Protein tyrosine phosphatase 1B regulates migration of ARPE-19 cells through EGFR/ERK signaling pathway

AIM: To evaluate whether protein tyrosine phosphatase1B(PTP1B) contributed to initiate human retinal pigment epithelium cells(ARPE)-19 migration and investigate the signaling pathways involved in this process.·METHODS: ARPE-19 cells were cultured and treated with the si RNA-PTP1 B. Expression of PTP1 B was confirmed by quantitative reverse transcriptase-polymerase chain reaction(q RT-PCR). AG1478 [a selective inhibitor of epidermal growth factor receptor(EGFR)] and PD98059(a specific inhibitor of the activation of mitogen-activated protein kinase) were used to help to determine the PTP1 B signaling mechanism.Western blot analysis verified expression of EGFR and extracellular signal-regulated kinase(ERK) in ARPE-19 cells. The effect of si RNA-PTP1 B on cell differentiation was confirmed by immunostaining for α-smooth muscle actin(α-SMA) and q RT-PCR. Cell migration ability was analyzed by transwell chamber assay.·RESULTS: The m RNA levels of PTP1 B were reduced by si RNA-PTP1 B as determined by q RT-PCR assay.Si RNA-PTP1 B activated EGFR and ERK phosphorylation.α-SMA staining and q RT-PCR assay demonstrated that si RNA-PTP1 B induced retinal pigment epithelium(RPE)cells to differentiate toward better contractility and motility. Transwell chamber assay proved that PTP1 B inhibition improved migration activity of RPE cells.Treatment with AG1478 and PD98059 abolished si RNA-PTP1B-induced activation of EGFR and ERK, α-SMA expression and cell migration.·CONCLUSION: PTP1 B inhibition promoted myofibroblast differentiation and migration of ARPE-19 cells, and EGFR/ERK signaling pathway played important role in migration process.