor remains unclear. Therefore, the development of versatile and specific anti-GPC5 monoclonal antibodies (mAbs) is desired to clarify the biological and pathological functions of GPC5. In this study, we successfully established an anti-human GPC5 mAb (clone G5Mab-1) using the Cell-Based Immunization and Screening method. G5Mab-1 is capable of using flow cytometric analysis. G5Mab-1 is specifically bound only to GPC5, not to the other GPC family members. The dissociation constant value of G5Mab-1 for GPC5-overexpressed Chinese hamster ovary K-1 (CHO/GPC5) cells was determined as 9.9 × 10-9 M. Furthermore, G5Mab-1 detected GPC5 in Western blot and immunohistochemistry using CHO/GPC5 cells. Therefore, the G5Mab-1 is highly versatile for basic research and is expected to contribute to clinical applications, such as antibody-based therapy and diagnosis of cancer.

  18. Targeting of bowel tissue by fully human antibodies cross-reactive with human and mouse GPA33 antigen. International-journal

    Genki Hichiwa, Abdur Rafique, Asaki Nagashima, Yayan Wang, Kanako Kazuki, Ryohei Ogihara, Muhammad Feisal Jatnika, Ryosuke Shimamoto, Yumi Iwai, Narumi Uno, Hiroyuki Satofuka, Kazuma Tomizuka, Yuji Ito, Yasuhiro Kazuki

    Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie　189　118336-118336　2025/08

    DOI： 10.1016/j.biopha.2025.118336 　

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    Monoclonal antibodies are indispensable therapeutic agents for various diseases, including cancer, autoimmune disorders, and infectious diseases. Glycoprotein A33 (GPA33), a cell surface antigen highly expressed in colorectal cancer, provides a compelling therapeutic target; however, the species-specificity of anti-GPA33 antibodies has limited their utility in preclinical models, thus inhibiting their development. Here, we generated and characterized fully human, cross-reactive anti-GPA33 antibodies using phage-display technology with transchromosomic antibody-producing animals. The resulting single-chain variable fragment and single-chain variable fragment crystallizable antibodies exhibited high specificity and affinity for both human and mouse GPA33. In vivo imaging confirmed their targeted retention in mouse intestine, indicating their potential for developing targeted therapeutic approaches. The ability of these antibodies to recognize both human and murine GPA33 enhances their applicability in preclinical models, improving their translation from experimental to clinical applications. These results highlight the feasibility of developing cross-reactive, fully human antibodies and support the advancement of GPA33-targeted diagnostic approaches and the exploration of novel therapeutic strategies for relevant gastrointestinal diseases.

  19. C7Mab-2: A novel monoclonal antibody against mouse CCR7 established by immunization of the extracellular loop domain

    Haruto Yamamoto, Hiroyuki Suzuki, Tomohiro Tanaka, Hiroyuki Satofuka, Mika K. Kaneko, Yukinari Kato

    Microbes & Immunity　3　(1)　172-172　2025/07/02

    Publisher: AccScience Publishing

    DOI： 10.36922/mi025130028 　

    ISSN： 3041-0886

    eISSN： 3029-2883

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    The chemokine receptors possess seven transmembrane helices connected by an extracellular N‐terminal region, three extracellular loops (ECL1–3), three intracellular loops, and an intracellular C‐terminal region. Specific monoclonal antibodies (mAbs) against chemokine receptors for flow cytometry have been developed using Cell-Based Immunization and Screening, and the N-terminal peptide immunization methods. However, there are few reports on the establishment of anti-chemokine receptor mAbs through immunization with ECL peptides. Here, an anti-mouse C–C chemokine receptor type 7 (mCCR7) mAb, C7Mab-2 (rat immunoglobulin G2b, kappa), was established through immunization with the ECL3 peptide. C7Mab-2 demonstrated reactivity to mCCR7-overexpressed Chinese hamster ovary-K1 (CHO/mCCR7) cells in flow cytometry, which was inhibited by the ECL3 peptide. C7Mab-2 did not show cross-reactivity with other mouse CC, CXC, CX3C, and XC chemokine receptors. The dissociation constant value of C7Mab-2 was determined to be 2.8 × 10−9 M for CHO/mCCR7 cells. Furthermore, C7Mab-2 detected mCCR7 in immunohistochemistry. This strategy could accelerate the development of novel chemokine receptor mAbs with high affinity and specificity.

