Evidence map›Paper›PMID 17595168›Full record

ArticleThe Journal of biological chemistry2007

The plasma membrane Ca2+ pump isoform 4a differs from isoform 4b in the mechanism of calmodulin binding and activation kinetics: implications for Ca2+ signaling.

Ariel J Caride, Adelaida G Filoteo, John T Penniston, Emanuel E Strehler

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

22 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Identification ofInternational journal of molecular sciences · 2022
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Plasma membrane calcium ATPases as novel candidates for therapeutic agent development.Journal of pharmacy & pharmaceutical sciences : a publication of the Canadian Society for Pharmaceutical Sciences, Societe canadienne des sciences pharmaceutiques · 2013
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Emanuel Strehler's work on calcium pumps and calcium signaling.World journal of biological chemistry · 2011
    Article
  16. Article
  17. Review
  18. Article
  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

4 authors at 2 institutions in 1 country.

Ariel J CarideDepartment of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, Minnesota 55905, and Massachusetts General Hospital, Boston 02114, USA.
Adelaida G Filoteo
John T Penniston
Emanuel E Strehler
Mayo Clinic · USMassachusetts General Hospital · US

Funding

PURIFICATION AND PROPERTIES OF CA2+ PUMPING ATPASER01GM028835 · NIGMS · MAYO CLINIC ROCHESTER · PI STREHLER, EMANUEL ERNST · 1986 to 2006
$1.8M
Membrane Targeting of Calcium-Pumping ATPaseR01NS051769 · NINDS · MAYO CLINIC ROCHESTER · PI STREHLER, EMANUEL ERNST · 2007 to 2010
$1.4M
NIGMS NIH HHS GM28835NIGMS NIH HHS R01 GM028835NINDS NIH HHS NS51769NINDS NIH HHS R01 NS051769
6 · The paper itself

Abstract

The inhibition by the regulatory domain and the interaction with calmodulin (CaM) vary among plasma membrane calcium pump (PMCA) isoforms. To explore these differences, the kinetics of CaM effects on PMCA4a were investigated and compared with those of PMCA4b. The maximal apparent rate constant for CaM activation of PMCA4a was almost twice that for PMCA4b, whereas the rates of activation for both isoforms showed similar dependence on Ca2+. The inactivation of PMCA4a by CaM removal was also faster than for PMCA4b, and Ca2+ showed a much smaller effect (2- versus 30-fold modification). The rate constants of the individual steps that determine the overall rates were obtained from stopped-flow experiments in which binding of TA-CaM was observed by changes in its fluorescence. TA-CaM binds to two conformations of PMCA4a, an "open" conformation with high activity, and a "closed" one with lower activity. Compared with PMCA4b (Penheiter, A. R., Bajzer, Z., Filoteo, A. G., Thorogate, R., Török, K., and Caride, A. J. (2003) Biochemistry 41, 12115-12124), the model for PMCA4a predicts less inhibition in the closed form and a much faster equilibrium between the open and closed forms. Based on the available kinetic parameters, we determined the constants to fit the shape of a Ca2+ signal in PMCA4b-overexpressing Chinese hamster ovary cells. Using the constants for PMCA4a, and allowing small variations in parameters of other systems contributing to a Ca2+ signal, we then simulated the effect of PMCA4a on the shape of a Ca2+ signal in Chinese hamster ovary cells. The results reproduce the published data (Brini, M., Coletto, L., Pierobon, N., Kraev, N., Guerini, D., and Carafoli, E. (2003) J. Biol. Chem. 278, 24500-24508), and thereby demonstrate the importance of altered regulatory kinetics for the different functional properties of PMCA isoforms.

Indexed as

AnimalsCalcium SignalingCalmodulinCell LineCHO CellsCricetinaeCricetulusHumansKineticsPlasma Membrane Calcium-Transporting ATPasesProtein BindingProtein ConformationProtein IsoformsSpodopteraATP2B4 protein, humanCalmodulinPlasma Membrane Calcium-Transporting ATPasesProtein Isoforms

Identifiers

PMID17595168
PMCPMC2680277
OpenAlexW2023119846

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.