Evidence map›Paper›PMID 24478313›Full record

ArticleThe Journal of biological chemistry2014

Proteolytic histone modification by mast cell tryptase, a serglycin proteoglycan-dependent secretory granule protease.

Fabio R Melo, Francesca Vita, Beata Berent-Maoz, Francesca Levi-Schaffer, Giuliano Zabucchi, Gunnar Pejler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

31 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Histone Tail Cleavage as a Mechanism for Epigenetic Regulation.International journal of molecular sciences · 2024
    Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Mast Cell and Basophil Granule Proteases -Frontiers in immunology · 2022
    Review
  15. Review
  16. Review
  17. Article
  18. Mast Cell β-Tryptase Is Enzymatically Stabilized by DNA.International journal of molecular sciences · 2020
    Article
  19. Article
  20. 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

6 authors at 3 institutions in 3 countries.

Fabio R MeloFrom the Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, 75123 Uppsala, Sweden.
Francesca Vita
Beata Berent-Maoz
Francesca Levi-Schaffer
Giuliano Zabucchi
Gunnar Pejler
Hebrew University of Jerusalem · ILSwedish University of Agricultural Sciences · SEUniversity of Trieste · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A hallmark feature of mast cells is their high content of cytoplasmic secretory granules filled with various preformed compounds, including proteases of tryptase-, chymase-, and carboxypeptidase A3 type that are electrostatically bound to serglycin proteoglycan. Apart from participating in extracellular processes, serglycin proteoglycan and one of its associated proteases, tryptase, are known to regulate cell death by promoting apoptosis over necrosis. Here we sought to outline the underlying mechanism and identify core histones as primary proteolytic targets for the serglycin-tryptase axis. During the cell death process, tryptase was found to relocalize from granules into the cytosol and nucleus, and it was found that the absence of tryptase was associated with a pronounced accumulation of core histones both in the cytosol and in the nucleus. Intriguingly, tryptase deficiency resulted in defective proteolytic modification of core histones even at baseline conditions, i.e. in the absence of cytotoxic agent, suggesting that tryptase has a homeostatic impact on nuclear events. Indeed, tryptase was found in the nucleus of viable cells and was shown to cleave core histones in their N-terminal tail. Moreover, it was shown that the absence of the serglycin-tryptase axis resulted in altered chromatin composition. Together, these findings implicate histone proteolysis through a secretory granule-derived serglycin-tryptase axis as a novel principle for histone modification, during both cell homeostasis and cell death.

Indexed as

AnimalsApoptosisBone Marrow CellsCell DeathCell NucleusCytosolHistonesMast CellsMiceMice, Inbred C57BLMice, KnockoutMicroscopy, ConfocalMicroscopy, ElectronProtein Structure, TertiaryProteoglycansSecretory VesiclesHistonesProteoglycansserglycinTryptasesVesicular Transport ProteinsApoptosisHistone ModificationMast CellmMCP-6ProteaseProteoglycanProteolytic EnzymesSecretory GranulesSerglycinTryptase

Identifiers

PMID24478313
PMCPMC3953279
OpenAlexW2059919195

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.