Development of fluorogenic substrates for colorectal tumor-related neuropeptidases for activity-based diagnosis

Norimichi Nagano; Yuki Ichihashi; Toru Komatsu; Hiroyuki Matsuzaki; Keisuke Hata; Toshiaki Watanabe; Yoshihiro Misawa; Misa Suzuki; Shingo Sakamoto; Yu Kagami; Ayumi Kashiro; Keiko Takeuchi; Yukihide Kanemitsu; Hiroki Ochiai; Rikiya Watanabe; Kazufumi Honda; Yasuteru Urano

doi:10.1039/d2sc07029d

Development of fluorogenic substrates for colorectal tumor-related neuropeptidases for activity-based diagnosis

Norimichi Nagano, Yuki Ichihashi, Toru Komatsu, Hiroyuki Matsuzaki, Keisuke Hata, Toshiaki Watanabe, Yoshihiro Misawa, Misa Suzuki, Shingo Sakamoto, Yu Kagami, Ayumi Kashiro, Keiko Takeuchi, Yukihide Kanemitsu, Hiroki Ochiai, Rikiya Watanabe, Kazufumi Honda, Yasuteru Urano

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

The M3 metalloproteases, neurolysin and THOP1, are neuropeptidases that are expressed in various tissues and metabolize neuropeptides, such as neurotensin. The biological roles of these enzymes are not well characterized, partially because the chemical tools to analyse their activities are not well developed. Here, we developed a fluorogenic substrate probe for neurolysin and thimet oligopeptidase 1 (THOP1), which enabled the analysis of enzymatic activity changes in tissue and plasma samples. In particular, the probe was useful for studying enzyme activities in a single-molecule enzyme assay platform, which can detect enzyme activity with high sensitivity. We detected the activity of neurolysin in plasma samples and revealed higher enzyme activity in the blood samples of patients with colorectal tumor. The result indicated that single-molecule neurolysin activity is a promising candidate for a blood biomarker for colorectal cancer diagnosis.

Original language	English
Pages (from-to)	4495-4499
Number of pages	5
Journal	Chemical Science
Volume	14
Issue number	17
DOIs	https://doi.org/10.1039/d2sc07029d
State	Published - 11 Apr 2023
Externally published	Yes

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10.1039/d2sc07029d

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Nagano, N., Ichihashi, Y., Komatsu, T., Matsuzaki, H., Hata, K., Watanabe, T., Misawa, Y., Suzuki, M., Sakamoto, S., Kagami, Y., Kashiro, A., Takeuchi, K., Kanemitsu, Y., Ochiai, H., Watanabe, R., Honda, K., & Urano, Y. (2023). Development of fluorogenic substrates for colorectal tumor-related neuropeptidases for activity-based diagnosis. Chemical Science, 14(17), 4495-4499. https://doi.org/10.1039/d2sc07029d

@article{094adf20babb4867a603738cc7c12746,

title = "Development of fluorogenic substrates for colorectal tumor-related neuropeptidases for activity-based diagnosis",

abstract = "The M3 metalloproteases, neurolysin and THOP1, are neuropeptidases that are expressed in various tissues and metabolize neuropeptides, such as neurotensin. The biological roles of these enzymes are not well characterized, partially because the chemical tools to analyse their activities are not well developed. Here, we developed a fluorogenic substrate probe for neurolysin and thimet oligopeptidase 1 (THOP1), which enabled the analysis of enzymatic activity changes in tissue and plasma samples. In particular, the probe was useful for studying enzyme activities in a single-molecule enzyme assay platform, which can detect enzyme activity with high sensitivity. We detected the activity of neurolysin in plasma samples and revealed higher enzyme activity in the blood samples of patients with colorectal tumor. The result indicated that single-molecule neurolysin activity is a promising candidate for a blood biomarker for colorectal cancer diagnosis.",

author = "Norimichi Nagano and Yuki Ichihashi and Toru Komatsu and Hiroyuki Matsuzaki and Keisuke Hata and Toshiaki Watanabe and Yoshihiro Misawa and Misa Suzuki and Shingo Sakamoto and Yu Kagami and Ayumi Kashiro and Keiko Takeuchi and Yukihide Kanemitsu and Hiroki Ochiai and Rikiya Watanabe and Kazufumi Honda and Yasuteru Urano",

note = "Publisher Copyright: {\textcopyright} 2023 The Royal Society of Chemistry.",

year = "2023",

month = apr,

day = "11",

doi = "10.1039/d2sc07029d",

language = "英語",

volume = "14",

pages = "4495--4499",

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publisher = "Royal Society of Chemistry",

