Evidence map›Paper›PMID 27748899›Full record

ArticleInternational journal of oncology2016

Feasibility of imaging of epidermal growth factor receptor expression with ZEGFR:2377 affibody molecule labeled with 99mTc using a peptide-based cysteine-containing chelator.

Ken G Andersson, Maryam Oroujeni, Javad Garousi, Bogdan Mitran, Stefan Ståhl, Anna Orlova, John Löfblom, Vladimir Tolmachev

Abstract read
In one paragraph

Article in International journal of oncology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Article
  2. Review
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  16. Article
  17. Cyclic versus Noncyclic Chelating Scaffold forMolecular pharmaceutics · 2018
    Article
  18. Article
  19. Article
  20. Affibody molecules as engineered protein drugs.Experimental & molecular medicine · 2017
    Review
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

8 authors.

Ken G AnderssonDivision of Protein Technology, KTH Royal Institute of Technology, SE-10691 Stockholm, Sweden.
Maryam OroujeniInstitute of Immunology, Genetic and Pathology, Uppsala University, SE-75185 Uppsala, Sweden.
Javad GarousiInstitute of Immunology, Genetic and Pathology, Uppsala University, SE-75185 Uppsala, Sweden.
Bogdan MitranDivision of Molecular Imaging, Department of Medicinal Chemistry, Uppsala University, SE-75183 Uppsala, Sweden.
Stefan StåhlDivision of Protein Technology, KTH Royal Institute of Technology, SE-10691 Stockholm, Sweden.
Anna OrlovaDivision of Molecular Imaging, Department of Medicinal Chemistry, Uppsala University, SE-75183 Uppsala, Sweden.
John LöfblomDivision of Protein Technology, KTH Royal Institute of Technology, SE-10691 Stockholm, Sweden.
Vladimir TolmachevInstitute of Immunology, Genetic and Pathology, Uppsala University, SE-75185 Uppsala, Sweden.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The epidermal growth factor receptor (EGFR) is overexpressed in a number of malignant tumors and is a molecular target for several specific anticancer antibodies and tyrosine kinase inhibitors. The overexpression of EGFR is a predictive biomarker for response to several therapy regimens. Radionuclide molecular imaging might enable detection of EGFR overexpression by a non-invasive procedure and could be used repeatedly. Affibody molecules are engineered scaffold proteins, which could be selected to have a high affinity and selectivity to predetermined targets. The anti-EGFR ZEGFR:2377 affibody molecule is a potential imaging probe for EGFR detection. The use of the generator-produced radionuclide 99mTc should facilitate clinical translation of an imaging probe due to its low price, availability and favorable dosimetry of the radionuclide. In the present study, we evaluated feasibility of ZEGFR:2377 labeling with 99mTc using a peptide-based cysteine-containing chelator expressed at the C-terminus of ZEGFR:2377. The label was stable in vitro under cysteine challenge. In addition, 99mTc-ZEGFR:2377 was capable of specific binding to EGFR-expressing cells with high affinity (274 pM). Studies in BALB/C nu/nu mice bearing A431 xenografts demonstrated that 99mTc-ZEGFR:2377 accumulates in tumors in an EGFR-specific manner. The tumor uptake values were 3.6±1 and 2.5±0.4% ID/g at 3 and 24 h after injection, respectively. The corresponding tumor-to-blood ratios were 1.8±0.4 and 8±3. The xenografts were clearly visualized at both time-points. This study demonstrated the potential of 99mTc-labeled ZEGFR:2377 for imaging of EGFR in vivo.

Indexed as

AnimalsCell Line, TumorErbB ReceptorsHumansMiceMice, Inbred BALB CMice, NudeMolecular ImagingNeoplasm TransplantationRadioisotopesRadionuclide ImagingRecombinant Fusion ProteinsTechnetiumTransplantation, HeterologousEGFR protein, humanErbB ReceptorsRadioisotopesRecombinant Fusion ProteinsTechnetium

Identifiers

PMID27748899
PMCPMC5118000

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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.