Evidence map›Paper›PMID 27323815›Full record

ArticleOncotarget2016

The a3 isoform of subunit a of the vacuolar ATPase localizes to the plasma membrane of invasive breast tumor cells and is overexpressed in human breast cancer.

Kristina Cotter, Rachel Liberman, GeHong Sun-Wada, Yoh Wada, Dennis Sgroi, Stephen Naber, Dennis Brown, Sylvie Breton, Michael Forgac

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

29 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  5. Eukaryotic yeast VFrontiers in molecular biosciences · 2024
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  11. Role of pH Regulatory Proteins and Dysregulation of pH in Prostate Cancer.Reviews of physiology, biochemistry and pharmacology · 2022
    Article
  12. Article
  13. The HAmerican journal of physiology. Cell physiology · 2021
    Review
  14. Article
  15. Regulation and function of V-ATPases in physiology and disease.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  16. Review
  17. Review
  18. Review
  19. 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

9 authors at 7 institutions in 2 countries.

Kristina CotterDepartment of Developmental, Molecular and Chemical Biology, Tufts University School of Medicine and The Program in Cellular and Molecular Physiology, Sackler School of Graduate Biomedical Sciences, Tufts University, Boston, Massachusetts 02111, USA.
Rachel LibermanProgram in Membrane Biology/Nephrology Division, Center for Systems Biology, Massachusetts General Hospital/Harvard Medical School, Boston, Massachusetts, 02114, USA.
GeHong Sun-WadaDepartment of Biochemistry, Faculty of Pharmaceutical Sciences, Doshisha Women's College, Kyotanabe, Kyoto 610-0395, Japan.
Yoh WadaDivision of Biological Science, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan.
Dennis SgroiDepartment of Pathology, Molecular Pathology Unit, Massachusetts General Hospital, Charlestown, Massachusetts 02129, USA.
Stephen NaberDepartment of Pathology, Tufts Medical Center, Boston, Massachusetts 02111, USA.
Dennis BrownProgram in Membrane Biology/Nephrology Division, Center for Systems Biology, Massachusetts General Hospital/Harvard Medical School, Boston, Massachusetts, 02114, USA.
Sylvie BretonProgram in Membrane Biology/Nephrology Division, Center for Systems Biology, Massachusetts General Hospital/Harvard Medical School, Boston, Massachusetts, 02114, USA.
Michael ForgacDepartment of Developmental, Molecular and Chemical Biology, Tufts University School of Medicine and The Program in Cellular and Molecular Physiology, Sackler School of Graduate Biomedical Sciences, Tufts University, Boston, Massachusetts 02111, USA.
Massachusetts General Hospital · USTufts University · USCenter for Systems Biology · USDoshisha Women's College of Liberal Arts · JPHarvard University · USOsaka University · JPTufts Medical Center · US

Funding

Transgenic CoreP30DK057521 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI HABENER, JOEL F · 2000 to 2019
$31.4M
Training Grant in Molecular Imaging Research (MGH/HMS)T32CA079443 · NCI · MASSACHUSETTS GENERAL HOSPITAL · PI WEISSLEDER, MD, PHD, RALPH · 2000 to 2025
$10.1M
Structure, Mechanism and Regulation of the V-ATPasesR37GM034478 · NIGMS · TUFTS UNIVERSITY BOSTON · PI FORGAC, MICHAEL D · 2001 to 2010
$5.0M
Regulation of proton pump trafficking in kidneyR37DK042956 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI BROWN, DENNIS · 2008 to 2017
$4.0M
STRUCTURE, MECHANISM AND REGULATION OF THE V-ATPASESR01GM034478 · NIGMS · TUFTS UNIVERSITY BOSTON · PI FORGAC, MICHAEL D · 1985 to 2015
$1.9M
pH-sensing and activation of acid secretion by the V-ATPaseR01DK097124 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI BRETON, SYLVIE · 2013 to 2016
$1.5M
Elucidating the Role of Plasma Membrane V-ATPases in Breast Cancer MetastasisF31CA192500 · NCI · TUFTS UNIVERSITY BOSTON · PI COTTER, KRISTINA · 2015 to 2015
$31k
NCI NIH HHS F31 CA192500NCI NIH HHS T32 CA079443NIDDK NIH HHS P30 DK057521NIDDK NIH HHS R01 DK097124NIDDK NIH HHS R37 DK042956NIGMS NIH HHS R01 GM034478NIGMS NIH HHS R37 GM034478
6 · The paper itself

Abstract

The vacuolar (H+)-ATPases (V-ATPases) are a family of ATP-driven proton pumps that acidify intracellular compartments and transport protons across the plasma membrane. Previous work has demonstrated that plasma membrane V-ATPases are important for breast cancer invasion in vitro and that the V-ATPase subunit a isoform a3 is upregulated in and critical for MDA-MB231 and MCF10CA1a breast cancer cell invasion. It has been proposed that subunit a3 is present on the plasma membrane of invasive breast cancer cells and is overexpressed in human breast cancer. To test this, we used an a3-specific antibody to assess localization in breast cancer cells. Subunit a3 localizes to the leading edge of migrating breast cancer cells, but not the plasma membrane of normal breast epithelial cells. Furthermore, invasive breast cancer cells express a3 throughout all intracellular compartments tested, including endosomes, the Golgi, and lysosomes. Moreover, subunit a3 knockdown in MB231 breast cancer cells reduces in vitro migration. This reduction is not enhanced upon addition of a V-ATPase inhibitor, suggesting that a3-containing V-ATPases are critical for breast cancer migration. Finally, we have tested a3 expression in human breast cancer tissue and mRNA prepared from normal and cancerous breast tissue. a3 mRNA was upregulated 2.5-47 fold in all breast tumor cDNA samples tested relative to normal tissue, with expression generally correlated to cancer stage. Furthermore, a3 protein expression was increased in invasive breast cancer tissue relative to noninvasive cancer and normal breast tissue. These studies suggest that subunit a3 plays an important role in invasive human breast cancer.

Indexed as

Breast NeoplasmsCell Line, TumorCell MembraneCell MovementFemaleHumansIsoenzymesVacuolar Proton-Translocating ATPasesIsoenzymesVacuolar Proton-Translocating ATPasesacidificationbreast cancerinvasionproton transportvacuolar ATPase

Identifiers

PMID27323815
PMCPMC5216787
OpenAlexW2437364606

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.