Evidence map›Paper›PMID 1385872›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1992

Sensitivity to vanadate and isoforms of subunits A and B distinguish the osteoclast proton pump from other vacuolar H+ ATPases.

D Chatterjee, M Chakraborty, M Leit, L Neff, S Jamsa-Kellokumpu, R Fuchs, R Baron

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

28 citing papers in PubMed, 152 citations in OpenAlex.

  1. HMedical molecular morphology · 2018
    Article
  2. Article
  3. Osteoclasts: New Insights.Bone research · 2013
    Review
  4. Article
  5. Article
  6. Article
  7. Proton pump inhibitors and gastritis.Journal of clinical biochemistry and nutrition · 2008
    Article
  8. Article
  9. Article
  10. Article
  11. Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  12. Novel treatments for osteoporosis.The Journal of clinical investigation · 2000
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Molecular aspects of osteoclast function.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 1996
    Review
  18. Article
  19. Article
  20. Alternative splicing generates a second isoform of the catalytic A subunit of the vacuolar H(+)-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 1995
    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

7 authors at 2 institutions in 2 countries.

D ChatterjeeDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.
M Chakraborty
M Leit
L Neff
S Jamsa-Kellokumpu
R Fuchs
R Baron
Yale University · USUniversity of Vienna · AT

Funding

Regulation of Osteoclastic Bone Resorption:Role of Cb1bR01DE004724 · NIDCR · YALE UNIVERSITY · PI BARON, ROLAND E · 1985 to 2008
$2.0M
REGULATION OF OSTEOCLASTIC BONE RESORPTIONR37DE004724 · NIDCR · YALE UNIVERSITY · PI BARON, ROLAND E · 1993 to 2002
$998k
OSTEOCLAST SPECIFIC PROTON PUMPR01AR041339 · NIAMS · YALE UNIVERSITY · PI BARON, ROLAND E · 1991 to 1997
–
NIAMS NIH HHS AR-41339NIDCR NIH HHS DE-04724
6 · The paper itself

Abstract

Analysis of proton (H+) transport by inside-out vesicles derived from highly purified chicken osteoclast (OC) membranes has revealed the presence of a newly discovered type of vacuolar H+ ATPase (V-ATPase). Unlike vesicles derived from any other cell type or organelle, H+ transport in OC-derived vesicles is sensitive to V-ATPase inhibitors (N-ethylmaleimide and Bafilomycin A1) and vanadate (IC50, 100 microM), an inhibitor previously found to affect only P-type ATPases. The OC H+ ATPase contains several V-like subunits (115, 39, and 16 kDa) but subunits A and B of the catalytic domain of the enzyme differ from that of other V-ATPases. In OCs, subunit A has a mass of 63 kDa instead of the 67-70 kDa expressed in monocytes, macrophages, and kidney microsomes, which contain a vanadate-insensitive H+ ATPase. Moreover, two types of 57- to 60-kDa B subunits are also found: one is expressed predominantly in OCs and the other is expressed in kidney microsomes. The OC H+ pump may therefore constitute a class of H+ ATPase with a unique pharmacology and specific isoforms of two subunits in the catalytic portion of the enzyme. This H+ ATPase is involved in resorption of bone and may be expressed in a cell-specific manner, thereby opening possibilities for therapeutic intervention.

Indexed as

AnimalsBiological Transport, ActiveChickensChromaffin GranulesEthylmaleimideFemaleIsoenzymesMolecular WeightOsteoclastsProton-Translocating ATPasesVacuolesVanadatesEthylmaleimideIsoenzymesProton-Translocating ATPasesVanadates

Identifiers

PMID1385872
PMCPMC49479
OpenAlexW1996855641

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.