Evidence map›Paper›PMID 10839810›Full record

ArticleThe Journal of experimental medicine2000

Receptor-mediated uptake of antigen/heat shock protein complexes results in major histocompatibility complex class I antigen presentation via two distinct processing pathways.

F Castellino, P E Boucher, K Eichelberg, M Mayhew, J E Rothman, A N Houghton, R N Germain

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
9.6field-weighted citation impact, top 1% 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

99 citing papers in PubMed, 400 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Review
  5. Article
  6. The Role of the NKG2D in Vitiligo.Frontiers in immunology · 2021
    Review
  7. Review
  8. Role of Heat Shock Proteins in Glaucoma.International journal of molecular sciences · 2019
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. High molecular weight stress proteins: Identification, cloning and utilisation in cancer immunotherapy.International journal of hyperthermia : the official journal of European Society for Hyperthermic Oncology, North American Hyperthermia Group · 2013
    Review

39 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

7 authors at 3 institutions in 1 country.

F CastellinoLaboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892-1892, USA.
P E Boucher
K Eichelberg
M Mayhew
J E Rothman
A N Houghton
R N Germain
Memorial Sloan Kettering Cancer Center · USNational Institutes of Health · USCenter for Biologics Evaluation and Research · US

Funding

Multiscale Analysis of Immune ResponsesZIAAI000545 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI GERMAIN, RONALD N · 2009 to 2025
$29.4M
Multiscale Analysis of Immune ResponsesZ01AI000545 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI GERMAIN, RONALD N · 1990 to 2008
$4.5M
6 · The paper itself

Abstract

Heat shock proteins (HSPs) derived from tumors or virally infected cells can stimulate antigen-specific CD8(+) T cell responses in vitro and in vivo. Although this antigenicity is known to arise from HSP-associated peptides presented to the immune system by major histocompatibility complex (MHC) class I molecules, the cell biology underlying this presentation process remains poorly understood. Here we show that HSP 70 binds to the surface of antigen presenting cells by a mechanism with the characteristics of a saturable receptor system. After this membrane interaction, processing and MHC class I presentation of the HSP-associated antigen can occur via either a cytosolic (transporter associated with antigen processing [TAP] and proteasome-dependent) or an endosomal (TAP and proteasome-independent) route, with the preferred pathway determined by the sequence context of the optimal antigenic peptide within the HSP-associated material. These findings not only characterize two highly efficient, specific pathways leading to the conversion of HSP-associated antigens into ligands for CD8(+) T cells, they also imply the existence of a mechanism for receptor-facilitated transmembrane transport of HSP or HSP-associated ligands from the plasma membrane or lumen of endosomes into the cytosol.

Indexed as

Amino Acid SequenceAnimalsAntigen PresentationCattleCells, CulturedCysteine EndopeptidasesEgg ProteinsH-2 AntigensHSP70 Heat-Shock ProteinsMacrophage-1 AntigenMacrophages, PeritonealMiceMice, Inbred C3HMice, Inbred C57BLMolecular Sequence DataMultienzyme ComplexesCysteine EndopeptidasesEgg ProteinsH-2 AntigensH-2Kb protein, mouseHSP70 Heat-Shock ProteinsMacrophage-1 AntigenMultienzyme ComplexesOVA-8OvalbuminPeptide FragmentsProteasome Endopeptidase Complex

Identifiers

PMID10839810
PMCPMC2213527
OpenAlexW1972486638

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.