Evidence map›Paper›PMID 11408569›Full record

ArticleMolecular biology of the cell2001

Involvement of p38 in apoptosis-associated membrane blebbing and nuclear condensation.

R G Deschesnes, J Huot, K Valerie, J Landry

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.2field-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

36 citing papers in PubMed, 120 citations in OpenAlex.

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  15. Glabridin arrests cell cycle and inhibits proliferation of hepatocellular carcinoma by suppressing braf/MEK signaling pathway.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
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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

4 authors at 2 institutions in 2 countries.

R G DeschesnesCentre de recherche en cancérologie de l'Université Laval, L'Hôtel-Dieu de Québec, Centre hospitalier universitaire de Québec, 9 rue McMahon, Québec, Canada G1R 2J6.
J Huot
K Valerie
J Landry
Hôtel-Dieu de Québec · CAVirginia Commonwealth University Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The stress-activated protein kinase p38 is often induced by cytotoxic agents, but its contribution to cell death is ill defined. In Rat-1 cells, we found a strong correlation between activation of p38 and induction of c-Myc-dependent apoptosis. In cells with deregulated c-Myc expression but not in control cells, cis-diamminedichloroplatinum induced p38 activity and typical features of apoptosis, including internucleosomal DNA degradation, induction of caspase activities, and both nuclear (nuclear condensation and fragmentation) and extranuclear (cell blebbing) morphological alterations. The pan-caspase inhibitor N-benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone did not block p38 activation and the p38 inhibitor SB203580 had no detectable effect on the activation of caspases or the in vivo cleavage of several caspase substrates, suggesting that p38 and caspase activation can contribute distinct features of apoptosis. Accordingly, we found that cell blebbing was independent of caspase activity and, rather, depended on p38-sensitive changes in microfilament dynamics likely mediated by heat shock protein 27 phosphorylation. Furthermore, p38 activity contributed to both caspase-dependent and caspase-independent nuclear condensation and fragmentation, suggesting a role in an early event triggering both mechanisms of apoptosis or sensitizing the cells to the action of both types of apoptosis executioners. Inhibiting p38 also resulted in a significant enhancement in cell survival estimated by colony formation. This capacity to modulate the sensitivity to apoptosis in cells with deregulated c-Myc expression suggests an important role for p38 in tumor cell killing by chemotherapeutic agents.

Indexed as

ApoptosisHeat-Shock ProteinsAmino Acid Chloromethyl KetonesAnimalsAntineoplastic AgentsCaspasesCell LineCell MembraneCell NucleusCell SurvivalCisplatinDNA FragmentationDose-Response Relationship, DrugEnzyme InhibitorsGene Expression RegulationHeLa CellsAmino Acid Chloromethyl KetonesAntineoplastic Agentsbenzyloxycarbonyl-valyl-alanyl-(methyl)aspartic acid fluoromethyl ketoneCaspasesCisplatinEnzyme InhibitorsHeat-Shock ProteinsHSP27 Heat-Shock ProteinsHSPB1 protein, humanHspb1 protein, ratHydrogen PeroxideImidazolesIntracellular Signaling Peptides and ProteinsMAP-Kinase-Activated Kinase 2Mitogen-Activated Protein KinasesMolecular ChaperonesNeoplasm Proteinsp38 Mitogen-Activated Protein KinasesProtein Serine-Threonine KinasesProto-Oncogene Proteins c-mycPyridinesSB 203580

Identifiers

PMID11408569
PMCPMC37325
OpenAlexW2168647880

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.