Evidence map›Paper›PMID 21454639›Full record

ArticleThe Journal of biological chemistry2011

Catalysis and pH control by membrane-associated carbonic anhydrase IX in MDA-MB-231 breast cancer cells.

Ying Li, Chingkuang Tu, Hai Wang, David N Silverman, Susan C Frost

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. 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
1.3field-weighted citation impact, top 21% 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, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Novel Thiopyrano[2,3-ACS omega · 2023
    Article
  5. Article
  6. Pharmaceuticals (Basel, Switzerland) · 2022
    Article
  7. Article
  8. Review
  9. Proton Transport in Cancer Cells: The Role of Carbonic Anhydrases.International journal of molecular sciences · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Biophysical Characterization of Cancer-Related Carbonic Anhydrase IX.International journal of molecular sciences · 2020
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Ying LiDepartment of Biochemistry and Molecular Biology, University of Florida, Gainesville, Florida 32610, USA.
Chingkuang Tu
Hai Wang
David N Silverman
Susan C Frost
University of Florida · US

Funding

ADAPTIVE REGULATION IN 3T3-L1 ADIPOCYTESR01DK045035 · NIDDK · UNIVERSITY OF FLORIDA · PI FROST, SUSAN COOKE · 1992 to 2007
$1.2M
SEQUENCE ANALYSIS OF BIOLOGICALLY ALTERED TRNAR01GM025254 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI DUDOCK, BERNARD S · 1985 to 1987
–
NIDDK NIH HHS DK45035NIDDK NIH HHS R01 DK045035NIGMS NIH HHS GM25254
6 · The paper itself

Abstract

Carbonic anhydrase IX (CAIX) is a membrane-bound, tumor-related enzyme whose expression is often considered a marker for hypoxia, an indicator of poor prognosis in the majority of cancer patients, and is associated with acidification of the tumor microenvironment. Here, we describe for the first time the catalytic properties of native CAIX in MDA-MB-231 breast cancer cells that exhibit hypoxia-inducible CAIX expression. Using (18)O exchange measured by membrane inlet mass spectrometry, we determined catalytic activity in membrane ghosts and intact cells. Exofacial carbonic anhydrase activity increases with exposure to hypoxia, an activity which is suppressed by impermeant sulfonamide CA inhibitors. Inhibition by sulfonamide inhibitors is not sensitive to reoxygenation. CAIX activity in intact cells increases in response to reduced pH. Data from membrane ghosts show that the increase in activity at reduced pH is largely due to an increase in the dehydration reaction. In addition, the kinetic constants of CAIX in membrane ghosts are very similar to our previous measurements for purified, recombinant, truncated forms. Hence, the activity of CAIX is not affected by the proteoglycan extension or membrane environment. These activities were measured at a total concentration for all CO(2) species at 25 mm and close to chemical equilibrium, conditions which approximate the physiological extracellular environment. Our data suggest that CAIX is particularly well suited to maintain the extracellular pH at a value that favors the survival fitness of tumor cells.

Indexed as

Antigens, NeoplasmBreast NeoplasmsCarbon DioxideCarbonic Anhydrase IXCarbonic AnhydrasesCatalysisCell Line, TumorCell MembraneCell SurvivalEnzyme InhibitorsFemaleHumansHydrogen-Ion ConcentrationNeoplasm ProteinsOxygenAntigens, NeoplasmCA9 protein, humanCarbon DioxideCarbonic Anhydrase IXCarbonic AnhydrasesEnzyme InhibitorsNeoplasm ProteinsOxygen

Identifiers

PMID21454639
PMCPMC3091188
OpenAlexW1969538906

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.