Evidence map›Paper›PMID 21982864›Full record

ReviewBiochimica et biophysica acta2012

Secreted heat shock protein-90 (Hsp90) in wound healing and cancer.

Wei Li, Divya Sahu, Fred Tsen

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

116 citing papers in PubMed, 211 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Exosome Mediated Cell-Cell Crosstalk in Tissue Injury and Repair.Results and problems in cell differentiation · 2024
    Review
  20. Article

56 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Wei LiThe Department of Dermatology, the University of Southern California, Los Angeles, CA, USA. wli@usc.edu
Divya Sahu
Fred Tsen
University of Southern California · US

Funding

Mechanisms of Human Dermal Fibroblast MigrationR01GM067100 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LI, WEI · 2003 to 2020
$5.2M
Signal Transduction of Human Keratinocyte MigrationR01GM066193 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LI, WEI · 2002 to 2010
$2.3M
Development of Extracellular Heat Shock Protein-90 as a Novel Topical Wound HealingR01AR059853 · NIAMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LI, WEI · 2011 to 2015
$1.8M
NIAMS NIH HHS R01 AR059853NIGMS NIH HHS GM066193NIGMS NIH HHS GM067100NIGMS NIH HHS R01 GM066193NIGMS NIH HHS R01 GM067100
6 · The paper itself

Abstract

Extracellular Hsp90 proteins, including "membrane-bound", "released" and "secreted", were first reported more than two decades ago. Only studies of the past 7years have begun to reveal a picture for when, how and why Hsp90 gets exported by both normal and tumor cells. Normal cells secrete Hsp90 in response to tissue injury. Tumor cells have managed to constitutively secrete Hsp90 for tissue invasion. In either case, sufficient supply of the extracellular Hsp90 can be guaranteed by its unusually abundant storage inside the cells. A well-characterized function of secreted Hsp90α is to promote cell motility, a crucial event for both wound healing and cancer. The reported targets for extracellular Hsp90α include MMP2, LRP-1, tyrosine kinase receptors and possibly more. The pro-motility activity of secreted Hsp90α resides within a fragment, called 'F-5', at the boundary between linker region and middle domain. Inhibition of its secretion, neutralization of its extracellular action or interruption of its signaling through LRP-1 block wound healing and tumor invasion in vitro and in vivo. In normal tissue, topical application of F-5 promotes acute and diabetic wound healing far more effectively than US FDA-approved conventional growth factor therapy in mice. In cancer, drugs that selectively target the F-5 region of secreted Hsp90 by cancer cells may be more effective and less toxic than those that target the ATPase of the intracellular Hsp90. This article is part of a Special Issue entitled: Heat Shock Protein 90 (HSP90).

Indexed as

Amino Acid SequenceAnimalsHSP90 Heat-Shock ProteinsHumansMolecular Sequence DataNeoplasmsSignal TransductionWound HealingHSP90 Heat-Shock Proteins

Identifiers

PMID21982864
PMCPMC3266443
OpenAlexW2002329594

What OpenQuestion holds

Textmetadata
LicenceTDM
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.