Evidence map›Paper›PMID 25686833›Full record

ArticleOncotarget2015

Vacuolar ATPase 'a2' isoform exhibits distinct cell surface accumulation and modulates matrix metalloproteinase activity in ovarian cancer.

Arpita Kulshrestha, Gajendra K Katara, Safaa Ibrahim, Sahithi Pamarthy, Mukesh K Jaiswal, Alice Gilman Sachs, Kenneth D Beaman

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.2field-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

38 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
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  7. Review
  8. The V-ATPases in cancer and cell death.Cancer gene therapy · 2022
    Review
  9. Article
  10. The V-ATPaseInternational journal of molecular sciences · 2021
    Review
  11. The Golgi as a "Proton Sink" in Cancer.Frontiers in cell and developmental biology · 2021
    Article
  12. Regulation and function of V-ATPases in physiology and disease.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
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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 2 institutions in 2 countries.

Arpita KulshresthaDepartment of Microbiology and Immunology, Rosalind Franklin University of Medicine and Science, North Chicago, IL, USA.
Gajendra K KataraDepartment of Microbiology and Immunology, Rosalind Franklin University of Medicine and Science, North Chicago, IL, USA.
Safaa IbrahimDepartment of Microbiology and Immunology, Rosalind Franklin University of Medicine and Science, North Chicago, IL, USA.
Sahithi PamarthyDepartment of Microbiology and Immunology, Rosalind Franklin University of Medicine and Science, North Chicago, IL, USA.
Mukesh K JaiswalDepartment of Microbiology and Immunology, Rosalind Franklin University of Medicine and Science, North Chicago, IL, USA.
Alice Gilman SachsDepartment of Microbiology and Immunology, Rosalind Franklin University of Medicine and Science, North Chicago, IL, USA.
Kenneth D BeamanDepartment of Microbiology and Immunology, Rosalind Franklin University of Medicine and Science, North Chicago, IL, USA.
Rosalind Franklin University of Medicine and Science · USCairo University · EG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tumor associated vacuolar H+-ATPases (V-ATPases) are multi-subunit proton pumps that acidify tumor microenvironment, thereby promoting tumor invasion. Subunit 'a' of its V0 domain is the major pH sensing unit that additionally controls sub-cellular targeting of V-ATPase and exists in four different isoforms. Our study reports an elevated expression of the V-ATPase-V0a2 isoform in ovarian cancer(OVCA) tissues and cell lines(A2780, SKOV-3 and TOV-112D). Among all V0'a' isoforms, V0a2 exhibited abundant expression on OVCA cell surface while normal ovarian epithelia did not. Sub-cellular distribution of V-ATPase-V0a2 confirmed its localization on plasma-membrane, where it was also co-associated with cortactin, an F-actin stabilizing protein at leading edges of cancer cells. Additionally, V0a2 was also localized in early and late endosomal compartments that are sites for modulations of several signaling pathways in cancer. Targeted inhibition of V-ATPase-V0a2 suppressed matrix metalloproteinase activity(MMP-9 & MMP-2) in OVCA cells. In conclusion, V-ATPase-V0a2 isoform is abundantly expressed on ovarian tumor cell surface in association with invasion assembly related proteins and plays critical role in tumor invasion by modulating the activity of matrix-degrading proteases. This study highlights for the first time, the importance of V-ATPase-V0a2 isoform as a distinct biomarker and possible therapeutic target for treatment of ovarian carcinoma.

Indexed as

Cell Line, TumorFemaleFlow CytometryHumansIsoenzymesMatrix MetalloproteinasesMicroscopy, ConfocalOvarian NeoplasmsTumor MicroenvironmentVacuolar Proton-Translocating ATPasesIsoenzymesMatrix MetalloproteinasesVacuolar Proton-Translocating ATPases

Identifiers

PMID25686833
PMCPMC4414154
OpenAlexW1865575659

What OpenQuestion holds

Textmetadata
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.