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

Daisuke Nanba; Shigeki Higashiyama

doi:10.1016/j.cytogfr.2003.10.002

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

Cytokine Growth Factor Rev. 2004 Feb;15(1):13-9. doi: 10.1016/j.cytogfr.2003.10.002.

Authors

Daisuke Nanba¹, Shigeki Higashiyama

Affiliation

¹ Department of Medical Biochemistry, Ehime University School of Medicine, Shitsukawa, Shigenobu-cho, Onsen-gun, Ehime 791-0295, Japan.

PMID: 14746810
DOI: 10.1016/j.cytogfr.2003.10.002

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.

Publication types

Review

MeSH terms

Animals
Cardiomegaly
Cell Membrane / metabolism*
Cytoplasm / pathology
Epidermal Growth Factor / chemistry
Epidermal Growth Factor / physiology*
Heparin / metabolism*
Heparin-binding EGF-like Growth Factor
Humans
Intercellular Signaling Peptides and Proteins
Models, Biological
Myocardium / pathology
Protein Structure, Tertiary
Signal Transduction*
Submandibular Gland / physiology
Wound Healing

Substances

HBEGF protein, human
Heparin-binding EGF-like Growth Factor
Intercellular Signaling Peptides and Proteins
Epidermal Growth Factor
Heparin