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Dual intracellular signaling by proteolytic cleavage of membrane-anchored heparin-binding EGF-like growth factor.
Cytokine & Growth Factor Reviews ( IF 13.0 ) Pub Date : 2004-01-30 , DOI: 10.1016/j.cytogfr.2003.10.002
Daisuke Nanba 1 , Shigeki Higashiyama
Affiliation  

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.

中文翻译:

通过蛋白水解裂解膜锚定的肝素结合EGF样生长因子的双重细胞内信号转导。

肝素结合型EGF样生长因子(HB-EGF)是EGF家族的一员,被合成为膜锚定的前体(proHB-EGF),被特定的金属蛋白酶裂解释放可溶的HB-EGF。proHB-EGF的蛋白水解裂解产生氨基和羧基末端片段(HB-EGF和HB-EGF-C)。最近的研究表明,proHB-EGF的加工受到严格调节,并参与多种生物学过程,不仅HB-EGF,而且HB-EGF-C都起信号分子的作用。ProHB-EGF通过蛋白水解裂解产生双重细胞内信号分子。
更新日期:2019-11-01
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