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Fibroblast Growth Factor-12(FGF12) Translocation into Intestinal Epithelial Cells is Dependent on a Novel Cell-Penetrating Peptide Domain: Involvement of Internalization in the in Vivo Role of Exogenous FGF12
https://repo.qst.go.jp/records/48382
https://repo.qst.go.jp/records/48382664292c0-b401-4939-8274-7b22f8a03f7c
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2017-11-22 | |||||
| タイトル | ||||||
| タイトル | Fibroblast Growth Factor-12(FGF12) Translocation into Intestinal Epithelial Cells is Dependent on a Novel Cell-Penetrating Peptide Domain: Involvement of Internalization in the in Vivo Role of Exogenous FGF12 | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | journal article | |||||
| アクセス権 | ||||||
| アクセス権 | metadata only access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
| 著者 |
Nakayama, Fumiaki
× Nakayama, Fumiaki× Yasuda, Takeshi× Umeda, Sachiko× Asada, Masahiro× Imamura, Toru× Meineke, Viktor× Akashi, Makoto× 中山 文明× 安田 武嗣× 梅田 禎子× 明石 真言 |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | The extracellular effect of fibroblast growth factor-12 (FGF12) remains unknown because FGF12 cannot activate any fibroblast growth factor receptors (FGFRs), and FGF12 is not currently thought to be released from cells. We reported previously that FGF12 plays an intracellular role in the inhibition of radiation-induced apoptosis. In this study, we demonstrated that recombinant FGF12 was able to be internalized into the cytoplasm of a rat intestinal epithelial cell line, IEC6, and this process was dependent on two novel cell-penetrating peptide (CPP) domains (CPP-M and CPP-C). In particular, CPP-C, composed of approximately 10 amino acids, was identified as a specific domain of FGF12 and its subfamily in the C-terminal region (residues 140-149), although CPP-M was a common domain in the internal region of the FGF family. The absence of CPP-C from FGF12 or a mutation (E142L) in the CPP-C domain drastically reduced the internalization of FGF12 into cells. Therefore, CPP-C played an essential role in the internalization of FGF12. In addition, CPP-C was able to deliver other polypeptides into cells as a CPP because an FGF1/CPP-C chimeric protein was internalized into IEC6 cells more efficiently than wild-type FGF1. Finally, intraperitoneally added FGF12 inhibited radiation-induced apoptosis in the intestinal epithelial cells of BALB/c mice, and deletion of the CPP-C domain decreased the inhibition of the apoptosis. These findings suggest that exogenous FGF12 can play a role in tissues by translocating into cells through the plasma membrane, and the availability of this novel CPP provides a new tool for the intracellular delivery of bioactive molecules. | |||||
| 書誌情報 |
The Journal of Biological Chemistry 巻 286, 号 29, p. 25823-25834, 発行日 2011-04 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0021-9258 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1074/jbc.m110.198267 | |||||
