Evidence map›Paper›PMID 9614190›Full record

ArticleMolecular biology of the cell1998

Delayed activation of the store-operated calcium current induced by calreticulin overexpression in RBL-1 cells.

C Fasolato, P Pizzo, T Pozzan

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Organellar calcium buffers.Cold Spring Harbor perspectives in biology · 2011
    Review
  8. Article
  9. Article
  10. Calreticulin in the heart.Molecular and cellular biochemistry · 2004
    Article
  11. Article
  12. Article
  13. Article
  14. Functional specialization of calreticulin domains.The Journal of cell biology · 2001
    Article
  15. Endoplasmic reticulum in the heart, a forgotten organelle?Molecular and cellular biochemistry · 2001
    Review
  16. Article
  17. Article
  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

3 authors at 1 institution in 1 country.

C FasolatoDepartment of Biomedical Sciences, National Research Center for Biomembranes, University of Padova, I-35121 Padova, Italy. fasolato@civ.bio.unipd.it
P Pizzo
T Pozzan
University of Padua · IT

Funding

Telethon 845
6 · The paper itself

Abstract

Calreticulin (CRT) is a high-capacity, low-affinity Ca2+-binding protein located in the lumen of the endoplasmic reticulum (ER) of all eukaryotic cells investigated so far. Its high level of conservation among different species suggests that it serves functions fundamental to cell survival. The role originally proposed for CRT, i.e., the main Ca2+ buffer of the ER, has been obscured or even casted by its implication in processes as diverse as gene expression, protein folding, and cell adhesion. In this work we seek the role of CRT in Ca2+ storing and signaling by evaluating its effects on the kinetics and amplitude of the store-operated Ca2+ current (ICRAC). We show that, in the rat basophilic leukemia cell line RBL-1, overexpression of CRT, but not of its mutant lacking the high-capacity Ca2+-binding domain, markedly retards the ICRAC development, however, only when store depletion is slower than the rate of current activation. On the contrary, when store depletion is rapid and complete, overexpression of CRT has no effect. The present results are compatible with a major Ca2+-buffering role of CRT within the ER but exclude a direct, or indirect, role of this protein on the mechanism of ICRAC activation.

Indexed as

AnimalsCalciumCalcium-Binding ProteinsCalcium ChannelsCalreticulinChelating AgentsEgtazic AcidElectrophysiologyInositol 1,4,5-TrisphosphateIonomycinIonophoresRatsRecombinant Fusion ProteinsRibonucleoproteinsTumor Cells, Cultured1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acidCalciumCalcium-Binding ProteinsCalcium ChannelsCalreticulinChelating AgentsEgtazic AcidInositol 1,4,5-TrisphosphateIonomycinIonophoresRecombinant Fusion ProteinsRibonucleoproteins

Identifiers

PMID9614190
PMCPMC25376
OpenAlexW2097511933

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.