@misc{oai:repo.qst.go.jp:00064881,
 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 = {Dec},
 note = {Although FGF11 subfamily members (FGF11-14) have structural similarity with FGF1, a significant structural difference between FGF11-14 and FGF1 is the C-terminal sequence because FGF11-14 possess unique C-terminal polypeptides. We identified novel cell-penetrating peptide domains (CPPC11-14) from the C-terminal region of FGF11-14 proteins, which could readily deliver FGF11-14 into cells independently of FGF receptors (FGFRs). This study evaluated and compared the protective activity of FGF1/CPPC fusion proteins (FGF1/CPPC11-14) and FGF1 against radiation damage. The in vitro mitogenic activity of FGF1/CPPC12 was examined by a cell growth assay using a BaF3 transfectant cell line expressing the FGFR1c subtype (BaF3-FGFR1c). FGF1/CPPC12 was less potent than FGF1 for mitogenic activity through FGFR1c regardless of whether heparin was added or not. In contrast, FGF1/CPPC12 significantly reduced radiation-induced apoptosis in the rat intestinal epithelial cell line IEC6 in the presence of heparin. The protective activity of FGF1/CPPC12 against radiation-induced intestinal injuries was evaluated in BALB/c mice. As a result, FGF1/CPPC12 significantly enhanced crypt survival compared with FGF1 even in the absence of heparin and FGF1/CPPC12-treatment significantly increased BrdU incorporation into the crypts and the depth of the crypts more than FGF1. These findings indicate that FGF1/CPPC fusion proteins strongly protect the jejunum against radiation-induced injury and suggest that cellular internalization of FGF1/CPPC11-14 is involved in their activities independently of FGFRs., The 35th Annual Meeting of the Molecular Biology Society of Japan},
 title = {Radioprotective effects of FGF1/CPPC fusion proteins},
 year = {2012}
}