Evidence map›Paper›PMID 21175594›Full record

ArticleClinical and experimental immunology2011

ADAM metallopeptidase domain 17 (ADAM17) is naturally processed through major histocompatibility complex (MHC) class I molecules and is a potential immunotherapeutic target in breast, ovarian and prostate cancers.

G Sinnathamby, J Zerfass, J Hafner, P Block, Z Nickens, A Hobeika, A A Secord, H K Lyerly, M A Morse, R Philip

Open access · greenAbstract read
In one paragraph

Article in Clinical and experimental immunology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.0field-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

19 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. ADAM-Mediated Signalling Pathways in Gastrointestinal Cancer Formation.International journal of molecular sciences · 2020
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Therapeutic vaccines and cancer: focus on DPX-0907.Biologics : targets & therapy · 2014
    Review
  14. Targeting natural killer cells to acute myeloid leukemia in vitro with a CD16 x 33 bispecific killer cell engager and ADAM17 inhibition.Clinical cancer research : an official journal of the American Association for Cancer Research · 2013
    Article
  15. ADAM17 is overexpressed in non-small cell lung cancer and its expression correlates with poor patient survival.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2013
    Article
  16. Article
  17. Prognostic value of ADAM17 in human gastric cancer.Medical oncology (Northwood, London, England) · 2012
    Article
  18. Article
  19. 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

10 authors at 2 institutions in 1 country.

G SinnathambyImmunotope, Inc., The Pennsylvania Biotechnology Center, Doylestown, PA 18902, USA.
J Zerfass
J Hafner
P Block
Z Nickens
A Hobeika
A A Secord
H K Lyerly
M A Morse
R Philip
Immunotope (United States) · USDuke University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Selection of suitable antigens is critical for the development of cancer vaccines. Most desirable are over-expressed cell surface proteins that may serve as targets for both antibodies and T cells, thus maximizing a concerted immune response. Towards this goal, we characterized the relevance of tumour necrosis factor-α-converting enzyme (ADAM17) for such targeted therapeutics. ADAM17 is one of the several metalloproteinases that play a key role in epidermal growth factor receptor (EGFR) signalling and has recently emerged as a new therapeutic target in several tumour types. In the present study, we analysed the expression profile of ADAM17 in a variety of normal and cancer cells of human origin and found that this protein is over-expressed on the surface of several types of cancer cells compared to the normal counterparts. Furthermore, we analysed the presentation of a human leucocyte antigen (HLA)-A2-restricted epitope from ADAM17 protein to specific T cells established from normal donors as well as ovarian cancer patients. Our analysis revealed that the HLA-A2-restricted epitope is processed efficiently and presented by various cancer cells and not by normal cells. Tumour-specific T cell activation results in the secretion of both interferon-γ and granzyme B that can be blocked by HLA-A2 specific antibodies. Collectively, our data present evidence that ADAM17 can be a potential target antigen to devise novel immunotherapeutic strategies against ovarian, breast and prostate cancer.

Indexed as

ImmunotherapyADAM17 ProteinADAM ProteinsAntigen PresentationAntigens, NeoplasmBreast NeoplasmsCell Line, TumorEpitopes, T-LymphocyteFemaleGene ExpressionGene Expression Regulation, NeoplasticGranzymesHistocompatibility Antigens Class IHLA-A2 AntigenHumansInterferon-gammaADAM17 ProteinADAM17 protein, humanADAM ProteinsAntigens, NeoplasmEpitopes, T-LymphocyteGranzymesHistocompatibility Antigens Class IHLA-A2 AntigenInterferon-gammaMembrane ProteinsPeptide Fragments

Identifiers

PMID21175594
PMCPMC3048615
OpenAlexW1943615635

What OpenQuestion holds

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Registered trials

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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.