Evidence map›Paper›PMID 26182360›Full record

ArticleBioscience reports2015

∆Np73 is capable of inducing apoptosis by co-ordinately activating several BH3-only proteins.

Dámaso Sánchez-Carrera, Mikel García-Puga, Lucrecia Yáñez, Íñigo Romón, Carlos Pipaón

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 43% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Review
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 1 institution in 1 country.

Dámaso Sánchez-CarreraLaboratorio de Hematología Molecular, Servicio de Hematología y Hemoterapia, Hospital Universitario Marqués de Valdecilla-IDIVAL, Santander, Spain.
Mikel García-PugaLaboratorio de Hematología Molecular, Servicio de Hematología y Hemoterapia, Hospital Universitario Marqués de Valdecilla-IDIVAL, Santander, Spain.
Lucrecia YáñezLaboratorio de Hematología Molecular, Servicio de Hematología y Hemoterapia, Hospital Universitario Marqués de Valdecilla-IDIVAL, Santander, Spain.
Íñigo RomónLaboratorio de Hematología Molecular, Servicio de Hematología y Hemoterapia, Hospital Universitario Marqués de Valdecilla-IDIVAL, Santander, Spain.
Carlos PipaónLaboratorio de Hematología Molecular, Servicio de Hematología y Hemoterapia, Hospital Universitario Marqués de Valdecilla-IDIVAL, Santander, Spain cpipaon@humv.es.
Instituto de Investigación Marqués de Valdecilla · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inactivation of p53 is one of the most relevant events in human cancer, since it allows transformed cells to escape their own proliferation control and leave them irresponsive to drugs that aim to damage their DNA. When p53 falls, other members of its family may become targets to attack tumoural cells. p73 has shown capacity to mediate these attacks. However, its N-terminal truncated isoforms have been associated with oncogenesis due to their capacity to act as dominant negatives of p53 and the transactivation (TA) isoforms of p73. We previously found a relationship between the overexpression of N-terminus-truncated p73 isoform (∆Np73) and that of the proapoptotic gene Bcl-2-interacting killer (BIK). In the present report we demonstrate that ∆Np73-α has the capacity to induce apoptosis through the co-ordinated activation of a group of genes harbouring GC-rich elements in their regulatory regions. ∆Np73-α synergizes with specificity protein (Sp1) on these elements but the overall response of these genes probably depends on the additional presence of consensus p53 elements. We explore the domains of ∆Np73-α involved in this transactivation capacity and found divergences with the previously described functions for them. Moreover, we found that the transforming mutation V12 of HRas impairs this transactivation capacity of ∆Np73-α, further supporting the anti-tumoural function of this later. Our data add complexity to the action of p73 on the induction of apoptosis and tumourogenesis, opening new interpretations to the expression profile of p73 isoforms in different human neoplasias.

Indexed as

ApoptosisApoptosis Regulatory ProteinsBase CompositionCells, CulturedCross-Linking ReagentsFanconi AnemiaFibroblastsHumansMembrane ProteinsMitochondrial ProteinsMutationPromoter Regions, GeneticProto-Oncogene ProteinsProto-Oncogene Proteins c-bcl-2Response ElementsSp1 Transcription FactorApoptosis Regulatory ProteinsBBC3 protein, humanBIK protein, humanCross-Linking ReagentsMembrane ProteinsMitochondrial ProteinsPMAIP1 protein, humanProto-Oncogene ProteinsProto-Oncogene Proteins c-bcl-2SP1 protein, humanSp1 Transcription FactorTP53 protein, humanTumor Protein p73Tumor Suppressor Protein p53Tumor Suppressor ProteinsapoptosisBH3-only proteinsFanconi anaemia∆Np73p53specificity protein 1 (Sp1)

Identifiers

PMID26182360
PMCPMC4613676
OpenAlexW2320870317

What OpenQuestion holds

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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.