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MGF Igf-1-ec

IGF-1Ec, IGF-1Eb, Mechano-Growth Factor

Quick Stats
Studies 62
Trials 100
Score 2
2013 pubmed 23 citations

Mechano-growth factor induces migration of rat mesenchymal stem cells by altering its mechanical properties and activating ERK pathway.

Wu. Jiamin J; Wu. Kewen K; Lin. Feng F; Luo. Qing Q; Yang. Li L; Shi. Yisong Y; Song. Guanbin G; Sung. Kuo-Li Paul KL

Key Findings

  • MGF boosts rat mesenchymal stem cell migration in a dose‑dependent way, with 50 ng/mL being optimal
  • MGF increases cell traction force and stiffness, mechanical traits linked to movement
  • MGF activates the ERK signalling pathway; blocking ERK stops the migration effect

Practical Outcomes

  • For now there’s no direct human protocol—this is early‑stage lab data. It suggests that MGF could potentially aid tissue repair by enhancing stem‑cell mobility via mechanical and ERK mechanisms, but safety, dosing, and effectiveness in humans remain untested.

Summary

The study shows that a protein called mechano‑growth factor (MGF) can make rat stem cells move more by making them stiffer and pulling harder, and it does this by turning on a cell‑signalling pathway called ERK. The effect was strongest at a lab dose of 50 ng/mL, but the work was done in petri dishes, not people.

Abstract

Mechano-growth factor (MGF) generated by cells in response to mechanical stimulation has been identified as a mechano effector molecule, playing a key role in regulating mesenchymal stem cell (MSC) function, including proliferation and migration. However, the mechanism(s) underlying how MGF-induced MSC migration occurs is still unclear. In the present study, MGF motivated migration of rat MSCs (rMSCs) in a concentration-dependent manner and optimal concentration of MGF at 50 ng/mL (defined as MGF treatment in this paper) was demonstrated. Notably, enhancement of mechanical properties that is pertinent to cell migration, such as cell traction force and cell stiffness were found to respond to MGF treatment. Furthermore, MGF increased phosphorylation of extracellular signal-regulated kinase (ERK), ERK inhibitor (i.e., PD98059) suppressed ERK phosphorylation, and abolished MGF-induced rMSC migration were found, demonstrating that ERK is involved molecule for MGF-induced rMSC migration. These in vitro evidences of MGF-induced rMSC migration and its direct link to altering rMSC mechanics and activating the ERK pathway, uncover the underlying biomechanical and biological mechanisms of MGF-induced rMSC migration, which may help find MGF-based application of MSC in clinical therapeutics.

Study Information

Provider

pubmed

Year

2013

Date

2013-10-16T00:00:00.000Z

DOI

10.1016/j.bbrc.2013.10.031

Citations

23

References

24