  20. A novel anti-mouse CXCR1 monoclonal antibody, Cx1Mab-8, demonstrates nanomolar affinity in flow cytometry. International-journal Peer-reviewed

    Guanjie Li, Hiroyuki Suzuki, Tomohiro Tanaka, Hiroyuki Satofuka, Mika K Kaneko, Yukinari Kato

    Biochemistry and biophysics reports　42　101965-101965　2025/06

    DOI： 10.1016/j.bbrep.2025.101965 　

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    CXC chemokine receptor 1 (CXCR1) is an important regulator for neutrophil granulocyte activation through binding to the ligand interleukin-8 (IL-8). Upon binding to IL-8, CXCR1 activates downstream signaling, critical for innate and adaptive immune responses. The IL-8-CXCR1 axis also plays an important role in tumor progression, especially in the tumor microenvironment. CXCR1 antagonists or anti-IL-8 monoclonal antibodies (mAbs) have been developed and evaluated in clinical trials for inflammatory diseases and tumors. In this study, we developed novel mAbs for mouse CXCR1 (mCXCR1) using the N-terminal peptide immunization. Among the established anti-mCXCR1 mAbs, Cx1Mab-8 (rat IgG2b, kappa) recognized mCXCR1-overexpressed Chinese hamster ovary-K1 (CHO/mCXCR1) and mCXCR1-overexpressed LN229 (LN229/mCXCR1) by flow cytometry. The dissociation constant (K D) values of Cx1Mab-8 for CHO/mCXCR1 and LN229/mCXCR1 were determined as 4.1 × 10-10 M and 1.5 × 10-9 M, respectively. These results indicated that Cx1Mab-8 is useful for detecting mCXCR1 by flow cytometry with high affinity and could contribute to obtaining the proof of concept in preclinical studies.

  21. Development of a Novel Anti-Mouse CCR7 Monoclonal Antibody C7Mab-2 by Immunization of the Extracellular Loop Domain

    Haruto Yamamoto, Hiroyuki Suzuki, Tomohiro Tanaka, Hiroyuki Satofuka, Mika K. Kaneko, Yukinari Kato

    2025/03/10

    DOI： 10.20944/preprints202503.0581.v1 　

  22. Development of Novel Anti-Rhinoceros Podoplanin Monoclonal Antibodies for Flow Cytometry, Western Blot, and Immunohistochemistry

    Hiroyuki Suzuki, Shiori Fujisawa, Rena Ubukata, Tomohiro Tanaka, Airi Nomura, Keisuke Shinoda, Takuya Nakamura, Hiroyuki Satofuka, Guanjie Li, Mika K. Kaneko, Yukinari Kato

    2025/02/13

    DOI： 10.20944/preprints202502.0986.v1 　

  23. Establishment of a Highly-Sensitive and Specific anti-EphB2 Monoclonal Antibody Eb2Mab-12 for Flow Cytometry

    Rena Ubukata, Hiroyuki Suzuki, Miu Hirose, Hiroyuki Satofuka, Tomohiro Tanaka, Mika K. Kaneko, Yukinari Kato

    2025/01/07

    DOI： 10.20944/preprints202406.0704.v2 　

  24. Development of a Novel Anti-Erythropoietin-Producing Hepatocellular Receptor B6 Monoclonal Antibody Eb6Mab-3 for Flow Cytometry International-journal

    Tomohiro Tanaka, Yu Kaneko, Haruto Yamamoto, Guanjie Li, Shiori Fujisawa, Hiroyuki Satofuka, Keisuke Shinoda, Takuya Nakamura, Mika K Kaneko, Hiroyuki Suzuki, Yukinari Kato

