Evidence map›Paper›PMID 26840447›Full record

ArticleCell proliferation2016

Inhibition of cell proliferation, migration and invasion by a glioma-targeted fusion protein combining the p53 C terminus and MDM2-binding domain.

Jiawen Yu, Meihua Guo, Ting Wang, Xiang Li, Dan Wang, Xinying Wang, Qian Zhang, Liang Wang, Yang Zhang, Chunhui Zhao and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell proliferation, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 27% 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

8 citing papers in PubMed, 12 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

11 authors at 2 institutions in 1 country.

Jiawen YuDepartment of Biotechnology, Dalian Medical University, Dalian, 116044, China.
Meihua GuoDepartment of Biotechnology, Dalian Medical University, Dalian, 116044, China.
Ting WangDepartment of Biotechnology, Dalian Medical University, Dalian, 116044, China.
Xiang LiDepartment of Biotechnology, Dalian Medical University, Dalian, 116044, China.
Dan WangDepartment of Biotechnology, Dalian Medical University, Dalian, 116044, China.
Xinying WangDepartment of Biotechnology, Dalian Medical University, Dalian, 116044, China.
Qian ZhangDepartment of Biotechnology, Dalian Medical University, Dalian, 116044, China.
Liang WangDepartment of Biotechnology, Dalian Medical University, Dalian, 116044, China.
Yang ZhangDepartment of Biotechnology, Dalian Medical University, Dalian, 116044, China.
Chunhui ZhaoCollege of Life Sciences, Liaoning Normal University, Dalian, 116029, China.
Bin FengDepartment of Biotechnology, Dalian Medical University, Dalian, 116044, China.
Dalian Medical University · CNLiaoning Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectivesThe aim of this study was to develop multifunctional fusion proteins for targeting and delivering therapy elements into glioma cells. MATERIALS AND

methodsMultifunctional fusion proteins were expressed in Escherichia coli and purified using Ni-NTA resin affinity chromatography. Human glioma cells and primary astrocytes were used to analyse their functions. Targeting proteins location to glioma cells was observed by confocal microscopy. Effects of cell viability and proliferation were evaluated using the Cell Counting Kit 8 and colony formation assays. Glioma cell migration and invasion were assessed using transwell assays, and apoptosis was analysed by flow cytometry. In addition, changes in expression of proteins related to the cell cycle and apoptosis were determined by Western blotting.

resultsThe protein with highest bioactivity was GL1-riHA2-p53c+m-TAT (GHPc+mT), which combines glioma-targeting peptide GL1 (G), and C terminus (Pc) and mouse double minute domains (Pm) of p53, with the destabilizing lipid membrane peptide riHA2 (H) and cell-penetrating peptide TAT (T). The purified fusion protein was stable in cell culture medium and specifically targeted, and was internalized by, epidermal growth factor receptor (EGFR)-overexpressing glioma cells (U87ΔEGFR). It inhibited cell proliferation, migration and invasion, while flow cytometric analysis showed increased apoptosis. In addition, GHPc+mT caused significant changes in expression of proteins related to the cell cycle and apoptosis.

conclusionGHPc+mT is a multifunctional protein combining targeting, inhibition of glioma cell proliferation and induction of apoptosis, providing some potential to be developed into an effective protein drug delivery system for glioma therapy.

Indexed as

ApoptosisCell CycleCell Line, TumorCell MovementCell ProliferationGliomaHumansNeoplasm InvasivenessProtein BindingProtein Structure, TertiaryRecombinant Fusion ProteinsTumor Stem Cell AssayTumor Suppressor Protein p53Recombinant Fusion ProteinsTumor Suppressor Protein p53

Identifiers

PMID26840447
PMCPMC6496415
OpenAlexW2287956177

What OpenQuestion holds

Textmetadata
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.