| アイテムタイプ |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2026-01-21 |
| タイトル |
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|
タイトル |
Dipeptidyl peptidase from Streptococcus anginosus with substrate specificity for Xaa-Pro/Ala and potential impact on tumor immunity |
|
言語 |
en |
| 言語 |
|
|
言語 |
eng |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
Chemokine cleavage |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
Dipeptidyl peptidase |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
Oral squamous cell carcinoma |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
Streptococcus anginosus |
| 資源タイプ |
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|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
journal article |
| 著者 |
Suzuki, Shu
Miura, Toshitaka
Shimoyama, Yu
Ohara-Nemoto, Yuko
Nemoto, Takayuki K.
Yamada, Hiroyuki
Ishikawa, Taichi
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| 抄録 |
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内容記述タイプ |
Abstract |
|
内容記述 |
Objectives: Streptococcus anginosus, an oral commensal bacterium, is a potential risk factor for malignancies of the oral cavity and upper gastrointestinal tract. Although this species harbors an Xaa-Pro dipeptidyl peptidase (DPP), its enzymatic characteristics and potential role in tumor-associated immune modulation remain unclear. In this study, S. anginosus Xaa-Pro DPP was characterized and its ability to cleave chemokine-related peptides was evaluated. Methods: Six oral streptococcal strains were analyzed for DPP activity using fluorogenic dipeptidyl substrates. The gene encoding S. anginosus Xaa-Pro DPP was cloned and the recombinant enzyme was purified and characterized. The enzymatic activity of the peptidase against synthetic dipeptidyl 7-amino-4-methylcoumarin (MCA) and chemokine-derived peptides was assessed using fluorescence assays and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The effect of the DPP4 inhibitor, P32/98, was also examined. Results: S. anginosus had the highest DPP activity among the tested oral streptococci, particularly towards Gly-Pro- and Lys-Ala-MCA. The recombinant enzyme selectively removed Xaa-Pro and Xaa-Ala dipeptides and the N-terminal Lys-Pro dipeptide from the CXCL12-derived peptide, whereas incretins were minimally affected. The enzymatic activity of Xaa-Pro DPP against synthetic substrates was markedly inhibited by P32/98. Conclusion: S. anginosus Xaa-Pro DPP has specificity for N-terminal Xaa-Pro/Ala in peptides and exhibits the ability to inactivate chemokine-related peptides, suggesting a potential contribution to immune dysregulation in the tumor microenvironment. |
|
言語 |
en |
| 書誌情報 |
en : Journal of Oral Biosciences
巻 68,
号 1,
p. art. no. 100723,
発行日 2025-12-11
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| 出版者 |
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出版者 |
Elsevier B.V. |
|
言語 |
en |
| ISSN |
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|
収録物識別子タイプ |
ISSN |
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収録物識別子 |
13490079 |
| DOI |
|
|
関連タイプ |
isVersionOf |
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|
識別子タイプ |
DOI |
|
|
関連識別子 |
https://doi.org/10.1016/j.job.2025.100723 |
| 権利 |
|
|
権利情報 |
© 2025 Japanese Association for Oral Biology. Published by Elsevier B.V. This manuscript version is made available under the CC-BY-NC-ND 4.0 license https://creativecommons.org/licenses/by-nc-nd/4.0/. |
|
言語 |
en |
| 著者版フラグ |
|
|
出版タイプ |
AM |
|
出版タイプResource |
http://purl.org/coar/version/c_ab4af688f83e57aa |
| 引用 |
|
|
内容記述タイプ |
Other |
|
内容記述 |
Journal of Oral Biosciences, 68(1), art. no. 100723; 2025 |
|
言語 |
en |
JOB68_100723.pdf (1.2 MB)
