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RGD-containing elastin-like polypeptide enhances β-cell proliferation by regulating the phosphorylation of Akt and Erk, and the levels of cyclin D1 and cyclinD2.

Title
RGD-containing elastin-like polypeptide enhances β-cell proliferation by regulating the phosphorylation of Akt and Erk, and the levels of cyclin D1 and cyclinD2.
Authors
Lee, Kyeong-MinHwang, Yeo-JinJeon, Wonbae
DGIST Authors
Lee, Kyeong-Min; Hwang, Yeo-Jin; Jeon, Wonbae
Issue Date
2019-08-02
Citation
2019 Asia Islet Biology and Incretin Symposium
Type
Conference
Abstract
Background: Proliferation of beta cell plays important role in the maintenance of beta cell mass and function. Extracellular matrix (ECM) components increase the adhesion and proliferation of beta cells. In this study, we investigated whether RGD-modified elastin-like polypeptide (REP), as a bioactive matrix, could enhance the adhesion and proliferation of beta cells and we elucidate signaling pathways involved. Methods: The RIN-m rat insulinoma cell line was cultured at 5% CO2-95% air at 37 °C in RPMI1640 medium. RIN-m cells were cultured on the surfaces coated with REP, fibronectin (FN), or laminin (LN). Cell adhesion and proliferation assay were performed. Quantitative real time PCR and western blot analysis were exploited to determine the mRNA and protein levels of insulin, PDX-1 and BETA. To measure the phosphorylation of Akt and Erk, and the levels of cyclin D1 and cyclin D2, we performed the western blot analysis. Results: When RIN-m cells cultured on REP, cell adhesion was increased in a concentration-dependent manner. Cell adhesion was also increased on another extracellular matrix, FN and LN. Moreover, cell proliferation was enhanced by culturing on REP, FN or LN. Beta-cell proliferation is regulated by cell cycle protein, protein kinases, or inhibitors. The levels of Cyclin D1 and Cyclin D2 was increased by REP while the expression of p27 was decreased. The mRNA levels of insulin, PDX-1 and BETA2 were increased by culturing on REP. The protein expression of PDX-1 and BETA2 also was increased on REP. The phosphorylation of both Akt and Erk was significantly up-regulated by the presence of REP and ECM proteins. To investigate whether PI3K/Akt and Erk pathways are involved in the up-regulation of cell adhesion and proliferation on REP, we treated with wortmannin and PD98059, the specific inhibitors of PI3kinase and Erk kinase. Blocking PI 3-kinase and Erk activities significantly decreased the cell adhesion and proliferation on REP. Conclusion: The results demonstrates that the up-regulation of PI3K/Akt and Erk signaling pathway and the regulation of cell cycle proteins by REP would be an effective strategy for improving the adhesion and proliferation of pancreatic beta cell.
URI
http://hdl.handle.net/20.500.11750/14352
Publisher
Asia Islet Biology and Incretin Research Association
Related Researcher
Files:
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Collection:
Division of Biotechnology2. Conference Papers


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