Evidence map›Paper›PMID 27503927›Full record

ArticleCancer research2016

Anticancer Effects of Targeting Hsp70 in Tumor Stromal Cells.

Vladimir L Gabai, Julia A Yaglom, Yongmei Wang, Le Meng, Hao Shao, Geunwon Kim, Teresa Colvin, Jason Gestwicki, Michael Y Sherman

Abstract read
In one paragraph

Article in Cancer research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

22 citing papers in PubMed, 34 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

9 authors at 2 institutions in 1 country.

Vladimir L GabaiDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts. CureLab Oncology, Needham, Massachusetts.
Julia A YaglomDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts.
Yongmei WangDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts.
Le MengDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts. Center for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, Massachusetts.
Hao ShaoDepartment of Pharmaceutical Chemistry and Institute for Neurodegenerative Disease, University of California at San Francisco, San Francisco, California.
Geunwon KimDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts.
Teresa ColvinDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts.
Jason GestwickiDepartment of Pharmaceutical Chemistry and Institute for Neurodegenerative Disease, University of California at San Francisco, San Francisco, California.
Michael Y ShermanDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts. sherma1@bu.edu.
Boston University · USUniversity of California, San Francisco · US

Funding

Molecular Chaperones and Small MoleculesR01NS059690 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Jason E Gestwicki · 2008 to 2026
$7.9M
Complex Role of HSF1 in Breast CancerR01CA176326 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI CALDERWOOD, STUART KEITH, SHERMAN, MICHAEL Y · 2014 to 2018
$1.8M
NCI NIH HHS R01 CA176326NINDS NIH HHS R01 NS059690
6 · The paper itself

Abstract

The stress-induced chaperone protein Hsp70 enables the initiation and progression of many cancers, making it an appealing therapeutic target for development. Here, we show that cancer cells resistant to Hsp70 inhibitors in vitro remain sensitive to them in vivo, revealing the pathogenic significance of Hsp70 in tumor stromal cells rather than tumor cells as widely presumed. Using transgenic mouse models of cancer, we found that expression of Hsp70 in host stromal cells was essential to support tumor growth. Furthermore, genetic ablation or pharmacologic inhibition of Hsp70 suppressed tumor infiltration by macrophages needed to enable tumor growth. Overall, our results illustrate how Hsp70 inhibitors mediate the anticancer effects by targeting both tumor cells and tumor stromal cells, with implications for the broad use of these inhibitors as tools to ablate tumor-associated macrophages that enable malignant progression. Cancer Res; 76(20); 5926-32. ©2016 AACR.

Indexed as

AnimalsAntineoplastic AgentsATP Binding Cassette Transporter, Subfamily B, Member 1Cell Line, TumorHSP70 Heat-Shock ProteinsHumansMacrophagesMiceMice, TransgenicNeoplasms, ExperimentalStromal CellsAntineoplastic AgentsATP Binding Cassette Transporter, Subfamily B, Member 1HSP70 Heat-Shock Proteins

Identifiers

PMID27503927
PMCPMC5065765
OpenAlexW2514978556

What OpenQuestion holds

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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.