Evidence map›Paper›PMID 24158396›Full record

ArticlePlant physiology2013

S-nitrosylation of ascorbate peroxidase is part of programmed cell death signaling in tobacco Bright Yellow-2 cells.

Maria Concetta de Pinto, Vittoria Locato, Alessandra Sgobba, Maria Del Carmen Romero-Puertas, Cosimo Gadaleta, Massimo Delledonne, Laura De Gara

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
18.9field-weighted citation impact, top 1% 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

57 citing papers in PubMed, 144 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. The ascorbate-glutathione cycle coming of age.Journal of experimental botany · 2024
    Review
  6. Article
  7. Review
  8. Redox Signaling in Plant Heat Stress Response.Antioxidants (Basel, Switzerland) · 2023
    Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. 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

7 authors at 4 institutions in 2 countries.

Maria Concetta de PintoDipartimento Biologia, Università degli Studi di Bari, 70125 Bari, Italy.
Vittoria Locato
Alessandra Sgobba
Maria Del Carmen Romero-Puertas
Cosimo Gadaleta
Massimo Delledonne
Laura De Gara
University of Bari Aldo Moro · ITUniversità Campus Bio-Medico · ITConsejo Superior de Investigaciones Científicas · ESUniversity of Verona · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nitric oxide (NO) is a small redox molecule that acts as a signal in different physiological and stress-related processes in plants. Recent evidence suggests that the biological activity of NO is also mediated by S-nitrosylation, a well-known redox-based posttranslational protein modification. Here, we show that during programmed cell death (PCD), induced by both heat shock (HS) or hydrogen peroxide (H2O2) in tobacco (Nicotiana tabacum) Bright Yellow-2 cells, an increase in S-nitrosylating agents occurred. NO increased in both experimentally induced PCDs, although with different intensities. In H2O2-treated cells, the increase in NO was lower than in cells exposed to HS. However, a simultaneous increase in S-nitrosoglutathione (GSNO), another NO source for S-nitrosylation, occurred in H2O2-treated cells, while a decrease in this metabolite was evident after HS. Consistently, different levels of activity and expression of GSNO reductase, the enzyme responsible for GSNO removal, were found in cells subjected to the two different PCD-inducing stimuli: low in H2O2-treated cells and high in the heat-shocked ones. Irrespective of the type of S-nitrosylating agent, S-nitrosylated proteins formed upon exposure to both of the PCD-inducing stimuli. Interestingly, cytosolic ascorbate peroxidase (cAPX), a key enzyme controlling H2O2 levels in plants, was found to be S-nitrosylated at the onset of both PCDs. In vivo and in vitro experiments showed that S-nitrosylation of cAPX was responsible for the rapid decrease in its activity. The possibility that S-nitrosylation induces cAPX ubiquitination and degradation and acts as part of the signaling pathway leading to PCD is discussed.

Indexed as

ApoptosisSignal TransductionAldehyde OxidoreductasesAscorbate PeroxidasesCell LineCell SurvivalCytosolHydrogen PeroxideHydrogen SulfideKineticsModels, BiologicalMolecular Sequence DataNicotianaNitric OxideNitrosationProteolysisAldehyde OxidoreductasesAscorbate Peroxidasesformaldehyde dehydrogenase, glutathione-independentHydrogen PeroxideHydrogen SulfideNitric OxideS-NitrosoglutathioneUbiquitin

Identifiers

PMID24158396
PMCPMC3846137
OpenAlexW2143306658

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.