Evidence map›Paper›PMID 22360692›Full record

ArticleThe Biochemical journal2012

Heat-shock proteins attenuate SERCA inactivation by the anti-apoptotic protein Bcl-2: possible implications for the ER Ca2+-mediated apoptosis.

Elena S Dremina, Victor S Sharov, Christian Schöneich

Abstract read
In one paragraph

Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Trial
  2. Article
  3. Isolation of the Sarcoplasmic Reticulum CaMethods and protocols · 2023
    Article
  4. Article
  5. Review
  6. Targeting Bcl-2-IPBiochimica et biophysica acta. Molecular cell research · 2018
    Review
  7. Review
  8. Article
  9. Review
  10. Inhibition and conformational change of SERCA3b induced by Bcl-2.Biochimica et biophysica acta. Proteins and proteomics · 2017
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Apoptosis in differentiating C2C12 muscle cells selectively targets Bcl-2-deficient myotubes.Apoptosis : an international journal on programmed cell death · 2014
    Article
  18. The selective BH4-domain biology of Bcl-2-family members: IP3Rs and beyond.Cellular and molecular life sciences : CMLS · 2013
    Review
  19. 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.

Elena S DreminaDepartment of Pharmaceutical Chemistry, University of Kansas, Lawrence, 66047, USA.
Victor S Sharov
Christian Schöneich
University of Kansas · US

Funding

SARCOPENIA AND APOPTOSIS: ROLE OF SERCA AND BCL-2P01AG012993 · NIA · UNIVERSITY OF KANSAS LAWRENCE · PI WILLIAMS, TODD D · 1995 to 2012
$14.0M
NIA NIH HHS P01 AG012993NIA NIH HHS P01AG12993
6 · The paper itself

Abstract

We have demonstrated previously that Bcl-2 and Bcl-2Δ21, a C-terminally truncated Bcl-2 sequence, inactivate SERCA (sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase) 1 in isolated SR (sarcoplasmic reticulum), accompanied by a translocation from CRDs (caveolae-related domains) of the SR. In the present study, we obtained evidence for the interaction of Bcl-2 with SERCA2b in C2C12 myoblasts and HEK (human embryonic kidney)-293 cells. Bcl-2 and SERCA2b co-immunoprecipitated from lysate and microsomal fractions of Bcl-2-overexpressing cells. However, Bcl-2 overexpression resulted only in a slight translocation from the CRDs and no significant SERCA inactivation. In isolated HEK-293 cell microsomes, incubation with Bcl-2Δ21 afforded SERCA2b inactivation and some translocation. HSP (heat-shock protein) 70, HSP90, HSP27 and α-crystallin attenuated Bcl-2Δ21-dependent SERCA2b inactivation. An in vitro mechanistic study with the SERCA1 isoform shows that HSP70 (i) protects SERCA1 from the inactivation by Bcl-2Δ21, (ii) inhibits SERCA1 translocation from CRD fractions, and (iii) prevents the Bcl-2Δ21-dependent loss of FITC labelling. Our data demonstrate that the mechanism of SERCA inactivation by Bcl-2 established in vitro for the SERCA1 isoform can be extended to the main housekeeping SERCA2b isoform, and that functional interactions of SERCA2b and Bcl-2 in the cell may be modulated by HSP70 and other chaperones and stress-regulated proteins.

Indexed as

ApoptosisAnimalsCalciumCell LineEndoplasmic ReticulumHSP70 Heat-Shock ProteinsHumansIn Vitro TechniquesMiceMicrosomesMuscle, SkeletalMyoblastsProtein IsoformsProtein TransportProto-Oncogene Proteins c-bcl-2RatsCalciumHSP70 Heat-Shock ProteinsProtein IsoformsProto-Oncogene Proteins c-bcl-2Sarcoplasmic Reticulum Calcium-Transporting ATPases

Identifiers

PMID22360692
PMCPMC3736812
OpenAlexW2008091311

What OpenQuestion holds

Textmetadata
LicenceTDM
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.