Evidence map›Paper›PMID 20686127›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2010

Heat shock protein 90 mediates efficient antigen cross presentation through the scavenger receptor expressed by endothelial cells-I.

Ayesha Murshid, Jianlin Gong, Stuart K Calderwood

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
3.8field-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

70 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
  2. The Scavenger Function of LSECs, a Regulator of Liver Diseases.Current issues in molecular biology · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. CanPharmaceuticals (Basel, Switzerland) · 2025
    Review
  8. Article
  9. Article
  10. HSP90 multi-functionality in cancer.Frontiers in immunology · 2024
    Review
  11. Review
  12. Article
  13. Article
  14. Organismal Roles of Hsp90.Biomolecules · 2023
    Review
  15. Molecular Chaperone Receptors: An Update.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  16. Article
  17. Article
  18. Peptide Aggregation Induced Immunogenic Rupture (PAIIR).Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Article
  19. Article
  20. Article

10 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 2 institutions in 1 country.

Ayesha MurshidDivision of Molecular and Cellular Biology, Department of Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA.
Jianlin Gong
Stuart K Calderwood
Beth Israel Deaconess Medical Center · USBoston University · US

Funding

TRANSMEMBRANE SIGNAL MODULATION BY HYPERTHERMIAR01CA047407 · NCI · DANA-FARBER CANCER INSTITUTE · PI CALDERWOOD, STUART KEITH · 1988 to 2014
$4.3M
Extracellular Hsp70 and hyperthermia in tumor therapyR01CA119045 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI CALDERWOOD, STUART KEITH · 2007 to 2016
$3.1M
Gene Repression by HSF1 during hyperthermia and stressesR01CA094397 · NCI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI CALDERWOOD, STUART KEITH · 2002 to 2006
$1.5M
NCI NIH HHS R01 CA047407NCI NIH HHS R01CA047407NCI NIH HHS R01 CA094397NCI NIH HHS R01CA094397NCI NIH HHS R01 CA119045NCI NIH HHS R01CA119045
6 · The paper itself

Abstract

Ag cross presentation is an important mechanism for CD8(+) T cell activation by APCs. We have investigated mechanisms involved in heat shock protein 90 (Hsp90) chaperone-mediated cross presentation of OVA-derived Ags. Hsp90-OVA peptide complexes bound to scavenger receptor expressed by endothelial cells (SREC-I) on the surface of APCs. SREC-I then mediated internalization of Hsp90-OVA polypeptide complexes through a Cdc42-regulated, dynamin-independent endocytic pathway known as the GPI-anchored protein-enriched early endosomal compartment to recycling endosomes. Peptides that did not require processing could then be loaded directly onto MHC class I in endosomes, whereas longer peptides underwent endosomal and cytosomal processing by aminopeptidases and proteases. Cross presentation of Hsp90-chaperoned peptides through this pathway to CD8(+) T cells was highly efficient compared with processing of free polypeptides. In addition, Hsp90 also activated c-Src kinase associated with SREC-I, an activity that we determined to be required for effective cross presentation. Extracellular Hsp90 can thus convey antigenic peptides through an efficient endocytosis pathway in APCs and facilitate cross presentation in a highly regulated manner.

Indexed as

Amino Acid SequenceAnimalsAntigen PresentationAntigen-Presenting CellsBone Marrow CellsCHO CellsCricetinaeCricetulusCross-PrimingCytosolDendritic CellsEndosomesGlycosylphosphatidylinositolsHSP90 Heat-Shock ProteinsHumansMiceGlycosylphosphatidylinositolsHSP90 Heat-Shock ProteinsSCARF1 protein, humanScavenger Receptors, Class F

Identifiers

PMID20686127
PMCPMC4109054
OpenAlexW2122991510

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.