    Biochemistry and biophysics reports　41　101960-101960　2024/12/16

    DOI： 10.20944/preprints202412.1235.v1 　

    More details Close

    Erythropoietin-producing hepatocellular receptor B6 (EphB6) is a member of the largest Eph subfamily of receptor tyrosine kinases. EphB6 is widely expressed in various tissues and regulates cellular homeostasis by interacting with its membrane-bound ephrin ligands and other receptors. EphB6 is involved in cancer pathology despite lacking kinase activity. Developing sensitive monoclonal antibodies (mAbs) for EphB6 has been desired for treatment, diagnosis, and further analysis of EphB6. This study established a novel specific and sensitive anti-human EphB6 mAb clone Eb6Mab-3 (mouse IgG1, kappa) by the Cell-Based Immunization and Screening (CBIS) method. In flow cytometry, Eb6Mab-3 demonstrated reactivity with EphB6-overexpressed Chinese hamster ovary-K1 cells (CHO/EphB6) and endogenously EphB6-expressing DLD-1 colorectal cancer cells. Cross-reactivity of Eb6Mab-3 was not observed. Eb6Mab-3 demonstrated a moderate binding affinity (dissociation constant; K D) for CHO/EphB6 (K D: 2.6 ± 1.0 × 10-8 M) and a high binding affinity for DLD-1 (K D: 3.4 ± 1.3 × 10-9 M). Eb6Mab-3 can detect EphB6 protein in CHO/EphB6 lysate in Western blot. Eb6Mab-3, established by the CBIS method, could be valuable for analyzing the EphB6-associated cellular functions and has potential applications in diagnosis and treatment with specificity and high affinity for cancer cells.

  25. Ea8Mab-9: A Novel Monoclonal Antibody Against Erythropoietin-Producing Hepatocellular Receptor A8 for Flow Cytometry

    Tomohiro Tanaka, Haruto Yamamoto, Yu Kaneko, Keisuke Shinoda, Takuya Nakamura, Guanjie Li, Shiori Fujisawa, Hiroyuki Satofuka, Mika K. Kaneko, Hiroyuki Suzuki, Yukinari Kato

    2024/12/12

    DOI： 10.20944/preprints202412.1044.v1 　

  26. Establishment of a Highly-sensitive Anti-EphB2 Monoclonal Antibody Eb2Mab-3 for Flow Cytometry

    Rena Ubukata, Hiroyuki Suzuki, Miu Hirose, Hiroyuki Satofuka, Tomohiro Tanaka, Mika K. Kaneko, Yukinari Kato

    2024/06/11

    DOI： 10.20944/preprints202406.0704.v1 　

  27. Establishment of an Antibody Specific for AMIGO2 Improves Immunohistochemical Evaluation of Liver Metastases and Clinical Outcomes in Patients with Colorectal Cancer International-journal Peer-reviewed

    Keisuke Goto, Mitsuhiko Osaki, Runa Izutsu, Hiroshi Tanaka, Ryo Sasaki, Akimitsu Tanio, Hiroyuki Satofuka, Yasuhiro Kazuki, Manabu Yamamoto, Hiroyuki Kugoh, Hisao Ito, Mitsuo Oshimura, Yoshiyuki Fujiwara, Futoshi Okada

