Evidence map›Paper›PMID 24737780›Full record

ArticleCancer medicine2014

Angiomodulin, a marker of cancer vasculature, is upregulated by vascular endothelial growth factor and increases vascular permeability as a ligand of integrin αvβ3.

Eriko Komiya, Hiroki Sato, Naoko Watanabe, Marii Ise, Shouichi Higashi, Yohei Miyagi, Kaoru Miyazaki

Open access · goldAbstract read
In one paragraph

Article in Cancer medicine, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

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  5. Structural insight into CD93 recognition by IGFBP7.Structure (London, England : 1993) · 2024
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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

7 authors at 3 institutions in 1 country.

Eriko KomiyaDepartment of Genome Science, Graduate School of Integrated Science and Nanobioscience, Yokohama City University, 641-12 Maioka-cho, Totsuka-ku, Yokohama, Kanagawa, 244-0813, Japan; Division of Cell Biology, Kihara Institute for Biological Research, Yokohama City University, 641-12 Maioka-cho, Totsuka-ku, Yokohama, Kanagawa, 244-0813, Japan.
Hiroki Sato
Naoko Watanabe
Marii Ise
Shouichi Higashi
Yohei Miyagi
Kaoru Miyazaki
Kihara Institute for Biological Research · JPYokohama City University · JPKanagawa Cancer Center

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Angiomodulin (AGM) is a member of insulin-like growth factor binding protein (IGFBP) superfamily and often called IGFBP-rP1 or IGFBP-7. AGM was originally identified as a tumor-derived cell adhesion factor, which was highly accumulated in blood vessels of human cancer tissues. AGM is also overexpressed in cancer-associated fibroblasts (CAFs) and activates fibroblasts. However, some studies have shown tumor-suppressing activity of AGM. To understand the roles of AGM in cancer progression, we here investigated the expression of AGM in benign and invasive breast cancers and its functions in cancer vasculature. Immunohistochemical analysis showed that AGM was highly expressed in cancer vasculature even in ductal carcinoma in situ (DCIS) as compared to normal vasculature, while its expression in CAFs was more prominent in invasive carcinomas than DCIS. In vitro analyses showed that AGM was strongly induced by vascular endothelial cell growth factor (VEGF) in vascular endothelial cells. Although AGM stimulated neither the growth nor migration of endothelial cells, it supported efficient adhesion of endothelial cells. Integrin αvβ3 was identified as a novel major receptor for AGM in vascular endothelial cells. AGM retracted endothelial cells by inducing actin stress fibers and loosened their VE-cadherin-mediated intercellular junction. Consequently, AGM increased vascular permeability both in vitro and in vivo. Furthermore, AGM and integrin αvβ3 were highly expressed and colocalized in cancer vasculature. These results suggest that AGM cooperates with VEGF to induce the aberrant functions of cancer vasculature as a ligand of integrin αvβ3.

Indexed as

Biomarkers, TumorBreast NeoplasmsCapillary PermeabilityCarcinoma, Intraductal, NoninfiltratingCell Adhesion MoleculesFemaleGene Expression Regulation, NeoplasticHumansHuman Umbilical Vein Endothelial CellsIntegrin alphaVbeta3LigandsNeoplasm ProteinsNeovascularization, PathologicVascular Endothelial Growth Factor ABiomarkers, TumorCell Adhesion Moleculescell aggregation factorsIntegrin alphaVbeta3LigandsNeoplasm Proteinstumor-derived adhesion factorVascular Endothelial Growth Factor AAngiomodulinIGFBPintegrin αvβ3tumor angiogenesisvascular permeability

Identifiers

PMID24737780
PMCPMC4101744
OpenAlexW2143388717

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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.