Am J Physiol Cell Physiol AJP: Gastrointestinal and Liver Physiology
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Am J Physiol Cell Physiol 291: C1-C10, 2006; doi:10.1152/ajpcell.00620.2005
0363-6143/06 $8.00
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INVITED REVIEW

ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors

Haruhiko Ohtsu,1 Peter J. Dempsey,2 and Satoru Eguchi1

1Cardiovascular Research Center and Department of Physiology, Temple University School of Medicine, Philadelphia, Pennsylvania; and 2Pacific Northwest Research Institute, and Department of Medicine, University of Washington, Seattle, Washington

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.

ectodomain shedding; angiotensin II


Address for reprint requests and other correspondence: S. Eguchi, Cardiovascular Research Center, Temple Univ. School of Medicine, 3420 N. Broad St., Philadelphia, PA 19140 (e-mail: seguchi{at}temple.edu)




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