Evidence map›Paper›PMID 25550780›Full record

ArticleInternational journal of clinical and experimental pathology2014

The role of integrin-β/FAK in cyclic mechanical stimulation in MG-63 cells.

Min Yang, Li-Wei Xiao, Er-Yuan Liao, Qiao-Jing Wang, Bei-Bei Wang, Jia-Xuan Lei

Open access · greenAbstract read
In one paragraph

Article in International journal of clinical and experimental pathology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Biomechanical Aspects in Bone Tumor Engineering.Tissue engineering. Part B, Reviews · 2024
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  14. IGF-binding protein 2 is a candidate target of therapeutic potential in cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
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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

6 authors at 1 institution in 1 country.

Min YangInstitute of Endocrinology and Metabolism, The Second Xiangya Hospital, Central South University Changsha, P. R. China ; Department of Internal Medicine, Affiliated Hospital of National Research for Rehabilitation Technical Aids Beijing, P. R. China.
Li-Wei XiaoMedical Center of Stomatology, The Second Xiangya Hospital, Central South University Changsha, P. R. China.
Er-Yuan LiaoInstitute of Endocrinology and Metabolism, The Second Xiangya Hospital, Central South University Changsha, P. R. China.
Qiao-Jing WangMedical Center of Stomatology, The Second Xiangya Hospital, Central South University Changsha, P. R. China.
Bei-Bei WangMedical Center of Stomatology, The Second Xiangya Hospital, Central South University Changsha, P. R. China.
Jia-Xuan LeiMedical Center of Stomatology, The Second Xiangya Hospital, Central South University Changsha, P. R. China.
Central South University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectiveThis study aims to explore the function of Integrin-β/FAK in the mechanical signal transduction and the connection with downstream ERK signal pathways.

methodsHuman osteosarcoma MG63 cell lines were used in this study. The effects of mechanical strain on the Integrin-β₁ expression, FAK and ERK signal pathway in Human osteosarcoma MG63 cells were detected using RT-PCR and Western-blotting methods. The localization of FAK in Human osteosarcoma MG63 cells were determined using immunofluorescent method. The interaction between Integrin-β₁ and FAK were detected by using co-immunoprecipitation method.

resultsThe expression of Integrin-β₁ shows a notable bimodel distribution, mechanical strain stimulation can promote Integrin-β₁ expression and the phosphorylation of FAK and ERK, mechanical strain activated FAK and ERK mediated by Integrin-β₁.

conclusionIntegrin-β₁ may play an important role in osteoblast proliferation differentiation process, it might feel external strain stimulation through ECM composition and makes FAK phosphated through the interaction with FAK, thus causing a series of activation of signal molecules. Finally it reduces MAPK (ERK) activation and cellular responses to finish mechanical signal transduction.

Indexed as

MAP Kinase Signaling SystemCell DifferentiationCell Line, TumorCell ProliferationFocal Adhesion Kinase 1HumansIntegrin beta1PhosphorylationFocal Adhesion Kinase 1Integrin beta1PTK2 protein, humanERK signal pathwayfocal adhesion kinase (FAK)human osteosarcoma MG63 cellsIntegrin-βmechanical stimulation

Identifiers

PMID25550780
PMCPMC4270589
OpenAlexW1691622795

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.