Evidence map›Paper›PMID 23894455›Full record

ArticlePloS one2013

Surface α-enolase promotes extracellular matrix degradation and tumor metastasis and represents a new therapeutic target.

Kuan-Chung Hsiao, Neng-Yao Shih, Hsun-Lang Fang, Tze-Sing Huang, Ching-Chuan Kuo, Pei-Yi Chu, Yi-Mei Hung, Shao-Wen Chou, Yi-Yuan Yang, Gee-Chen Chang and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

84 citing papers in PubMed, 122 citations in OpenAlex.

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  11. The regulatory roles and clinical significance of glycolysis in tumor.Cancer communications (London, England) · 2024
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  14. BeyondMolecular therapy oncolytics · 2023
    Review
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24 more citing papers are in PubMed but not listed here.

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

11 authors at 6 institutions in 1 country.

Kuan-Chung HsiaoInstitute of Clinical Pharmacy and Pharmaceutical Sciences, National Cheng Kung University, Tainan, Taiwan.
Neng-Yao Shih
Hsun-Lang Fang
Tze-Sing Huang
Ching-Chuan Kuo
Pei-Yi Chu
Yi-Mei Hung
Shao-Wen Chou
Yi-Yuan Yang
Gee-Chen Chang
Ko-Jiunn Liu
National Health Research Institutes · TWNational Cheng Kung University · TWTaipei Medical University · TWMin-Hwei College of Health Care Management · TWNational Chung Hsing University · TWSt. Martin de Porres Hospital · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In previous research, we found α-enolase to be inversely correlated with progression-free and overall survival in lung cancer patients and detected α-enolase on the surface of lung cancer cells. Based on these findings, we hypothesized that surface α-enolase has a significant role in cancer metastasis and tested this hypothesis in the current study. We found that α-enolase was co-immunoprecipitated with urokinase-type plasminogen activator, urokinase-type plasminogen activator receptor, and plasminogen in lung cancer cells and interacted with these proteins in a cell-free dot blotting assay, which can be interrupted by α-enolase-specific antibody. α-Enolase in lung cancer cells co-localized with these proteins and was present at the site of pericellular degradation of extracellular matrix components. Treatment with antibody against α-enolase in vitro suppressed cell-associated plasminogen and matrix metalloproteinase activation, collagen and gelatin degradation, and cell invasion. Examination of the effect of treatment with shRNA plasmids revealed that down regulation of α-enolase decreases extracellular matrix degradation by and the invasion capacity of lung cancer cells. Adoptive transfer of α-enolase-specific antibody to mice resulted in accumulation of antibody in subcutaneous tumor and inhibited the formation of tumor metastasis in lung and bone. This study demonstrated that surface α-enolase promotes extracellular matrix degradation and invasion of cancer cells and that targeting surface α-enolase is a promising approach to suppress tumor metastasis.

Indexed as

AnimalsAntibodies, MonoclonalBiomarkers, TumorBone NeoplasmsCell Line, TumorCell MembraneCell MovementDNA-Binding ProteinsExtracellular MatrixHumansImmunocompromised HostLung NeoplasmsMaleMiceNeoplasm MetastasisNeoplasmsAntibodies, MonoclonalBiomarkers, TumorDNA-Binding ProteinsENO1 protein, humanPhosphopyruvate HydratasePlasminogenReceptors, Urokinase Plasminogen ActivatorTumor Suppressor ProteinsUrokinase-Type Plasminogen Activator

Identifiers

PMID23894455
PMCPMC3716638
OpenAlexW2051675224

What OpenQuestion holds

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LicenceCC BY
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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.