Evidence map›Paper›PMID 25989275›Full record

ArticleBritish journal of cancer2015

KPNA2 is a nuclear export protein that contributes to aberrant localisation of key proteins and poor prognosis of breast cancer.

A T Alshareeda, O H Negm, A R Green, C C Nolan, P Tighe, N Albarakati, R Sultana, S Madhusudan, I O Ellis, E A Rakha

Open access · hybridAbstract read
In one paragraph

Article in British journal of cancer, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed, 1 pooled it
3.6field-weighted citation impact, top 7% 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

44 citing papers in PubMed, 1 synthesis or guideline pooled it, 74 citations in OpenAlex.

  1. Pooled it
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  3. The role of KPNA3 in multiple myeloma: implications for targeting nuclear import.Apoptosis : an international journal on programmed cell death · 2026
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  20. KPNA2 promotes renal cell carcinoma proliferation and metastasis via NPM.Journal of cellular and molecular medicine · 2021
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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

10 authors at 3 institutions in 1 country.

A T Alshareeda1] Department of Histopathology and School of Medicine, The University of Nottingham and Nottingham University Hospitals NHS Trust, Nottingham City Hospital, Nottingham, UK [2] Ministry of Higher Education, Riyadh, Saudi Arabia.
O H Negm1] Immunology Department, School of Life Sciences, University of Nottingham, Nottingham, UK [2] Medical Microbiology and Immunology Department, Faculty of Medicine, Mansoura University, Mansoura, Egypt.
A R GreenDepartment of Histopathology and School of Medicine, The University of Nottingham and Nottingham University Hospitals NHS Trust, Nottingham City Hospital, Nottingham, UK.
C C NolanDepartment of Histopathology and School of Medicine, The University of Nottingham and Nottingham University Hospitals NHS Trust, Nottingham City Hospital, Nottingham, UK.
P TigheImmunology Department, School of Life Sciences, University of Nottingham, Nottingham, UK.
N AlbarakatiDepartment of Oncology and School of Medicine, The University of Nottingham and Nottingham University Hospitals NHS Trust, Nottingham City Hospital, Nottingham, UK.
R SultanaDepartment of Oncology and School of Medicine, The University of Nottingham and Nottingham University Hospitals NHS Trust, Nottingham City Hospital, Nottingham, UK.
S MadhusudanDepartment of Oncology and School of Medicine, The University of Nottingham and Nottingham University Hospitals NHS Trust, Nottingham City Hospital, Nottingham, UK.
I O EllisDepartment of Histopathology and School of Medicine, The University of Nottingham and Nottingham University Hospitals NHS Trust, Nottingham City Hospital, Nottingham, UK.
E A RakhaDepartment of Histopathology and School of Medicine, The University of Nottingham and Nottingham University Hospitals NHS Trust, Nottingham City Hospital, Nottingham, UK.
University of Nottingham · GBNottingham City Hospital · GBNottingham University Hospitals NHS Trust · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundIt is recognised that modulations of the nuclear import of macromolecules have a role in changing cellular phenotypes and carcinogenesis. We and others have noticed that aberrant subcellular localisation of DNA damage response (DDR) proteins in breast cancer (BC) is associated with loss-of-function phenotype. This study aims to investigate the biological and clinical significance of the nucleocytoplasmic transport protein karyopherin α-2 (KPNA2), and its role in controlling DDR proteins subcellular localisation in BC.

methodsA large (n=1494) and well-characterised series of early-stage invasive BC with a long-term follow-up was assessed for KPNA2 protein by using immunohistochemistry.

resultsKPNA2 expression was associated with the subcellular localisation of key DDR proteins that showed cytoplasmic expression including BRCA1, RAD51, SMC6L1, γH2AX, BARD1, UBC9, PIAS1 and CHK1. High level of KPNA2 was associated not only with cytoplasmic localisation of these proteins but also with their low/negative nuclear expression. Positive KPNA2 expression was associated with negative oestrogen receptor and triple-negative phenotype. Survival analysis showed that KPNA2 was associated with poor outcome (P<0.0001), but this effect was not independent of other prognostic variables.

conclusionsThis study provides further evidence for the complexity of DDR mechanism in BC, and that KNPA2 has a role in the aberrant subcellular localisation of DDR proteins with subsequent impaired function.

Indexed as

DNA DamageActive Transport, Cell Nucleusalpha KaryopherinsBiomarkers, TumorBRCA1 ProteinBreast NeoplasmsCell Cycle ProteinsCell Line, TumorCell NucleusCheckpoint Kinase 1Cohort StudiesCytoplasmFemaleHistonesHumansImmunohistochemistryalpha KaryopherinsBARD1 protein, humanBiomarkers, TumorBRCA1 ProteinBRCA1 protein, humanCell Cycle ProteinsCheckpoint Kinase 1CHEK1 protein, humanH2AX protein, humanHistonesKPNA2 protein, humanPIAS1 protein, humanProtein Inhibitors of Activated STATProtein KinasesRAD51 protein, humanRad51 RecombinaseSmall Ubiquitin-Related Modifier ProteinsSMC6 protein, humanTumor Suppressor ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Ubiquitin-Protein Ligases

Identifiers

PMID25989275
PMCPMC4580386
OpenAlexW1890349608

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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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.