Dual intracellular signaling by proteolytic cleavage of membrane-anchored heparin-binding EGF-like growth factor.

Abstract:

: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.

authors

Nanba D,Higashiyama S

doi

10.1016/j.cytogfr.2003.10.002

subject

Has Abstract

pub_date

2004-02-01 00:00:00

pages

13-9

issue

1

eissn

1359-6101

issn

1879-0305

pii

S1359610103000984

journal_volume

15

pub_type

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