Evidence map›Paper›PMID 28416796›Full record

ArticleNature communications2017

Lysyl oxidase drives tumour progression by trapping EGF receptors at the cell surface.

HaoRan Tang, Leo Leung, Grazia Saturno, Amaya Viros, Duncan Smith, Gianpiero Di Leva, Eamonn Morrison, Dan Niculescu-Duvaz, Filipa Lopes, Louise Johnson and 3 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

49 citing papers in PubMed, 87 citations in OpenAlex.

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  10. Multi-stage mechanisms of tumor metastasis and therapeutic strategies.Signal transduction and targeted therapy · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 2 institutions in 1 country.

HaoRan TangMolecular Oncology Group, Cancer Research UK Manchester Institute, University of Manchester, Manchester M20 4BX, UK.
Leo LeungGene and Oncogene Targeting Team, CRUK Cancer Therapeutics Unit, The Institute of Cancer Research, London SM2 5NG, UK.
Grazia SaturnoMolecular Oncology Group, Cancer Research UK Manchester Institute, University of Manchester, Manchester M20 4BX, UK.
Amaya VirosMolecular Oncology Group, Cancer Research UK Manchester Institute, University of Manchester, Manchester M20 4BX, UK.
Duncan SmithBiological Mass Spectrometry Unit, Cancer Research UK Manchester Institute, University of Manchester, Manchester M20 4BX, UK.
Gianpiero Di LevaMolecular Oncology Group, Cancer Research UK Manchester Institute, University of Manchester, Manchester M20 4BX, UK.
Eamonn MorrisonMolecular Oncology Group, Cancer Research UK Manchester Institute, University of Manchester, Manchester M20 4BX, UK.
Dan Niculescu-DuvazGene and Oncogene Targeting Team, CRUK Cancer Therapeutics Unit, The Institute of Cancer Research, London SM2 5NG, UK.
Filipa LopesGene and Oncogene Targeting Team, CRUK Cancer Therapeutics Unit, The Institute of Cancer Research, London SM2 5NG, UK.
Louise JohnsonGene and Oncogene Targeting Team, CRUK Cancer Therapeutics Unit, The Institute of Cancer Research, London SM2 5NG, UK.
Nathalie DhomenMolecular Oncology Group, Cancer Research UK Manchester Institute, University of Manchester, Manchester M20 4BX, UK.
Caroline SpringerGene and Oncogene Targeting Team, CRUK Cancer Therapeutics Unit, The Institute of Cancer Research, London SM2 5NG, UK.
Richard MaraisMolecular Oncology Group, Cancer Research UK Manchester Institute, University of Manchester, Manchester M20 4BX, UK.ORCID 0000-0001-7484-4183
University of Manchester · GBInstitute of Cancer Research · GB

Funding

Cancer Research UK 22902Wellcome Trust 110078/Z/15/Z
6 · The paper itself

Abstract

Lysyl oxidase (LOX) remodels the tumour microenvironment by cross-linking the extracellular matrix. LOX overexpression is associated with poor cancer outcomes. Here, we find that LOX regulates the epidermal growth factor receptor (EGFR) to drive tumour progression. We show that LOX regulates EGFR by suppressing TGFβ1 signalling through the secreted protease HTRA1. This increases the expression of Matrilin2 (MATN2), an EGF-like domain-containing protein that traps EGFR at the cell surface to facilitate its activation by EGF. We describe a pharmacological inhibitor of LOX, CCT365623, which disrupts EGFR cell surface retention and delays the growth of primary and metastatic tumour cells in vivo. Thus, we show that LOX regulates EGFR cell surface retention to drive tumour progression, and we validate the therapeutic potential of inhibiting this pathway with the small molecule inhibitor CCT365623.

Indexed as

Disease ProgressionAminopropionitrileAnimalsBiosensing TechniquesCell Line, TumorCell MembraneCell ProliferationDogsEnzyme ActivationEnzyme InhibitorsEpidermal Growth FactorErbB ReceptorsHigh-Temperature Requirement A Serine Peptidase 1HumansMatrilin ProteinsMiceAminopropionitrileEnzyme InhibitorsEpidermal Growth FactorErbB ReceptorsHigh-Temperature Requirement A Serine Peptidase 1HTRA1 protein, humanMATN2 protein, humanMatrilin ProteinsProtein-Lysine 6-OxidaseTransforming Growth Factor beta1

Identifiers

PMID28416796
PMCPMC5399287
OpenAlexW2604541426

What OpenQuestion holds

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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.