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Nagano, N, Ichihashi, Y, Komatsu, T, Matsuzaki, H, Hata, K, Watanabe, T, Misawa, Y, Suzuki, M, Sakamoto, S, Kagami, Y, Kashiro, A, Takeuchi, K, Kanemitsu, Y, Ochiai, H, Watanabe, R, Honda, K & Urano, Y 2023, 'Development of fluorogenic substrates for colorectal tumor-related neuropeptidases for activity-based diagnosis', Chemical Science, vol. 14, no. 17, pp. 4495-4499. https://doi.org/10.1039/d2sc07029d

TY - JOUR

T1 - Development of fluorogenic substrates for colorectal tumor-related neuropeptidases for activity-based diagnosis

AU - Nagano, Norimichi

AU - Ichihashi, Yuki

AU - Komatsu, Toru

AU - Matsuzaki, Hiroyuki

AU - Hata, Keisuke

AU - Watanabe, Toshiaki

AU - Misawa, Yoshihiro

AU - Suzuki, Misa

AU - Sakamoto, Shingo

AU - Kagami, Yu

AU - Kashiro, Ayumi

AU - Takeuchi, Keiko

AU - Kanemitsu, Yukihide

AU - Ochiai, Hiroki

AU - Watanabe, Rikiya

AU - Honda, Kazufumi

AU - Urano, Yasuteru

PY - 2023/4/11

Y1 - 2023/4/11

N2 - The M3 metalloproteases, neurolysin and THOP1, are neuropeptidases that are expressed in various tissues and metabolize neuropeptides, such as neurotensin. The biological roles of these enzymes are not well characterized, partially because the chemical tools to analyse their activities are not well developed. Here, we developed a fluorogenic substrate probe for neurolysin and thimet oligopeptidase 1 (THOP1), which enabled the analysis of enzymatic activity changes in tissue and plasma samples. In particular, the probe was useful for studying enzyme activities in a single-molecule enzyme assay platform, which can detect enzyme activity with high sensitivity. We detected the activity of neurolysin in plasma samples and revealed higher enzyme activity in the blood samples of patients with colorectal tumor. The result indicated that single-molecule neurolysin activity is a promising candidate for a blood biomarker for colorectal cancer diagnosis.

AB - The M3 metalloproteases, neurolysin and THOP1, are neuropeptidases that are expressed in various tissues and metabolize neuropeptides, such as neurotensin. The biological roles of these enzymes are not well characterized, partially because the chemical tools to analyse their activities are not well developed. Here, we developed a fluorogenic substrate probe for neurolysin and thimet oligopeptidase 1 (THOP1), which enabled the analysis of enzymatic activity changes in tissue and plasma samples. In particular, the probe was useful for studying enzyme activities in a single-molecule enzyme assay platform, which can detect enzyme activity with high sensitivity. We detected the activity of neurolysin in plasma samples and revealed higher enzyme activity in the blood samples of patients with colorectal tumor. The result indicated that single-molecule neurolysin activity is a promising candidate for a blood biomarker for colorectal cancer diagnosis.

UR - https://www.scopus.com/pages/publications/85153288058

U2 - 10.1039/d2sc07029d

DO - 10.1039/d2sc07029d

M3 - 記事

AN - SCOPUS:85153288058

SN - 2041-6520

VL - 14

SP - 4495

EP - 4499

JO - Chemical Science

JF - Chemical Science

IS - 17

ER -

Development of fluorogenic substrates for colorectal tumor-related neuropeptidases for activity-based diagnosis

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