Evidence map›Paper›PMID 25419715›Full record

ArticlePloS one2014

TRIM28 and β-actin identified via nanobody-based reverse proteomics approach as possible human glioblastoma biomarkers.

Ivana Jovčevska, Neja Zupanec, Nina Kočevar, Daniela Cesselli, Neža Podergajs, Clara Limbaeck Stokin, Michael P Myers, Serge Muyldermans, Gholamreza Hassanzadeh Ghassabeh, Helena Motaln and 4 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 31 citations in OpenAlex.

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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

14 authors at 6 institutions in 3 countries.

Ivana JovčevskaMedical Centre for Molecular Biology, Institute of Biochemistry, Faculty of Medicine, University of Ljubljana, Ljubljana, Slovenia.
Neja ZupanecMedical Centre for Molecular Biology, Institute of Biochemistry, Faculty of Medicine, University of Ljubljana, Ljubljana, Slovenia.
Nina KočevarMedical Centre for Molecular Biology, Institute of Biochemistry, Faculty of Medicine, University of Ljubljana, Ljubljana, Slovenia.
Daniela CesselliDepartment of Medical and Biological Sciences (DSMB), University of Udine, Udine, Italy.
Neža PodergajsDepartment of Genetic Toxicology and Cancer Biology, National Institute of Biology (NIB), Ljubljana, Slovenia.
Clara Limbaeck StokinInstitute of Pathology, Faculty of Medicine, University of Ljubljana, Ljubljana, Slovenia.
Michael P MyersInternational Centre for Genetic Engineering and Biotechnology (ICGEB), Trieste, Italy.
Serge MuyldermansCellular and Molecular Immunology, Vrije Universiteit Brussel (VUB), Brussels, Belgium; Structural Biology Research Center, VIB, Brussels, Belgium.
Gholamreza Hassanzadeh GhassabehCellular and Molecular Immunology, Vrije Universiteit Brussel (VUB), Brussels, Belgium; Nanobody Service Facility, VIB, Brussels, Belgium.
Helena MotalnDepartment of Genetic Toxicology and Cancer Biology, National Institute of Biology (NIB), Ljubljana, Slovenia.
Maria Elisabetta RuaroDepartment of Medical and Biological Sciences (DSMB), University of Udine, Udine, Italy.
Evgenia BourkoulaDepartment of Medical and Biological Sciences (DSMB), University of Udine, Udine, Italy.
Tamara Lah TurnšekDepartment of Genetic Toxicology and Cancer Biology, National Institute of Biology (NIB), Ljubljana, Slovenia.
Radovan KomelMedical Centre for Molecular Biology, Institute of Biochemistry, Faculty of Medicine, University of Ljubljana, Ljubljana, Slovenia.
University of Ljubljana · SINational Institute of Biology · SIUniversity of Udine · ITInternational Centre for Genetic Engineering and Biotechnology · ITVIB-VUB Center for Structural Biology · BEVrije Universiteit Brussel · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Malignant gliomas are among the rarest brain tumours, and they have the worst prognosis. Grade IV astrocytoma, known as glioblastoma multiforme (GBM), is a highly lethal disease where the standard therapies of surgery, followed by radiation and chemotherapy, cannot significantly prolong the life expectancy of the patients. Tumour recurrence shows more aggressive form compared to the primary tumour, and results in patient survival from 12 to 15 months only. Although still controversial, the cancer stem cell hypothesis postulates that cancer stem cells are responsible for early relapse of the disease after surgical intervention due to their high resistance to therapy. Alternative strategies for GBM therapy are thus urgently needed. Nanobodies are single-domain antigen-binding fragments of heavy-chain antibodies, and together with classical antibodies, they are part of the camelid immune system. Nanobodies are small and stable, and they share a high degree of sequence identity to the human heavy chain variable domain, and these characteristics offer them advantages over classical antibodies or antibody fragments. We first immunised an alpaca with a human GBM stem-like cell line prepared from primary GBM cultures. Next, a nanobody library was constructed in a phage-display vector. Using nanobody phage-display technology, we selected specific GBM stem-like cell binders through a number of affinity selections, using whole cell protein extracts and membrane protein-enriched extracts from eight different GBM patients, and membrane protein-enriched extracts from two established GBM stem-like cell lines (NCH644 and NCH421K cells). After the enrichment, periplasmic extract ELISA was used to screen for specific clones. These nanobody clones were recloned into the pHEN6 vector, expressed in Escherichia coli WK6, and purified using immobilised metal affinity chromatography and size-exclusion chromatography. Specific nanobody:antigen pairs were obtained and mass spectrometry analysis revealed two proteins, TRIM28 and β-actin, that were up-regulated in the GBM stem-like cells compared to the controls.

Indexed as

ActinsAmino Acid SequenceAnimalsAntibody AffinityBiomarkers, TumorBlotting, WesternBrain NeoplasmsCamelids, New WorldCell Line, TumorGlioblastomaHumansMaleMass SpectrometryMolecular Sequence DataNeoplastic Stem CellsPeptide LibraryActinsBiomarkers, TumorPeptide LibraryRepressor ProteinsSingle-Domain AntibodiesTRIM28 protein, humanTripartite Motif-Containing Protein 28

Identifiers

PMID25419715
PMCPMC4242679
OpenAlexW2019184963

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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.