2004年2月
Dual intracellular signaling by proteolytic cleavage of membrane-anchored heparin-binding EGF-like growth factor
CYTOKINE & GROWTH FACTOR REVIEWS
- ,
- 巻
- 15
- 号
- 1
- 開始ページ
- 13
- 終了ページ
- 19
- 記述言語
- 英語
- 掲載種別
- 書評論文,書評,文献紹介等
- DOI
- 10.1016/j.cyotogfr.2003.10.002
- 出版者・発行元
- ELSEVIER SCI LTD
Heparin-binding EGF-like growth factor (HB-EGF), a member of the EGF family, is synthesized as a membrane-anchored precursor (proHB-EGF) that is cleaved to release a soluble HB-EGF by specific metalloproteases. Proteolytic cleavage of proHB-EGF yields amino- and carboxy-terminal fragments (HB-EGF and HB-EGF-C). Recent studies indicate that the processing of proHB-EGF is strictly regulated and involved in a variety of biological processes and that not only HB-EGF but also HB-EGF-C functions as a signaling molecule. ProHB-EGF generates dual intracellular signaling molecules by its proteolytic cleavage. (C) 2003 Elsevier Ltd. All rights reserved.
- リンク情報
- ID情報
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- DOI : 10.1016/j.cyotogfr.2003.10.002
- ISSN : 1359-6101
- PubMed ID : 14746810
- Web of Science ID : WOS:000220870300002