Evidence map›Paper›PMID 36721170›Full record

ArticleMolecular cancer2023

Lysyl hydroxylase LH1 promotes confined migration and metastasis of cancer cells by stabilizing Septin2 to enhance actin network.

Zihan Yang, Li Zhou, Tongxu Si, Siyuan Chen, Chengxi Liu, Kelvin Kaki Ng, Zesheng Wang, Zhiji Chen, Chan Qiu, Guopan Liu and 7 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular cancer, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
5.5field-weighted citation impact, top 4% of its field
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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

21 citing papers in PubMed, 23 citations in OpenAlex.

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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

17 authors at 5 institutions in 2 countries.

Zihan YangDepartment of Biomedical Sciences, and Tung Biomedical Sciences Center, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, People's Republic of China.
Li ZhouDepartment of Biomedical Sciences, and Tung Biomedical Sciences Center, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, People's Republic of China.
Tongxu SiDepartment of Biomedical Sciences, and Tung Biomedical Sciences Center, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, People's Republic of China.
Siyuan ChenDepartment of Gastroenterology, the Second Affiliated Hospital of Chongqing Medical University, Chongqing, China.
Chengxi LiuState Key Laboratory of Chemical Biology and Drug Discovery, Research Institute for Future Food and Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong SAR, China.
Kelvin Kaki NgDepartment of Biomedical Sciences, and Tung Biomedical Sciences Center, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, People's Republic of China.
Zesheng WangDepartment of Biomedical Sciences, and Tung Biomedical Sciences Center, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, People's Republic of China.
Zhiji ChenDepartment of Gastroenterology, the Second Affiliated Hospital of Chongqing Medical University, Chongqing, China.
Chan QiuDepartment of Gastroenterology, the Second Affiliated Hospital of Chongqing Medical University, Chongqing, China.
Guopan LiuDepartment of Biomedical Sciences, and Tung Biomedical Sciences Center, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, People's Republic of China.
Qingliang WangDepartment of Pathology, the Second Affiliated Hospital of Chongqing Medical University, Chongqing, China.
Xiaoyu ZhouDepartment of Biomedical Sciences, and Tung Biomedical Sciences Center, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, People's Republic of China.
Liang ZhangDepartment of Biomedical Sciences, and Tung Biomedical Sciences Center, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, People's Republic of China.
Zhongping YaoState Key Laboratory of Chemical Biology and Drug Discovery, Research Institute for Future Food and Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong SAR, China.
Song HeDepartment of Gastroenterology, the Second Affiliated Hospital of Chongqing Medical University, Chongqing, China.
Mengsu YangDepartment of Biomedical Sciences, and Tung Biomedical Sciences Center, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, People's Republic of China. bhmyang@cityu.edu.hk.
Zhihang ZhouDepartment of Biomedical Sciences, and Tung Biomedical Sciences Center, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, People's Republic of China. zhouzhihang@cqmu.edu.cn.
City University of Hong Kong, Shenzhen Research Institute · CNDalian Medical University · CNChongqing Medical University · CNHong Kong Polytechnic University · HKSecond Affiliated Hospital of Chongqing Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundExcessive extracellular matrix deposition and increased stiffness are typical features of solid tumors such as hepatocellular carcinoma (HCC) and pancreatic ductal adenocarcinoma (PDAC). These conditions create confined spaces for tumor cell migration and metastasis. The regulatory mechanism of confined migration remains unclear.

methodsLC-MS was applied to determine the differentially expressed proteins between HCC tissues and corresponding adjacent tissue. Collective migration and single cell migration microfluidic devices with 6 μm-high confined channels were designed and fabricated to mimic the in vivo confined space. 3D invasion assay was created by Matrigel and Collagen I mixture treat to adherent cells. 3D spheroid formation under various stiffness environment was developed by different substitution percentage GelMA. Immunoprecipitation was performed to pull down the LH1-binding proteins, which were identified by LC-MS. Immunofluorescent staining, FRET, RT-PCR, Western blotting, FRAP, CCK-8, transwell cell migration, wound healing, orthotopic liver injection mouse model and in vivo imaging were used to evaluate the target expression and cellular phenotype.

resultsLysyl hydroxylase 1 (LH1) promoted the confined migration of cancer cells at both collective and single cell levels. In addition, LH1 enhanced cell invasion in a 3D biomimetic model and spheroid formation in stiffer environments. High LH1 expression correlated with poor prognosis of both HCC and PDAC patients, while it also promoted in vivo metastasis. Mechanistically, LH1 bound and stabilized Septin2 (SEPT2) to enhance actin polymerization, depending on the hydroxylase domain. Finally, the subpopulation with high expression of both LH1 and SEPT2 had the poorest prognosis.

conclusionsLH1 promotes the confined migration and metastasis of cancer cells by stabilizing SEPT2 and thus facilitating actin polymerization.

Indexed as

Carcinoma, HepatocellularCarcinoma, Pancreatic DuctalLiver NeoplasmsPancreatic NeoplasmsActinsAnimalsMiceProcollagen-Lysine, 2-Oxoglutarate 5-DioxygenaseSeptinsActinsProcollagen-Lysine, 2-Oxoglutarate 5-DioxygenaseSeptinsCancer metastasisConfined migrationLysyl Hydroxylase 1Microfluidic chipSeptin2

Identifiers

PMID36721170
PMCPMC9887875
OpenAlexW4318707236

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.