Evidence map›Paper›PMID 11524434›Full record

ArticleThe Journal of cell biology2001

Functional specialization of calreticulin domains.

K Nakamura, A Zuppini, S Arnaudeau, J Lynch, I Ahsan, R Krause, S Papp, H De Smedt, J B Parys, W Muller-Esterl and 5 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

111 citing papers in PubMed, 311 citations in OpenAlex.

  1. Article
  2. Review
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  12. Article
  13. Calreticulin as a marker and therapeutic target for cancer.Clinical and experimental medicine · 2023
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Resveratrol Treatment in HumanBiomolecules · 2021
    Article

51 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

15 authors at 7 institutions in 4 countries.

K NakamuraCanadian Institutes of Health Research Group in Molecular Biology of Membranes and the Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
A Zuppini
S Arnaudeau
J Lynch
I Ahsan
R Krause
S Papp
H De Smedt
J B Parys
W Muller-Esterl
D P Lew
K H Krause
N Demaurex
M Opas
M Michalak
University Hospital of Geneva · CHUniversity of Alberta · CACanadian Institutes of Health Research · CAKU Leuven · BEUniversity of Geneva · CHUniversity of Toronto · CAUniversity Hospital Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calreticulin is a Ca2+-binding chaperone in the endoplasmic reticulum (ER), and calreticulin gene knockout is embryonic lethal. Here, we used calreticulin-deficient mouse embryonic fibroblasts to examine the function of calreticulin as a regulator of Ca2+ homeostasis. In cells without calreticulin, the ER has a lower capacity for Ca2+ storage, although the free ER luminal Ca2+ concentration is unchanged. Calreticulin-deficient cells show inhibited Ca2+ release in response to bradykinin, yet they release Ca2+ upon direct activation with the inositol 1,4,5-trisphosphate (InsP3). These cells fail to produce a measurable level of InsP3 upon stimulation with bradykinin, likely because the binding of bradykinin to its cell surface receptor is impaired. Bradykinin binding and bradykinin-induced Ca2+ release are both restored by expression of full-length calreticulin and the N + P domain of the protein. Expression of the P + C domain of calreticulin does not affect bradykinin-induced Ca2+ release but restores the ER Ca2+ storage capacity. Our results indicate that calreticulin may play a role in folding of the bradykinin receptor, which affects its ability to initiate InsP3-dependent Ca2+ release in calreticulin-deficient cells. We concluded that the C domain of calreticulin plays a role in Ca2+ storage and that the N domain may participate in its chaperone functions.

Indexed as

AnimalsBradykininCalciumCalcium-Binding ProteinsCalcium ChannelsCalcium-Transporting ATPasesCalreticulinCell LineEndoplasmic ReticulumEnzyme InhibitorsFibroblastsFlow CytometryHomeostasisImmunoblottingInositol 1,4,5-Trisphosphate ReceptorsMiceBradykininCalciumCalcium-Binding ProteinsCalcium ChannelsCalcium-Transporting ATPasesCalreticulinEnzyme InhibitorsInositol 1,4,5-Trisphosphate ReceptorsMolecular ChaperonesProtein IsoformsReceptors, BradykininReceptors, Cytoplasmic and NuclearRibonucleoproteinsSarcoplasmic Reticulum Calcium-Transporting ATPasesThapsigargin

Identifiers

PMID11524434
PMCPMC2196195
OpenAlexW2135913162

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.