ID | 66889 |
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Takahashi, Tetta
Department of Cell Biology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Tomonobu, Nahoko
Department of Cell Biology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Kinoshita, Rie
Department of Cell Biology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
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Yamamoto, Ken-Ichi
Department of Cell Biology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Murata, Hitoshi
Department of Cell Biology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
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Komalasari, Ni Luh Gede Yoni
Faculty of Medicine, Udayana University
Chen, Youyi
Department of Breast Surgery, The First Affiliated Hospital, Zhejiang University School of Medicine
Jiang, Fan
Department of Cell Biology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Gohara, Yuma
Department of Cell Biology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Ochi, Toshiki
Department of Cell Biology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Ruma, I. Made Winarsa
Faculty of Medicine, Udayana University
Sumardika, I. Wayan
Faculty of Medicine, Udayana University
Zhou, Jin
Medical Oncology Department of Gastrointestinal Tumors, Liaoning Cancer Hospital & Institute, Cancer Hospital of the Dalian University of Technology
Honjo, Tomoko
Department of Interdisciplinary Science and Engineering in Health Systems, Okayama University
Sakaguchi, Yoshihiko
Department of Microbiology, Tokushima Bunri University
Yamauchi, Akira
Department of Biochemistry, Kawasaki Medical School
Kuribayashi, Futoshi
Department of Biochemistry, Kawasaki Medical School
Kondo, Eisaku
Division of Tumor Pathology, Near InfraRed Photo-Immuno-Therapy Research Institute, Kansai Medical University
Inoue, Yusuke
Faculty of Science and Technology, Division of Molecular Science, Gunma University
Futami, Junichiro
Department of Interdisciplinary Science and Engineering in Health Systems, Okayama University
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Toyooka, Shinichi
Department of General Thoracic Surgery and Breast and Endocrinological Surgery, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
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Zamami, Yoshito
Department of Pharmacy, Okayama University Hospital
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Sakaguchi, Masakiyo
Department of Cell Biology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
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Abstract | Background: Our earlier research revealed that the secreted lysyl oxidase-like 4 (LOXL4) that is highly elevated in triple-negative breast cancer (TNBC) acts as a catalyst to lock annexin A2 on the cell membrane surface, which accelerates invasive outgrowth of the cancer through the binding of integrin-β1 on the cell surface. However, whether this machinery is subject to the LOXL4-mediated intrusive regulation remains uncertain.
Methods: Cell invasion was assessed using a transwell-based assay, protein–protein interactions by an immunoprecipitation–Western blotting technique and immunocytochemistry, and plasmin activity in the cell membrane by gelatin zymography. Results: We revealed that cell surface annexin A2 acts as a receptor of plasminogen via interaction with S100A10, a key cell surface annexin A2-binding factor, and S100A11. We found that the cell surface annexin A2/S100A11 complex leads to mature active plasmin from bound plasminogen, which actively stimulates gelatin digestion, followed by increased invasion. Conclusion: We have refined our understanding of the role of LOXL4 in TNBC cell invasion: namely, LOXL4 mediates the upregulation of annexin A2 at the cell surface, the upregulated annexin 2 binds S100A11 and S100A10, and the resulting annexin A2/S100A11 complex acts as a receptor of plasminogen, readily converting it into active-form plasmin and thereby enhancing invasion. |
Keywords | breast cancer
lysyl oxidase
annexin A2
S100A11
plasmin
cancer microenvironment
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Published Date | 2024-03-26
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Publication Title |
Frontiers in Oncology
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Volume | volume14
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Publisher | Frontiers Media
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Start Page | 1371342
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ISSN | 2234-943X
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Content Type |
Journal Article
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language |
English
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OAI-PMH Set |
岡山大学
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Copyright Holders | © 2024 Takahashi, Tomonobu, Kinoshita, Yamamoto, Murata, Komalasari, Chen, Jiang, Gohara, Ochi, Ruma, Sumardika, Zhou, Honjo, Sakaguchi, Yamauchi, Kuribayashi, Kondo, Inoue, Futami, Toyooka, Zamami and Sakaguchi.
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File Version | publisher
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PubMed ID | |
DOI | |
Web of Science KeyUT | |
Related Url | isVersionOf https://doi.org/10.3389/fonc.2024.1371342
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License | https://creativecommons.org/licenses/by/4.0/
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Citation | Takahashi T, Tomonobu N, Kinoshita R, Yamamoto K-i, Murata H, Komalasari NLGY, Chen Y, Jiang F, Gohara Y, Ochi T, Ruma IMW, Sumardika IW, Zhou J, Honjo T, Sakaguchi Y, Yamauchi A, Kuribayashi F, Kondo E, Inoue Y, Futami J, Toyooka S, Zamami Y and Sakaguchi M (2024) Lysyl oxidase-like 4 promotes the invasiveness of triple-negative breast cancer cells by orchestrating the invasive machinery formed by annexin A2 and S100A11 on the cell surface. Front. Oncol. 14:1371342. doi: 10.3389/fonc.2024.1371342
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Funder Name |
Japan Society for the Promotion of Science
Zhejiang Provincial Natural Science Foundation of China
National Natural Science Foundation of China
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助成番号 | 23H02748
23K06717
22K20793
23K14595
LQ21H160021
82103072
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