Abstract
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
Protein & Peptide Letters
Title: Metalloproteinase-Mediated Shedding of Heparin-Binding Egf-Like Growth Factor and Its Pathophysiological Roles
Volume: 11 Issue: 5
Author(s): Shigeki Higashiyama
Affiliation:
Keywords: hb-egf, adam12, metalloproteinase, ectodomain shedding, gpcr, egfr transactivation, wound healing, cardiac hypertrophy
Abstract: 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.
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Cite this article as:
Higashiyama Shigeki, Metalloproteinase-Mediated Shedding of Heparin-Binding Egf-Like Growth Factor and Its Pathophysiological Roles, Protein & Peptide Letters 2004; 11 (5) . https://dx.doi.org/10.2174/0929866043406562
DOI https://dx.doi.org/10.2174/0929866043406562 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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