Evidence map›Paper›PMID 19617626›Full record

ArticleThe Journal of biological chemistry2009

Calpain-1 cleaves and activates caspase-7.

Juliette Gafni, Xin Cong, Sylvia F Chen, Bradford W Gibson, Lisa M Ellerby

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.1field-weighted citation impact, top 15% 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

37 citing papers in PubMed, 67 citations in OpenAlex.

  1. Trial
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  9. Article
  10. Review
  11. The role of calcium-calpain pathway in hyperthermia.Frontiers in molecular medicine · 2022
    Review
  12. Article
  13. A Novel Probe for Spliceosomal Proteins that Induces Autophagy and Death of Melanoma Cells Reveals New Targets for Melanoma Drug Discovery.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. TNFα induces CaJournal of experimental & clinical cancer research : CR · 2018
    Article
  18. Article
  19. The cellular autophagy/apoptosis checkpoint during inflammation.Cellular and molecular life sciences : CMLS · 2017
    Review
  20. Caspase-3 and caspase-8 expression in breast cancer: caspase-3 is associated with survival.Apoptosis : an international journal on programmed cell death · 2017
    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

5 authors at 1 institution in 1 country.

Juliette GafniBuck Institute for Age Research, Novato, California 94945, USA.
Xin Cong
Sylvia F Chen
Bradford W Gibson
Lisa M Ellerby
Buck Institute for Research on Aging · US

Funding

Core--RESEARCH DEVELOPMENTP30AG025708 · NIA · BUCK INSTITUTE FOR RESEARCH ON AGING · PI CAMPISI, JUDITH · 2005 to 2009
$3.7M
TRIPLET REPEAT DISEASE: REQUIREMENT FOR CASPASE CLEAVAGER01NS040251 · NINDS · BUCK INSTITUTE FOR RESEARCH ON AGING · PI ELLERBY, LISA M. · 1999 to 2007
$3.1M
NIA NIH HHS P30 AG025708NINDS NIH HHS NS40251ANINDS NIH HHS R01 NS040251
6 · The paper itself

Abstract

Caspase-7 is an executioner caspase that plays a key role in apoptosis, cancer, and a number of neurodegenerative diseases. The mechanism of caspase-7 activation by granzyme B and caspase-3 has been well characterized. However, whether other proteases such as calpains activate or inactivate caspase-7 is not known. Here, we present that recombinant caspase-7 is directly cleaved by calpain-1 within the large subunit of caspase-7 to produce two novel products, large subunit p18 and p17. This new form of caspase-7 has a 6-fold increase in V(max) when compared with the previously characterized p20/p12 form. Zymography revealed that the smaller caspase-7 product (p17) is 18-fold more active than either the caspase-3-cleaved product (p20) or the larger calpain-1 product of caspase-7 (p18). Mass spectrometry and site-directed mutagenesis identified the calpain cleavage sites within the caspase-7 large subunit at amino acid 36 and 45/47. These proteolysis events occur in vivo as indicated by the accumulation of caspase-7 p18 and p17 subunits in cortical neurons undergoing Ca(2+) dysregulation. Further, cleavage at amino acid 45/47 of caspase-7 by calpain results in a reduction in nuclear localization when compared with the caspase-3 cleavage product of caspase-7 (p20). Our studies suggest the calpain-activated form of caspase-7 has unique enzymatic activity, localization, and binding affinity when compared with the caspase-activated form.

Indexed as

Amino Acid SequenceApoptosisBinding SitesCalpainCaspase 7Cell LineEnzyme ActivationGranzymesHumansMass SpectrometryModels, BiologicalMolecular Sequence DataMutagenesis, Site-DirectedMutationProtein Structure, TertiaryCalpainCaspase 7Granzymes

Identifiers

PMID19617626
PMCPMC2757245
OpenAlexW1973659226

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.