Evidence map›Paper›PMID 39368988›Full record

ArticleScientific reports2024

Cysteine protease I29 propeptide from Calotropis procera R. Br. As a potent cathepsin L inhibitor and its suppressive activity in breast cancer metastasis.

Yong-Jin Kwon, Juno Lee, Eun-Bi Seo, Juchan Lee, Jaehyeon Park, Seul-Ki Kim, Hyunjong Yu, Sang-Kyu Ye, Pahn-Shick Chang

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In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Yong-Jin Kwon *Department of Pharmacology and Biomedical Sciences, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea.
Juno Lee *Center for Agricultural Microorganism and Enzyme, Seoul National University, Seoul, 08826, Republic of Korea.
Eun-Bi SeoDepartment of Pharmacology and Biomedical Sciences, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea.
Juchan LeeDepartment of Agricultural Biotechnology, Seoul National University College of Agricultural and Life Sciences, Seoul, 08826, Republic of Korea.
Jaehyeon ParkDepartment of Agricultural Biotechnology, Seoul National University College of Agricultural and Life Sciences, Seoul, 08826, Republic of Korea.
Seul-Ki KimDepartment of Pharmacology and Biomedical Sciences, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea.
Hyunjong YuMajor of Food Science and Biotechnology, Division of Bio-Convergence, Kyonggi University, Suwon, 16227, Republic of Korea.
Sang-Kyu YeDepartment of Pharmacology and Biomedical Sciences, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea. sangkyu@snu.ac.kr.
Pahn-Shick ChangCenter for Agricultural Microorganism and Enzyme, Seoul National University, Seoul, 08826, Republic of Korea. pschang@snu.ac.kr.

Funding

National Research Foundation of Korea NRF-2022R1A2C1011914Rural Development Administration, Republic of Korea RS-2021-RD009467
6 · The paper itself

Abstract

Breast cancer metastasis is associated with a poor prognosis and a high rate of mortality. Cathepsin L (CTSL) is a lysosomal cysteine protease that promotes tumor metastasis by degrading the extracellular matrix. Gene set enrichment analysis revealed that CTSL expression was higher in tumorous than in non-tumorous tissues of breast cancer patients and that high-level CTSL expression correlated positively with the epithelial-mesenchymal transition. Therefore, we hypothesized that inhibiting CTSL activity in tumor cells would prevent metastasis. In this study, we characterized the inhibitory activity of SnuCalCpI15, the I29 domain of a CTSL-like cysteine protease from Calotropis procera R. Br., and revealed that the propeptide stereoselectively inhibited CTSL in a reversible slow-binding manner, with an inhibitory constant (K

Indexed as

Breast NeoplasmsCalotropisCathepsin LCell MovementNeoplasm MetastasisCell Line, TumorCysteine Proteinase InhibitorsEpithelial-Mesenchymal TransitionFemaleHumansCathepsin LCTSL protein, humanCysteine Proteinase InhibitorsAnti-cancer therapyBreast cancerCathepsin LHigh-molecular-weight protein inhibitorI29 domain

Identifiers

PMID39368988
PMCPMC11457494

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.