    Diagnostic Pathology　17　(1)　16-16　2021/10/05

    Publisher: Research Square Platform LLC

    DOI： 10.1186/s13000-021-01176-2 　

    More details Close

    <title>Abstract</title> <bold>Instruction</bold>: The human amphoterin-induced gene and open reading frame (AMIGO) was identified as a novel cell adhesion molecule of type I transmembrane protein. AMIGO2 is one of three members of the AMIGO family (AMIGO1, 2, and 3), and the similarity between them is approximately 40% at the amino acid level. We have previously shown that AMIGO2 functions as a driver of liver metastasis. Immunohistochemical analysis of AMIGO2 expression in colorectal cancer (CRC) using a commercially available anti-AMIGO2 mouse monoclonal antibody clone sc-373699 (sc mAb) correlated with liver metastasis and poor prognosis. However, the sc mAb was found to be cross-reactive with all three molecules in the AMIGO family. <bold>Methods</bold>: We generated a rat monoclonal antibody clone rTNK1A0012 (rTNK mAb) for human AMIGO2. The rTNK mAb was used to re-evaluate the association between AMIGO2 expression and liver metastases/clinical outcomes using the same CRC tissue samples previously reported with sc mAb. <bold>Results</bold>: Western blot analysis revealed that a rTNK mAb was identified as being specific for AMIGO2 protein and did not cross-react with AMIGO1 and AMIGO3. The rTNK mAb and sc mAb showed higher AMIGO2 expression, which correlates with a high frequency of liver metastases (65.3% and 47.5%, respectively), while multivariate analysis showed that AMIGO2 expression was an independent prognostic factor for liver metastases (p = 7.930E-10 and p = 1.707E-5). The Kaplan-Meier analyses showed that the rTNK mAb (p = 0.004), but not sc mAb (p = 0.107), predicted worse overall survival in patients with high AMIGO2 expression. The relationship between AMIGO2 expression and poor disease-specific survival showed a higher level of significance for rTNK mAb (p = 0.00004) compared to sc mAb (p = 0.001). <bold>Conclusion</bold>: These results indicate that the developed rTNK1A0012 mAb is an antibody that specifically recognizes AMIGO2 by immunohistochemistry and can be a more reliable and applicable method for the diagnostic detection of liver metastases and worse prognosis in patients with high AMIGO2-expressing CRC.

  28. Nuclear beta-catenin and CD44 upregulation characterize invasive cell populations in non-aggressive MCF-7 breast cancer cells International-journal Peer-reviewed

    Masahiro Uchino, Hiroko Kojima, Kenta Wada, Mika Imada, Fumitoshi Onoda, Hiroyuki Satofuka, Takahiko Utsugi, Yasufumi Murakami

    BMC CANCER　10　414-414　2010/08

    DOI： 10.1186/1471-2407-10-414 　

    ISSN： 1471-2407

  29. Cellular toxicity of cadmium ions and their detoxification by heavy metal-specific plant peptides, phytochelatins, expressed in mammalian cells International-journal Peer-reviewed

    M Takagi, H Satofuka, S Amano, H Mizuno, Y Eguchi, K Hirata, K Miyamoto, K Fukui, T Imanaka

    JOURNAL OF BIOCHEMISTRY　131　(2)　233-239　2002/02

    ISSN： 0021-924X

  30. Apoptotic signal transduction by cadmium ion and detoxification by plant peptides Peer-reviewed

    M Takagi, H Satofuka, T Imanaka

    BIOLOGICAL SYSTEMS ENGINEERING　830　163-176　2002

    ISSN： 0097-6156

  31. Metal-binding properties of phytochelatin-related peptides Peer-reviewed

    H Satofuka, T Fukui, M Takagi, H Atomi, T Imanaka

    JOURNAL OF INORGANIC BIOCHEMISTRY　86　(2-3)　595-602　2001/09

    DOI： 10.1016/S0162-0134(01)00223-9 　

    ISSN： 0162-0134

  32. Anti-phytochelatin monoclonal antibody Peer-reviewed

    Hiroyuki Satofuka, Satoshi Amano, Toshiaki Fukui, Haruyuki Atomi, Masahiro Takagi & Tadayuki Imanaka

    Biotechnology Letters　22　(17)　1423-1428　2000/10/16

    DOI： 10.1023/A:1005673218300 　

    ISSN： 0141-5492

  33. Rapid method for detection and detoxification of heavy metal ions in water environments using phytochelatin Peer-reviewed

