Evidence map›Paper›PMID 29950929›Full record

ArticleProteome science2018

iTRAQ-Based Proteomic Analysis reveals possible target-related proteins and signal networks in human osteoblasts overexpressing FGFR2.

Tianyi Cai, Baojin Wu, Xinjie Tang, Zhaoping Zhou, Junyi Yang, Ronghu Ke, Xiongzheng Mu

Open access · goldAbstract read
In one paragraph

Article in Proteome science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

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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

4 citing papers in PubMed, 7 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

7 authors at 2 institutions in 1 country.

Tianyi Cai *Department of Plastic and Reconstructive Surgery, Huashan Hospital, Fudan University School of Medicine, No. 12, Wu Lu Mu Qi Road (M), Shanghai, 200040 China.
Baojin Wu *Department of Plastic and Reconstructive Surgery, Huashan Hospital, Fudan University School of Medicine, No. 12, Wu Lu Mu Qi Road (M), Shanghai, 200040 China.
Xinjie TangDepartment of Plastic and Reconstructive Surgery, Huashan Hospital, Fudan University School of Medicine, No. 12, Wu Lu Mu Qi Road (M), Shanghai, 200040 China.
Zhaoping ZhouDepartment of Plastic and Reconstructive Surgery, Huashan Hospital, Fudan University School of Medicine, No. 12, Wu Lu Mu Qi Road (M), Shanghai, 200040 China.
Junyi YangDepartment of Plastic and Reconstructive Surgery, Huashan Hospital, Fudan University School of Medicine, No. 12, Wu Lu Mu Qi Road (M), Shanghai, 200040 China.
Ronghu KeDepartment of Plastic and Reconstructive Surgery, Huashan Hospital, Fudan University School of Medicine, No. 12, Wu Lu Mu Qi Road (M), Shanghai, 200040 China.
Xiongzheng MuDepartment of Plastic and Reconstructive Surgery, Huashan Hospital, Fudan University School of Medicine, No. 12, Wu Lu Mu Qi Road (M), Shanghai, 200040 China.
Fudan University · CNHuashan Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundFibroblast growth factor receptor 2 (FGFR2) play a vital role in skeletogenesis. However, the molecular mechanisms triggered by FGFR2 in osteoblasts are still not fully understood. In this study, proteomics and bioinformatics analysis were performed to investigate changes in the protein profiles regulated by FGFR2, with the goal of characterizing the molecular mechanisms of FGFR2 function in osteoblasts.

methodsIn this study, FGFR2-overexpression cell line was established using the lentivirus-packaging vector in human osteoblasts (hFOB1.19). Next, the isobaric tags for relative and absolute quantitation (iTRAQ) in combination with the liquid chromatography-tandem mass spectrometry (LC-MS/MS) method was used to compare the proteomic changes between control and FGFR2-overexpression cells. Thresholds (fold-change of ≥ 1.5 and a

resultsA Total of 149 DEPs was identified. The DEPs mainly located within organelles and involved in protein binding and extracellular regulation of signal transduction. ColI, TNC, FN1 and CDKN1A were strikingly downregulated while UBE2E3, ADNP2 and HSP70 were significantly upregulated in FGFR2-overexpression cells. KEEG analysis suggested the key pathways included cell death, PI3K-Akt signaling, focal adhesion and cell cycle.

conclusionsTo our knowledge, this is the first protomic research to investigate alterations in protein levels and affected pathways in FGFR2-overexpression osteoblasts. Thus, this study not only provides a comprehensive dataset on overall protein changes regulated by FGFR2, but also shed light on its potential molecular mechanism in human osteoblasts.

Indexed as

FGFR2 osteoblastiTRAQ

Identifiers

PMID29950929
PMCPMC6011184
OpenAlexW2808953203

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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.