Evidence map›Paper›PMID 19802014›Full record

ArticleOncogene2010

Heat shock cognate 70 protein secretion as a new growth arrest signal for cancer cells.

P Nirdé, D Derocq, M Maynadier, M Chambon, I Basile, M Gary-Bobo, M Garcia

Open access · greenAbstract read
In one paragraph

Article in Oncogene, 2010. 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
1.3field-weighted citation impact, top 21% 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, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Tumor suppressive functions of WNT5A in rhabdomyosarcoma.International journal of oncology · 2022
    Article
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  7. Review
  8. All-or-none amyloid disassembly via chaperone-triggered fibril unzipping favors clearance of α-synuclein toxic species.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Review
  11. Article
  12. Unconventional Secretion of Heat Shock Proteins in Cancer.International journal of molecular sciences · 2017
    Review
  13. Yeast as a tool to explore cathepsin D function.Microbial cell (Graz, Austria) · 2015
    Review
  14. Article
  15. Metastasis review: from bench to bedside.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
    Review
  16. Article
  17. Article
  18. 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

7 authors at 4 institutions in 1 country.

P NirdéIRCM, institut de Recherche en Cancérologie de Montpellier, Montpellier, France.
D Derocq
M Maynadier
M Chambon
I Basile
M Gary-Bobo
M Garcia
Institut de Recherche en Cancérologie de Montpellier · FRCEA Valduc · FRInserm · FRUniversité de Montpellier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Earlier studies indicated that density-arrested cancer cells released an unidentified growth inhibitor whose secretion was prevented by overexpression of the lysosomal protease cathepsin D (cath D). In this study, this growth inhibitor was purified by affinity chromatography and identified as the heat shock cognate 70 protein (hsc70) based on its peptide microsequencing and specific antibody recognition. Among intracellular proteins, including other heat shock proteins, only constitutive hsc70 was secreted in response to the high-cell density. Moreover, hsc70 secretion from cancer cells was generated by serum deprivation, whereas its cellular concentration did not change. Prevention of Hsc70 secretion by cath D overexpression was associated with the formation of multilayer cell cultures, thus indicating a loss of contact inhibition. In addition, we showed that supplementing the culture medium with purified hsc70 inhibited cell proliferation in the nanomolar range. Conversely, removal of this extracellular hsc70 from the medium by either retention on ADP-agarose or competition at the Hsc70 binding site restored cell proliferation. Hsc70 appears active in human breast cancer cells and hypersecreted by direct cath D inhibition. These results suggest a new role of this secreted hsc70 chaperone in cell proliferation that might account for the higher tumor growth of cancer cells overexpressing cath D.

Indexed as

Cell ProliferationAnimalsBlotting, WesternBreast NeoplasmsCathepsin DCell CountCell LineCell Line, TumorChromatography, High Pressure LiquidCulture Media, Serum-FreeElectrophoresis, Polyacrylamide GelFemaleHSC70 Heat-Shock ProteinsHumansMicroscopy, Electron, ScanningNeoplasmsCathepsin DCulture Media, Serum-FreeHSC70 Heat-Shock ProteinsRecombinant Proteins

Identifiers

PMID19802014
PMCPMC2864961
OpenAlexW2027651772

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.