    H Satofuka, S Amano, H Atomi, M Takagi, K Hirata, K Miyamoto, T Imanaka

    JOURNAL OF BIOSCIENCE AND BIOENGINEERING　88　(3)　287-292　1999/09

    DOI： 10.1016/S1389-1723(00)80011-0 　

    ISSN： 1389-1723

Show all ︎Show first 5

Misc. 30

  1. 染色体工学技術による完全ヒト抗体産生動物を用いた腸組織指向性抗体-腸AcuumBodyの開発とIBD治療への応用

    飛知和弦輝, WANG Yayan, 飛知和弦輝, WANG Yayan, 荻原諒平, 香月加奈子, 永島明咲, MUHAMMAD Jatnika Feisal, 岩井優実, 嶋本亮輔, 本多英嗣, 宇野佳奈, 里深博幸, ABDUR Rafique, 宇野愛海, 冨塚一磨, 伊東祐二, 香月康宏, 香月康宏, 香月康宏, 香月康宏

    Journal of Toxicological Sciences (Web)　50　(Supplement 1)　2025

    ISSN： 1880-3989

  2. Application of chromosome engineering technology to antibody research (1) Generation and characterization of a bowel-targeting fully human antibody

    飛知和弦輝, 飛知和弦輝, 飛知和弦輝, RAFIQUE Abdur, 永島明咲, WANG Yayan, WANG Yayan, 香月加奈子, 荻原諒平, 本多英嗣, 宇野佳奈, MUHAMMAD Feisal Jatnika, 嶋本亮輔, 岩井優実, 宇野愛海, 里深博幸, 冨塚一磨, 伊東祐二, 香月康宏, 香月康宏, 香月康宏, 香月康宏

    日本抗体学会学術大会プログラム・抄録集(Web)　4th　2025

  3. 完全ヒト抗体産生動物×ファージディスプレイによる腸AccumBody作製と複合バイオロジクスへの応用

    飛知和弦輝, 飛知和弦輝, 岩井優実, 永島明咲, 嶋本亮輔, WANG Yayan, WANG Yayan, 荻原諒平, 香月加奈子, 本多英嗣, 宇野佳奈, 宇野愛海, RAFIQUE Abdur, 里深博幸, 冨塚一磨, 伊東祐二, 香月康宏, 香月康宏, 香月康宏, 香月康宏

    日本実験動物学会総会講演要旨集(Web)　71st　2024

  4. Application of chromosome engineering technology to antibody research (3) Isolation and characterization of Bowel AccumBody for therapeutic application.

    飛知和弦輝, 飛知和弦輝, RAFIQUE Abdur, 永島明咲, WANG Yayan, WANG Yayan, 荻原諒平, 香月加奈子, 本多英嗣, 宇野佳奈, 嶋本亮輔, 岩井優実, 宇野愛海, 里深博幸, 冨塚一磨, 伊東祐二, 香月康宏, 香月康宏, 香月康宏

    日本抗体学会学術大会プログラム・抄録集(Web)　3rd　2024

  5. 染色体工学技術の抗体研究への応用(4)完全ヒト抗体産生動物×ファージディスプレイ法による腸組織移行性抗体の獲得および次世代抗体医薬品への応用

    飛知和弦輝, 飛知和弦輝, 嶋本亮輔, 岩井優実, 西田昂平, 永島明咲, JATNIKA Feisal, WANG Yayan, WANG Yayan, 荻原諒平, 高島海, 高島海, 香月加奈子, 本多英嗣, 宇野佳奈, 宇野愛海, RAFIQUE Abdur, 里深博幸, 冨塚一磨, 香月康宏, 香月康宏, 香月康宏, 伊東祐二

    日本抗体学会学術大会プログラム・抄録集(Web)　2nd　2023

  6. Application of chromosome engineering technology (14): Analysis of antibody and B cell production in fully human antibody producing rats

    森脇崇史, 森脇崇史, 里深博幸, 阿部智志, 岡田茜, 香月加奈子, 濱道修生, 香月康宏, 香月康宏, 香月康宏

    日本分子生物学会年会プログラム・要旨集(Web)　46th　2023

  7. 抗体部位特異的修飾技術CCAP,tCAP法による多機能性抗体医薬染色体工学技術の抗体研究への応用(9)mammalian display法による抗SARS-Cov-2合成ヒトポリクローナル抗体取得

