@misc{oai:repo.qst.go.jp:00071094,
 author = {Nakayama, Fumiaki and Umeda, Sachiko and Yasuda, Takeshi and Asada, Masahiro and Imamura, Toru and Imai, Takashi and 中山 文明 and 梅田 禎子 and 安田 武嗣 and 今井 高志},
 month = {May},
 note = {Signals for FGF1 functions come from not only activated FGF receptors (FGFR) but also internalized FGF1. Although FGF11 subfamily members (FGF11-14) have structural similarity with FGF1, FGF11-14 possess unique C-terminal polypeptides. Novel cell-penetrating peptide domains (CPPC11-14) were identified from the C-terminal region of FGF11-14 proteins, which could readily deliver FGFs into cells independently of FGFRs. In this study, we created FGF1/CPPC fusion proteins (FGF1/CPPC11-14) following the alignment of FGF12 C-terminal region and evaluated the protective activity of FGF1/CPPC11-14 against radiation damage. FGF1/CPPC11-14 fusion proteins were internalized into the rat intestinal epithelial cell line IEC6 more efficiently than FGF1. However, the mitogenic activity of FGF1/CPPC12 through FGFR1c was less than that of FGF1. In contrast, FGF1/CPPC11-14 significantly reduced radiation-induced apoptosis in IEC6 cells in the presence of heparin, and the administration of FGF1/CPPC11-14 to BALB/c mice without heparin reduced the induction of apoptosis in hair bulbs 24 hafter irradiation. In addition, pre-treatment with FGF1/CPPC11-14 maintained K15 positive stem cells in the bulge after irradiation, although K15 positive stem cells decreased in anagen hair follicles after irradiation.
These findings indicate that FGF1/CPPC fusion proteins protect the hair follicles against radiation-induced injury and suggest that cellular internalization of FGF1/CPPC11-14 is involved in their activities independently of FGFRs., International Investigative Dermatology EDINBURGH 2013},
 title = {Enhanced cellular internalization of FGF1/CPPC fusion protein promoted its radioprotective effect in the hair follicles.},
 year = {2013}
}