| 1. |
C. W. Kim, R. Toita, J.-H. Kang, T. Mori, A. Kishimura, Y. Katayama*, Protein kinase C α-responsive gene carrier for cancer-specific transgene expression and cancer therapy, ACS Biomater. Sci. Eng., 10.1021/acsbiomaterials.1c00213, 2021.04. |
| 2. |
C. W. Kim, R. Toita, J.-H. Kang, T. Mori, A. Kishimura, Y. Katayama*, Protein kinase C α-responsive gene carrier for cancer-specific transgene expression and cancer therapy, ACS Biomater. Sci. Eng., 10.1021/acsbiomaterials.1c00213, 2021.04. |
| 3. |
T. Nobori, A. Kishimura, T. Mori*, Y. Katayama*, A FRET-based Protein Kinase Assay using Phos-tag-modified Quantum Dots and Fluorophore-labeled Peptides, Anal. Sci., 10.2116/analsci.20P443, 2021.10. |
| 4. |
Y. Mu, Y. Kinashi, J. Li, T. Yoshikawa, A. Kishimura, M. Tanaka, T. Matsui, T. Mori*, K. Hase*, Y. Katayama*, Polyvinyl butyrate nanoparticles as butyrate donors for colitis treatment, ACS Applied Bio Mater., https://doi.org/10.1021/acsabm.0c01105, 4, 2335-2341, 2021.02. |
| 5. |
K. Sasaki, K. Muguruma, R. Osawa, A. Fukuda, A. Taniguchi, A. Kishimura, Y. Hayashi*, T. Mori*, Y. Katayama*, Synthesis and biological evaluation of a monocyclic Fc-binding antibody-recruiting molecule for cancer immunotherapy, RSC Med. Chem., https://doi.org/10.1039/D0MD00337A, 12, 406-409, 2021.02. |
| 6. |
1. K. Sasaki, M. Harada, T. Yoshikawa, H. Tagawa, Y. Harada, Y. Yonemitsu, T. Ryujin, A. Kishimura, T. Mori*, Y. Katayama*, Fc-binding antibody-recruiting molecules targeting prostate-specific membrane antigen: defucosylation of antibody for efficacy improvement, ChemBioChem, https://doi.org/10.26434/chemrxiv.12654602.v1, 22, 496-500, 2021.02. |
| 7. |
14. Y. Mu, Y. Kinashi, A. Kishimura, T. Mori*, K. Hase*, Y. Katayama*, Effect of polyvinyl butyrate nanoparticles incorporated with immune suppressing vitamins on alteration of population of intestinal immune cells, Prog. Nat. Sci. Mater. Int., https://doi.org/10.1016/j.pnsc.2020.10.003, 30, 707-710, 2020.10. |
| 8. |
X. Sun, R. Tokunaga, Y. Nagai, R. Miyahara, A. Kishimura, S. Kawakami, Y. Katayama*, T. Mori*, Ligand design for specific MHC class I molecules on the cell surface, Biochemistry, https://doi.org/10.1021/acs.biochem.0c00735, 59, 4646-4653, 2020.12. |
| 9. |
Hiroshi Tagawa, Katsuya Maruyama, Koichi Sasaki, Natsuki Konoue, Akihiro Kishimura, Motomu Kanai, Takeshi Mori, Kounosuke Oisaki, Yoshiki Katayama, Induction of ADCC by a folic acid-mAb conjugate prepared by tryptophan-selective reaction toward folate-receptor-positive cancer cells, RSC Advances, 10.1039/d0ra03291c, 10, 28, 16727-16731, 2020.04, We developed conjugates between monoclonal antibody (mAb) and folic acid (FA) by using a tryptophan (Trp)-selective reaction, which yields relatively homogenous products compared to conventional methods. The obtained mAb-FA conjugates showed significant cellular cytotoxicity toward folate receptor-expressing cancer cells, demonstrating that the conjugates retained the Fc region's original function.. |
| 10. |
Koichi Sasaki, Minori Harada, Yoshiki Miyashita, Hiroshi Tagawa, Akihiro Kishimura, Takeshi Mori, Yoshiki Katayama, Fc-binding antibody-recruiting molecules exploit endogenous antibodies for anti-tumor immune responses, Chemical Science, 10.1039/d0sc00017e, 11, 12, 3208-3214, 2020.03, Redirecting endogenous antibodies in the bloodstream to tumor cells using synthetic molecules is a promising approach to trigger anti-tumor immune responses. However, current molecular designs only enable the use of a small fraction of endogenous antibodies, limiting the therapeutic potential. Here, we report Fc-binding antibody-recruiting molecules (Fc-ARMs) as the first example addressing this issue. Fc-ARMs are composed of an Fc-binding peptide and a targeting ligand, enabling the exploitation of endogenous antibodies through constant affinity to the Fc region of antibodies, whose sequence is conserved in contrast to the Fab region. We show that Fc-ARM targeting folate receptor-α (FR-α) redirects a clinically used antibody mixture to FR-α+ cancer cells, resulting in cancer cell lysis by natural killer cells in vitro. Fc-ARMs successfully interacted with antibodies in vivo and accumulated in tumors. Furthermore, Fc-ARMs recruited antibodies to suppress tumor growth in a mouse model. Thus, Fc-ARMs have the potential to be a novel class of cancer immunotherapeutic agents.. |