    安倍麻莉奈, 福島隆斗, 石津由紀, 宇野愛海, 平塚正治, 下谷和人, 森脇崇史, 里深博幸, 濱道修生, 金井亨輔, 景山誠二, 香月康宏, 末次正幸, 冨塚一磨

    日本抗体学会学術大会プログラム・抄録集(Web)　2nd　2023

  8. 染色体工学技術の抗体研究への応用(10)Mammalian display法による抗SARS-CoV-2合成ヒトモノクローナル抗体取得法の開発

    宇野愛海, 安倍麻莉奈, 福島隆斗, 石津由紀, 冨塚一磨, 平塚正治, 下谷和人, 森脇崇史, 里深博幸, 濱道修生, 金井亨輔, 景山誠二, 香月康宏, 末次正幸

    日本抗体学会学術大会プログラム・抄録集(Web)　2nd　2023

  9. Application of chromosome engineering technology (4): Generation of trans-chromosomic mice by direct injection of microcells with mouse artificial chromosome

    水谷英二, 里深博幸, 山崎匡太郎, 遠藤猛, 松岡美伶, 岡田茜, 香月康宏, 香月康宏, 香月康宏

    日本分子生物学会年会プログラム・要旨集(Web)　46th　2023

  10. 染色体工学技術の抗体研究への応用(2)完全ヒト抗体産生ラット(TC-mAbラット)の作製と抗体レパトアの解析

    里深博幸, 森脇崇史, 阿部智志, 岡田茜, 香月加奈子, 濱道修生, 香月康宏, 香月康宏

    日本抗体学会学術大会プログラム・抄録集(Web)　1st　2022

  11. 染色体工学技術の抗体研究への応用(11)完全ヒト抗体産生マウスを用いた迅速なヒト抗体作製技術の開発

    下谷和人, 濱道修生, 里深博幸, 大安知里, 遠藤猛, 金澤伊織, 森本佳世子, 高山悠, 嵩原昇子, 押村光雄, 富塚一磨, 香月康宏, 香月康宏

    日本抗体学会学術大会プログラム・抄録集(Web)　1st　2022

  12. Application of chromosome engineering technology (1): Efficiently micronucleation and chromosome transfer in CHO cells using inhibitors of chromosome distribution mechanisms and mitotic checkpoints

    宇野愛海, 里深博幸, 宮本人丸, 本間和久, 鈴木輝彦, 山崎匡太郎, 伊東涼太, 森脇崇史, 冨塚一磨, 押村光雄, 香月康宏, 香月康宏, 香月康宏

    日本分子生物学会年会プログラム・要旨集(Web)　45th　2022

  13. Novel therapeutic approach for cancer using chromosome engineering techniques

    久郷裕之, 里深博幸, 大平崇人, 大平崇人, 平塚正治, 平塚正治, 香月加奈子, 森脇崇史, 森脇崇史, 香月康宏, 香月康宏

    日本がん転移学会学術集会・総会プログラム抄録集　30th　2021

  14. Application of chromosome engineering technology (19): Development of new chromosome transfer technology for cell therapy using human iPS cells as a chromosome donor.

    宮本人丸, 宇野愛海, 黛亮太, 川崎元希, 里深博幸, 冨塚一磨, 香月康宏, 香月康宏

    日本分子生物学会年会プログラム・要旨集(Web)　44th　2021

  15. Application of chromosome engineering technology (16): Design of highly functionalized mesenchymal stem cell medicine using human artificial chromosomes(HAC)

    小野寺千紘, 宮崎夏美, 宇野愛海, 山内玲奈, 山内玲奈, 石津由紀, 若狭由布子, 黛亮太, 里深博幸, 香月康宏, 香月康宏, 冨塚一磨

    日本分子生物学会年会プログラム・要旨集(Web)　44th　2021

  16. Application of chromosome engineering technology (13): Development of inducibly diversified antibody-expressing cell library that enables antibody phenotypic screening

