Evidence map›Paper›PMID 23584482›Full record

ArticleOncogene2014

PDLIM2 expression is driven by vitamin D and is involved in the pro-adhesion, and anti-migration and -invasion activity of vitamin D.

E Vanoirbeek, G Eelen, L Verlinden, G Carmeliet, C Mathieu, R Bouillon, R O'Connor, G Xiao, A Verstuyf

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. PDLIM2 in Lung Adenocarcinoma Metastasis.bioRxiv : the preprint server for biology · 2025
    Article
  6. PDLIM2 Repression: A Common Mechanism in Viral Lung Infection.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. PDLIM2: Signaling pathways and functions in cancer suppression and host immunity.Biochimica et biophysica acta. Reviews on cancer · 2021
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Vitamin DCurrent nutrition reports · 2019
    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 at 3 institutions in 3 countries.

E VanoirbeekLaboratory of Clinical and Experimental Endocrinology, KU Leuven, Leuven, Belgium.
G Eelen1] Laboratory of Clinical and Experimental Endocrinology, KU Leuven, Leuven, Belgium [2] Laboratory of Angiogenesis & Neurovascular link, Vesalius Research Center, VIB/KU Leuven, Leuven, Belgium.
L VerlindenLaboratory of Clinical and Experimental Endocrinology, KU Leuven, Leuven, Belgium.
G CarmelietLaboratory of Clinical and Experimental Endocrinology, KU Leuven, Leuven, Belgium.
C MathieuLaboratory of Clinical and Experimental Endocrinology, KU Leuven, Leuven, Belgium.
R BouillonLaboratory of Clinical and Experimental Endocrinology, KU Leuven, Leuven, Belgium.
R O'ConnorDepartment of Biochemistry, University College, Cork, Ireland.
G XiaoHillman Cancer Center Research Pavilion, University of Pittsburgh, Pittsburgh, PA, USA.
A VerstuyfLaboratory of Clinical and Experimental Endocrinology, KU Leuven, Leuven, Belgium.
KU Leuven · BEUniversity College Cork · IEUPMC Hillman Cancer Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1Alpha,25-dihydroxyvitamin D3 [1,25(OH)2D3], the biologically active form of vitamin D3, is a pleiotropic hormone that exerts its effects on a wide range of tissues, resulting in different biological responses such as anticancer activity. It is the ligand of the vitamin D receptor (VDR), a nuclear receptor with transactivating capacity. We demonstrated in this study that 1,25(OH)2D3 induces PDZ-LIM domain-containing protein 2 (PDLIM2) expression. PDLIM2 is an adaptor molecule that links different components of the cytoskeleton, and was recently shown to be repressed in human breast cancer cells by hypermethylation of regulatory promoter regions, leading to enhanced tumorigenicity. We demonstrated that PDLIM2 was a direct target gene of 1,25(OH)2D3; its upregulation was VDR-dependent and a functional VDRE in the promoter was identified. Moreover, 1,25(OH)2D3 induced demethylation of the PDLIM2 promoter, leading to enhanced transcription. Finally, PDLIM2 was found to be crucial for 1,25(OH)2D3-induced cell adhesion and for mediating the ability of 1,25(OH)2D3 to suppress cancer cell migration and invasion. This study provides mechanistic insights into the anticancer activities of 1,25(OH)2D3 in human breast cancer cells.

Indexed as

Cell MovementAntineoplastic AgentsBlotting, WesternCell AdhesionChromatin ImmunoprecipitationGene Expression Regulation, NeoplasticHumansLIM Domain ProteinsMCF-7 CellsMicrofilament ProteinsNeoplasm InvasivenessPromoter Regions, GeneticReal-Time Polymerase Chain ReactionReceptors, CalcitriolTranscriptional ActivationVitamin DAntineoplastic Agentsdihydroxy-vitamin D3LIM Domain ProteinsMicrofilament ProteinsPDLIM2 protein, humanReceptors, CalcitriolVitamin D

Identifiers

PMID23584482
OpenAlexW2056992148

What OpenQuestion holds

Textmetadata
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.