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ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors
Author(s): Ohtsu H, Dempsey PJ, Eguchi S
Source: AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY    Volume: 291    Issue: 1    Pages: C1-C10    Published: JUL 2006  
Times Cited: 69     References: 119     
Abstract: A disintegrin and metalloprotease (ADAM) is a membrane-anchored metalloprotease implicated in the ectodomain shedding of cell surface proteins, including the ligands for epidermal growth factor (EGF) receptors (EGFR)/ErbB. It has been well documented that the transactivation of the EGFR plays critical roles for many cellular functions, such as proliferation and migration mediated through multiple G protein-coupled receptors (GPCRs). Recent accumulating evidence has suggested that ADAMs are the key metalloproteases activated by several GPCR agonists to produce a mature EGFR ligand leading to the EGFR transactivation. In this review, we describe the current knowledge on ADAMs implicated in mediating EGFR transactivation. The major focus of the review will be on the possible upstream mechanisms of ADAM activation by GPCRs as well as downstream signal transduction and the pathophysiological significances of ADAM-dependent EGFR transactivation.
Document Type: Review
Language: English
Reprint Address: Eguchi, S (reprint author), Temple Univ, Sch Med, Cardiovasc Res Ctr, 3420 N Broad St, Philadelphia, PA 19140 USA
Addresses:
1. Temple Univ, Sch Med, Cardiovasc Res Ctr, Philadelphia, PA 19140 USA
2. Temple Univ, Sch Med, Dept Physiol, Philadelphia, PA 19140 USA
3. Univ Washington, Pacific NW Res Inst, Seattle, WA 98195 USA
4. Univ Washington, Dept Med, Seattle, WA 98195 USA
Publisher: AMER PHYSIOLOGICAL SOC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
Subject Category: Cell Biology; Physiology
IDS Number: 053EI
ISSN: 0363-6143
DOI: 10.1152/ajpcell.00620.2005
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