    橋本七海, 笹川航, 宇野愛海, 里深博幸, 香月康宏, 香月康宏, 堀田秋津, 冨塚一磨

    日本分子生物学会年会プログラム・要旨集(Web)　44th　2021

  17. Discovery of novel drug target against triple negative breast cancer from fully human phage library

    飛知和弦輝, 里深博幸, 押村光雄, RAFIQUE Abdur, 伊東祐二, 香月康宏, 香月康宏

    日本がん転移学会学術集会・総会プログラム抄録集　30th　2021

  18. Application of chromosome engineering technology (9): Generation of internalizing monoclonal antibodies using fully human antibody-producing mice and their comprehensive analyses by cytotoxicity-based assay systems

    下谷和人, 下谷和人, 里深博幸, 貞包和樹, 貞包和樹, 飛知和弦輝, 飛知和弦輝, 香月康宏, 香月康宏, 香月康宏

    日本分子生物学会年会プログラム・要旨集(Web)　44th　2021

  19. Application of chromosome engineering technology (10): Development of a simple technique for producing monoclonal antibodies using protein probes

    日本分子生物学会年会プログラム・要旨集(Web)　44th　2021

  20. Comparison of screening methods suitable for fully human antibody-drug conjugate development

    WANG Yayan, WANG Yayan, 里深博幸, 山崎匡太郎, 三宅直美, 福原武志, 押村光雄, XU Gao, 香月康宏, 香月康宏

    日本がん転移学会学術集会・総会プログラム抄録集　30th　2021

  21. 新型コロナウイルスspike蛋白質と中和抗体NT-193複合体のX線結晶構造解析

    喜多俊介, 小野寺大志, 安達悠, 森山彩野, 野村尚生, 田所高志, 安楽佑樹, 湯本航平, 田聡, 福原秀雄, 鈴木干城, 佐々木慈英, 福士秀悦, 里深博幸, 香月康宏, 押村光雄, 橋口隆生, 高橋宜聖, 前仲勝実

    日本結晶学会年会講演要旨集　2021　2021

  22. The analysis of immune response in fully human antibody-producing TC-mAb mice

    森脇崇史, 里深博幸, 阿部智志, 田中博志, 山崎匡太郎, 飛知和弦輝, 冨塚一磨, 押村光雄, 香月康宏, 香月康宏

    日本がん転移学会学術集会・総会プログラム抄録集　30th　2021

  23. 完全ヒト抗体産生マウスを用いた研究(1):ヒト抗体遺伝子全長を搭載した人工染色体を保持するtrans-chromosomicマウスのレパトア解析

    里深博幸, 森脇崇史, 森脇崇史, 阿部智志, 田中博志, 森本佳世子, 山崎匡太郎, 冨塚一磨, 押村光雄, 香月康宏, 香月康宏

    日本分子生物学会年会プログラム・要旨集(Web)　43rd　2020

  24. ヒト/マウス人工染色体技術応用(4):生きた細胞内における人工染色体の蛍光標識法

    松尾京亮, 里深博幸, 山崎匡太郎, 本間和久, 押村光雄, 香月康宏, 香月康宏

    日本分子生物学会年会プログラム・要旨集(Web)　42nd　2019

  25. ヒト/マウス人工染色体技術応用(12):EpCAMをモデル抗原とした完全ヒト抗体産生マウスの免疫と完全ヒトモノクローナル抗体の作製

    山崎匡太郎, 里深博幸, 阿部智志, 森脇崇史, 田中博志, 押村光雄, 香月康宏, 香月康宏

    日本分子生物学会年会プログラム・要旨集(Web)　42nd　2019

  26. ヒト/マウス人工染色体技術応用(11):完全ヒト抗体産生マウスの免疫応答に関する解析

    里深博幸, 森脇崇史, 田中博志, 阿部智志, 山崎匡太郎, 富塚一磨, 押村光雄, 香月康宏, 香月康宏

    日本分子生物学会年会プログラム・要旨集(Web)　42nd　2019

  27. ヒト/マウス人工染色体技術応用(13):完全ヒトポリクローナル抗体を用いたがん治療薬の開発

    飛知和弦輝, 里深博幸, 押村光雄, 香月康宏, 香月康宏

    日本分子生物学会年会プログラム・要旨集(Web)　42nd　2019

  28. Heavy metal-binding and detoxification properties of phytochelatin-related peptides.

    Satofuka Hiroyuki, Fukui Toshiaki, Atomi Haruyuki, Takagi Masahiro, Imanaka Tadayuki

