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22대 대한민국 국회 국회정보길라잡이 국회의원검색
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Title Page

ABSTRACT

Contents

INTRODUCTION 10

RESULTS 12

Discovery of an bFGF-derived agonist peptide 12

F3 showed the most outstanding wound-healing effect among several candidate peptides. 12

F3 specifically induces phosphorylation of FGFR and acts full agonist 14

F3 activates downstream signaling proteins related to cell proliferation and mediates fibroblast migration 15

F3 shows potent wound healing effect 15

DISCUSSION 24

MATERIALS & METHOD 26

Cell culture 26

Computational design of peptides 26

Cell viability analysis 27

Cell proliferation analysis 27

Western blot analysis 27

Scratch wound assay 28

Surface Plasmon Resonance (SPR) 28

Reference 30

List of Figures

Figure 1. Feature of FGFR agonist peptide. 17

Figure 2. Screening of FGFR agonist peptide. 18

Figure 3. The F3 peptide specifically activates FGFR and induces phosphorylation. 20

Figure 4. Measurement of wound healing efficiency of the F3 peptide. 21

Figure 5. The use of specific inhibitor showed that F3 interact with FGFR. 23

초록보기

 Fibroblast growth factors (FGFs) are a large family of growth factors and cell-signaling proteins that act through tyrosine kinase receptors known as FGF receptors (FGFRs). bFGF, also known as basic FGF, regulates diverse functions such as cell development, repair, and metabolism. bFGF upon binding with FGFR, phosphorylates tyrosine residues of FGFR by bFGF, activates the phospholipase C gamma, phosphatidylinositol-4,5-bisphosphate 3-kinase/protein kinase B, and mitogen-activated protein kinase pathways to induce the release of cytokines. These cytokines trigger cell proliferation, differentiation, and migration. In this study, we designed three bFGF agonistic peptides and their agonistic effect was checked in comparison to bFGF. Among the three designed peptides, F3 peptide showed the best activity. F3 induced cell proliferation in a similar fashion to bFGF. Treatment of human breast cancer cells with F3 resulted in the phosphorylation of FGFR. When F3 was co-treated with bFGF, bFGF didn't decrease the phosphorylation level of FGFR, which confirmed the F3 peptide is full agonist of bFGF. F3 also activated the downstream signaling proteins including mitogen activated protein kinases. In the in-vitro wound healing assay, F3 demonstrated wound healing effect which was inhibited when F3 was co-treated with Erdafitinib, which shows that F3 specifically activates FGFR. Through surface plasmon resonance analysis it was confirmed that F3 binds specifically with FGFR in a concentration dependent manner. In conclusion, F3 is functional agonist specific to FGFR and seems to have therapeutic effects in wound healing.

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