| 11. |
Takanobu Nobori, Masumi Kawamura, Ryosuke Yoshida, Taisei Joichi, Kenta Kamino, Akihiro Kishimura, Eishi Baba, Takeshi Mori, Yoshiki Katayama, Fluorescence Signal Amplification by Using β-Galactosidase for Flow Cytometry; Advantages of an Endogenous Activity-Free Enzyme, Analytical chemistry, 10.1021/acs.analchem.9b04471, 92, 4, 3069-3076, 2020.02, We previously proposed using a hydrolysis enzyme for fluorescent signal amplification in flow cytometric detection of antigen proteins, which was named the catalyzed reporter penetration (CARP) method. In this method, antigen proteins are labeled with enzyme-modified antibodies, and then fluorophore-modified substrates stain cells by penetrating the cell membrane upon hydrolysis of the substrate. We proved the concept by using alkaline phosphatase (AP) as the hydrolysis enzyme. However, a required prior inactivation process of endogenous AP activity on the cell surface risked disrupting recognition of antigen proteins by antibodies. In this report, the CARP method was extended to β-galactosidase (β-gal) as an amplification enzyme, which circumvented the requirement of an initial inactivation process because endogenous β-gal activity on the surface of examined cells was found to be negligible. The substrate structure for β-gal was optimized and used for the CARP method. The CARP method showed significantly higher fluorescent signals than a conventional method using fluorophore-modified antibodies. Moreover, the degree of amplification of the fluorescence signal was higher for antigens with low expression levels, showing that the CARP method is a suitable signal amplification method over current conventional approaches.. |
| 12. |
＃K. Zai, M. Hirota, T. Yamada, N. Ishihara, T. Mori, A. Kishimura, K. Suzuki, K. Hase, Y. Katayama, Therapeutic effect of vitamin D3-containing nanostructured lipid carriers on inflammatory bowel disease, J. Controlled Release, https://doi.org/10.1016/j.jconrel.2018.07.019, 286, 94-102, 2018.09. |
| 13. |
K. Sasaki, Y. Miyashita, D. Asai, D. Funamoto, K. Sato, Y. Yamaguchi, Y. Mishima, T. Iino, S. Takaishi, J. Nagano, A. Kishimura, T. Mori, Y. Katayama, A Peptide Inhibitor of Antibody-Dependent Cell-Mediated Cytotoxicity against EGFR/Folate Receptor-α Double Positive Cells, Med. Chem. Commun., 10.1039/C8MD00010G, 9, 783-788, 2018.05. |
| 14. |
T. Nobori, K. Tosaka, A. Kawamura, T. Joichi, K. Kamino, A. Kishimura, E. Baba, T. Mori, Y. Katayama, Alkaline Phosphatase-Catalyzed Amplification of a Fluores-cence Signal for Flow Cytometry, Langmuir, 10.1021/acs.analchem.7b03893, 90, 2, 1059-1062, 2018.01. |
| 15. |
E. Nakahei, K. Takehara, H. Sato, EK. Zai, A. Kishimura, T. Mori, Y. Katayama, Ligand design for cancer imaging with long blood circulation and enhanced accumulation ability in tumors, Med. Chem. Commun, 10.1039/C8MD00010G, ９, 783-788, 2018.02. |
| 16. |
E. Nakahei, K. Takehara, H. Sato, K. Zai, A. Kishimura, T. Mori, Y. Katayama, A Dual Alkylated Peptide-ligand Enhances Affinity to Human Serum Albumin, Anal. Sci, 10.2116/analsci.17P614, 31, 4, 501-504, 2018.04. |
| 17. |
Elnaz Nakhaei, Chan Woo Kim, Daiki Funamoto, Hikari Sato, Yuta Nakamura, Akihiro Kishimura, Takeshi Mori, Yoshiki Katayama, Ligand design for cancer imaging with long blood circulation and enhanced accumulation ability in tumors, Med. Chem. Comm., DOI: 10.1039/c7md00102a, 2017.04. |
| 18. |
Cui Cui Li, Masafumi Takeo, Masayoshi Matsuda, Hiroko Nagai, Sun Xizheng, Wataru Hatanaka, Hiroyuki Inoue, Kenzaburo Tani, Akihiro Kishimura, Takeshi Mori, Yoshiki Katayama, Fabrication of Dendrimer‐Based Polyion Complex Submicrometer‐Scaled Structures with Enhanced Stability under Physiological Conditions, MedChemComm, DOI: 10.1039/C7MD00188F, 2017.04. |