    13　276-276　2001

    Publisher: 日本生物工学会

  29. Functional analysis of analogues of a heavy metal-binding peptide, phytochelatin.

    Satofuka Hiroyuki, Fukui Toshiaki, Takagi Masahiro, Atomi Haruyuki, Imanaka Tadayuki

    12　95-95　2000

    Publisher: 日本生物工学会

  30. Induction of anti-phytochelatin monoclonal antibodies and cloning and sequencing of the genes encoding H and L chain variable regions.

    Satofuka Hiroyuki, Amano Satoshi, Takagi Masahiro, Atomi Haruyuki, Imanaka Tadayuki

    10　49-49　1998

    Publisher: 日本生物工学会

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Books and Other Publications 1

  1. Clinical Immunology & Allergology

    2023/04

Industrial Property Rights 15

  1. タンパク質−微粒子複合体、及びそれを用いた標的生体物質の検出方法

    里深 博幸

    Property Type: Patent

  2. 目的抗原に対する抗体の作製方法

    里深 博幸, 岡部 洋子

    Property Type: Patent

  3. 抗SLC6A6抗体を用いたがん治療用医薬組成物

    里深 博幸, 岡部 洋子, 大瀬 賢介, 向畑 成樹, 村上 康文

    Property Type: Patent

  4. 浸潤能の高い癌細胞の検出用又は診断用試薬

    里深 博幸, 岡部 洋子

    Property Type: Patent

  5. 抗SLC6A6抗体を用いたがん治療用医薬組成物

    里深 博幸, 大瀬 賢介, 向畑 成樹, 秋山 弘匡, 大津 正也, 岡部 洋子, 村上 康文

    Property Type: Patent

  6. 抗LGR6抗体を含む癌の検出用又は診断用試薬

    里深 博幸, 村上 康文

    Property Type: Patent

  7. がん治療用医薬組成物

    里深 博幸, 大瀬 賢介, 向畑 成紀, 加藤 由美子, 岡部 洋子, 松村 保広, 安永 正浩

    Property Type: Patent

  8. 大腸がんマーカーに対する抗体

    里深 博幸, 岡部 洋子, 松村 保広, 安永 正浩

    Property Type: Patent

  9. がん細胞を用いた抗体の製造方法

    里深 博幸, 内野 雅浩, 花岡 慎悟

    Property Type: Patent

  10. がん細胞を用いた免疫方法

    里深 博幸, 内野 雅浩, 小島 弘子

    Property Type: Patent

  11. 表面プラズモン共鳴による物質の検出方法

    里深 博幸

    Property Type: Patent

  12. 造血幹細胞の分化抑制又は増殖方法

    戸所 一雄, 里深 博幸, 桑原 義和

    Property Type: Patent

  13. 重金属の測定方法および回収方法

    今中 忠行, 里深 博幸, 高木 昌宏

    Property Type: Patent

  14. がん治療用医薬組成物

    里深 博幸, 大瀬 賢介, 向畑 成紀, 加藤 由美子, 岡部 洋子, 松村 保広, 安永 正浩

    特許第5747283号

    Property Type: Patent

  15. がん細胞を用いた免疫方法

    里深 博幸, 内野 雅浩, 小島 弘子

    特許第5688699号

    Property Type: Patent

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Research Projects 1

  1. Development of an analytical method for virus neutralizing mAbs using surface IgG of hybridoma cells

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research

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

    Institution: Tohoku University

    2024/04/01 - 2027/03/31