Evidence map›Paper›PMID 31591429›Full record

ArticleScientific reports2019

Functional redundancy of HSPA1, HSPA2 and other HSPA proteins in non-small cell lung carcinoma (NSCLC); an implication for NSCLC treatment.

Damian Robert Sojka, Agnieszka Gogler-Pigłowska, Natalia Vydra, Alexander Jorge Cortez, Piotr Teodor Filipczak, Zdzisław Krawczyk, Dorota Scieglinska

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

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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 2 institutions in 2 countries.

Damian Robert SojkaCenter for Translational Research and Molecular Biology of Cancer, Maria Sklodowska-Curie Institute - Oncology Center Gliwice Branch, 44-101, Gliwice, Poland.
Agnieszka Gogler-PigłowskaCenter for Translational Research and Molecular Biology of Cancer, Maria Sklodowska-Curie Institute - Oncology Center Gliwice Branch, 44-101, Gliwice, Poland.
Natalia VydraCenter for Translational Research and Molecular Biology of Cancer, Maria Sklodowska-Curie Institute - Oncology Center Gliwice Branch, 44-101, Gliwice, Poland.
Alexander Jorge CortezCenter for Translational Research and Molecular Biology of Cancer, Maria Sklodowska-Curie Institute - Oncology Center Gliwice Branch, 44-101, Gliwice, Poland.
Piotr Teodor FilipczakCenter for Translational Research and Molecular Biology of Cancer, Maria Sklodowska-Curie Institute - Oncology Center Gliwice Branch, 44-101, Gliwice, Poland.
Zdzisław KrawczykCenter for Translational Research and Molecular Biology of Cancer, Maria Sklodowska-Curie Institute - Oncology Center Gliwice Branch, 44-101, Gliwice, Poland.
Dorota ScieglinskaCenter for Translational Research and Molecular Biology of Cancer, Maria Sklodowska-Curie Institute - Oncology Center Gliwice Branch, 44-101, Gliwice, Poland. dorota.scieglinska@io.gliwice.pl.ORCID http://orcid.org/0000-0003-3489-8464
The Maria Sklodowska-Curie National Research Institute of Oncology · PLLovelace Respiratory Research Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock proteins (HSPs) are a large group of chaperones considered critical for maintaining cellular proteostasis. Their aberrant expression in tumors can modulate the course of processes defined as hallmarks of cancer. Previously, we showed that both stress-inducible HSPA1 and testis-enriched HSPA2, highly homologous members of the HSPA (HSP70) family, are often overexpressed in non-small cell lung carcinoma (NSCLC). HSPA1 is among the best characterized cancer-related chaperones, while the significance of HSPA2 for cancer remains poorly understood. Previously we found that in primary NSCLC, HSPA1 was associated with good prognosis while HSPA2 correlated with bad prognosis, suggesting possible different roles of these proteins in cancer. Therefore, in this work we investigated the impact of HSPA1 and HSPA2 on NSCLC cell phenotype. We found that neither paralog-selective nor simultaneous knockdown of HSPA1 and HSPA2 gene expression reduced growth and chemoresistance of NSCLC cells. Only blocking of HSPA proteins using pan-HSPA inhibitors, VER-155008 or JG-98, exerted potent anticancer effect on NSCLC cells, albeit the final outcome was cell type-dependent. Pan-HSPA inhibition sensitized NSCLC cells to bortezomib, but not to platinum derivates. Our result suggests the inhibitors of proteasome and HSPAs seem an effective drug combination for pre-clinical development in highly aggressive NSCLC.

Indexed as

Carcinoma, Non-Small-Cell LungCell Line, TumorCell ProliferationCisplatinDrug Resistance, NeoplasmGene Knockdown TechniquesHSP70 Heat-Shock ProteinsHSP72 Heat-Shock ProteinsHumansLung NeoplasmsCisplatinHSP70 Heat-Shock ProteinsHSP72 Heat-Shock ProteinsHSPA2 protein, human

Identifiers

PMID31591429
PMCPMC6779912
OpenAlexW2978828954

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.