Evidence map›Paper›PMID 28211870›Full record

ReviewCell death and differentiation2017

Non-apoptotic functions of caspases in myeloid cell differentiation.

Stéphanie Solier, Michaela Fontenay, William Vainchenker, Nathalie Droin, Eric Solary

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell death and differentiation, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

33 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
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  3. Review
  4. Review
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  8. Frontiers in immunology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Larval hematopoietic organs of multiplemicroPublication biology · 2024
    Article
  14. Mechanisms ofOpen medicine (Warsaw, Poland) · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Article
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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

5 authors at 3 institutions in 1 country.

Stéphanie SolierInserm U1170, Université Paris-Sud, Faculté de Médecine Paris-Sud, Gustave Roussy, Villejuif, France.
Michaela FontenayINSERM U1016, Institut Cochin, Paris, France.
William VainchenkerInserm U1170, Université Paris-Sud, Faculté de Médecine Paris-Sud, Gustave Roussy, Villejuif, France.
Nathalie DroinInserm U1170, Université Paris-Sud, Faculté de Médecine Paris-Sud, Gustave Roussy, Villejuif, France.
Eric SolaryInserm U1170, Université Paris-Sud, Faculté de Médecine Paris-Sud, Gustave Roussy, Villejuif, France.
Inserm · FRUniversité Paris-Sud · FRAssistance Publique – Hôpitaux de Paris · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Subtle caspase activation is associated with the differentiation of several myeloid lineages. A tightly orchestrated dance between caspase-3 activation and the chaperone HSP70 that migrates to the nucleus to protect the master regulator GATA-1 from cleavage transiently occurs in basophilic erythroblasts and may prepare nucleus and organelle expel that occurs at the terminal phase of erythroid differentiation. A spatially restricted activation of caspase-3 occurs in maturing megakaryocytes to promote proplatelet maturation and platelet shedding in the bloodstream. In a situation of acute platelet need, caspase-3 could be activated in response to IL-1α and promote megakaryocyte rupture. In peripheral blood monocytes, colony-stimulating factor-1 provokes the formation of a molecular platform in which caspase-8 is activated, which downregulates nuclear factor-kappa B (NF-κB) activity and activates downstream caspases whose target fragments such as those generated by nucleophosmin (NPM1) cleavage contribute to the generation of resting macrophages. Human monocytes secrete mature IL-1β in response to lipopolysaccharide through an alternative inflammasome activation that involves caspase-8, a pathway that does not lead to cell death. Finally, active caspase-3 is part of the proteases contained in secretory granules of mast cells. Many questions remain on how these proteases are activated in myeloid cell lineages, which target proteins are cleaved, whereas other are protected from proteolysis, the precise role of cleaved proteins in cell differentiation and functions, and the link between these non-apoptotic functions of caspases and the death of these diverse cell types. Better understanding of these functions may generate therapeutic strategies to control cytopenias or modulate myeloid cell functions in various pathological situations.

Indexed as

AnimalsBlood PlateletsCaspase 3Cell DifferentiationErythroblastsGene Expression RegulationHSP70 Heat-Shock ProteinsHumansMacrophagesMegakaryocytesMonocytesNF-kappa BNuclear ProteinsNucleophosminSignal TransductionCASP3 protein, humanCaspase 3HSP70 Heat-Shock ProteinsNF-kappa BNPM1 protein, humanNuclear ProteinsNucleophosmin

Identifiers

PMID28211870
PMCPMC5520450
OpenAlexW2587847620

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.