Metalloproteinase-Mediated Shedding of Heparin-Binding Egf-Like Growth Factor and Its Pathophysiological Roles

Author(s): Shigeki Higashiyama

Journal Name: Protein & Peptide Letters

Volume 11 , Issue 5 , 2004

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Heparin-binding EGF-like growth factor (HB-EGF) exists as a membrane-anchored form (proHBEGF) and as its soluble cleaved product (sHB-EGF). The conversion (ectodomain shedding) of proHB-EGF to sHB-EGF is tightly regulated by specific metalloproteinases. Ectodomain shedding plays a central role in GPCR-mediated EGFR transactivation. Antagonizing metalloproteinases can inhibit EGFR transactivation and might be of therapeutic value, for example in cardiac hypertrophy, skin remodeling and tumor growth.

Keywords: hb-egf, adam12, metalloproteinase, ectodomain shedding, gpcr, egfr transactivation, wound healing, cardiac hypertrophy

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Article Details

Year: 2004
Page: [443 - 450]
Pages: 8
DOI: 10.2174/0929866043406562
Price: $65

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