Evidence map›Paper›PMID 26912656›Full record

ArticleThe Journal of biological chemistry2016

Extracellular and Luminal pH Regulation by Vacuolar H+-ATPase Isoform Expression and Targeting to the Plasma Membrane and Endosomes.

Gina A Smith, Gareth J Howell, Clair Phillips, Stephen P Muench, Sreenivasan Ponnambalam, Michael A Harrison

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  9. Review
  10. pH regulates the lumen diameter of tissue-engineered capillaries.Experimental and therapeutic medicine · 2022
    Article
  11. Role of pH Regulatory Proteins and Dysregulation of pH in Prostate Cancer.Reviews of physiology, biochemistry and pharmacology · 2022
    Article
  12. Article
  13. Article
  14. Regulation and function of V-ATPases in physiology and disease.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  15. Review
  16. The Vacuolar HCells · 2020
    Article
  17. Article
  18. Review
  19. Article
  20. Article
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

6 authors at 1 institution in 1 country.

Gina A SmithFrom the Endothelial Cell Biology Unit, School of Molecular and Cellular Biology and.
Gareth J HowellFrom the Endothelial Cell Biology Unit, School of Molecular and Cellular Biology and.
Clair PhillipsSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom.
Stephen P MuenchSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom.
Sreenivasan PonnambalamFrom the Endothelial Cell Biology Unit, School of Molecular and Cellular Biology and.
Michael A HarrisonSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom m.a.harrison@leeds.ac.uk.
University of Leeds · GB

Funding

British Heart Foundation FS/12/20/29462Medical Research Council G1000567
6 · The paper itself

Abstract

Plasma membrane vacuolar H(+)-ATPase (V-ATPase) activity of tumor cells is a major factor in control of cytoplasmic and extracellular pH and metastatic potential, but the isoforms involved and the factors governing plasma membrane recruitment remain uncertain. Here, we examined expression, distribution, and activity of V-ATPase isoforms in invasive prostate adenocarcinoma (PC-3) cells. Isoforms 1 and 3 were the most highly expressed forms of membrane subunit a, with a1 and a3 the dominant plasma membrane isoforms. Correlation between plasma membrane V-ATPase activity and invasiveness was limited, but RNAi knockdown of either a isoform did slow cell proliferation and inhibit invasion in vitro Isoform a1 was recruited to the cell surface from the early endosome-recycling complex pathway, its knockdown arresting transferrin receptor recycling. Isoform a3 was associated with the late endosomal/lysosomal compartment. Both a isoforms associated with accessory protein Ac45, knockdown of which stalled transit of a1 and transferrin-transferrin receptor, decreased proton efflux, and reduced cell growth and invasiveness; this latter effect was at least partly due to decreased delivery of the membrane-bound matrix metalloproteinase MMP-14 to the plasma membrane. These data indicate that in prostatic carcinoma cells, a1 and a3 isoform populations predominate in different compartments where they maintain different luminal pH. Ac45 plays a central role in navigating the V-ATPase to the plasma membrane, and hence it is an important factor in expression of the invasive phenotype.

Indexed as

Cell Line, TumorCell MembraneEndosomesHumansHydrogen-Ion ConcentrationIsoenzymesMatrix Metalloproteinase 14Vacuolar Proton-Translocating ATPasesATP6AP1 protein, humanIsoenzymesMatrix Metalloproteinase 14MMP14 protein, humanVacuolar Proton-Translocating ATPasesendocytosismembrane traffickingreceptor internalizationreceptor recyclingvacuolar ATPase

Identifiers

PMID26912656
PMCPMC4861423
OpenAlexW2280443309

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.