Evidence map›Paper›PMID 9620867›Full record

ArticleThe Biochemical journal1998

Inhibition of etoposide-induced apoptosis with peptide aldehyde inhibitors of proteasome.

C Stefanelli, F Bonavita, I Stanic, C Pignatti, G Farruggia, L Masotti, C Guarnieri, C M Caldarera

Abstract read
In one paragraph

Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Proteasome inhibitors disrupt the unfolded protein response in myeloma cells.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Proteasome involvement and accumulation of ubiquitinated proteins in cerebellar granule neurons undergoing apoptosis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000
    Article
  12. Article
  13. 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

8 authors.

C StefanelliDepartment of Biochemistry 'G. Moruzzi', University of Bologna, Via Irnerio 48, I-40126 Bologna, Italy. cstefan@biofarm.unibo.it
F Bonavita
I Stanic
C Pignatti
G Farruggia
L Masotti
C Guarnieri
C M Caldarera

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent investigations have indicated the involvement of proteasome in programmed cell death. The present studies show that although peptide aldehyde inhibitors of proteasome are by themselves weak inducers of apoptosis, they inhibit the apoptotic effect of the anticancer drug etoposide in rat thymocytes. Acetyl-Leu-Leu-norvalinal (LLnV-al) and other related peptide aldehydes inhibited the increase in caspase activity and DNA fragmentation that followed treatment with etoposide and their effect was related to their potency as proteasome inhibitors. To inhibit etoposide-induced apoptosis, LLnV-al must be present within 3 h of treatment with etoposide, in the same way as the inhibitor of protein synthesis cycloheximide must be. Etoposide caused a rapid accumulation of p53 protein that was not inhibited by LLnV-al, which was also a strong inducer of p53. Peptide aldehydes were also weak activators of caspase activity, suggesting that the same mechanism, i.e. the blocking of proteasome function, both triggers apoptosis and inhibits the effect of etoposide. These results are consistent with a model in which proteasome is selectively involved in the pathway used by etoposide to induce cell suicide.

Indexed as

AldehydesAnimalsAntineoplastic Agents, PhytogenicApoptosisCysteine EndopeptidasesCysteine Proteinase InhibitorsDNA FragmentationEtoposideIn Vitro TechniquesLymphocytesMaleMultienzyme ComplexesOligopeptidesProteasome Endopeptidase ComplexRatsRats, WistarAldehydesAntineoplastic Agents, PhytogenicCysteine EndopeptidasesCysteine Proteinase InhibitorsEtoposideMultienzyme ComplexesOligopeptidesProteasome Endopeptidase Complex

Identifiers

PMID9620867
PMCPMC1219525

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.