HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Moriguchi, T. Articles by Akiyama, T. Search for Related Content PubMed PubMed Citation Articles by Moriguchi, T. Articles by Akiyama, T.

¹ Laboratory of Molecular and Genetic Information, and ³ Laboratory of Molecular Regulation, Institute for Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
² Department of Oncogene Research, Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan
⁴ PharmaDesign Inc., 4-2-10 Hacchoubori, Chuou-ku, Tokyo 104-0032, Japan

We have identified and characterized a novel member of the G protein-coupled receptor (GPCR) family, termed DREG. DREG belongs to the LNB-TM7 subfamily and possesses a long amino-terminus that contains a CUB domain, a PTX domain, a hormone binding domain and a GPCR proteolytic site (GPS) domain. RT-PCR experiments and whole mount in situ hybridization in mice showed that DREG is expressed at high levels in the heart and somite during embryogenesis and in the adult lung. When DREG was transiently expressed in mammalian cultured cells, a 35-kD fragment was generated by endogenous proteolytic processing at the conserved GPS domain. This short fragment was found associated with the cell membrane, typical of GPCRs. DREG was further cleaved in the middle of the extracellular domain, generating a soluble 70-kD fragment containing the CUB and PTX domains. This processing was inhibited by an inhibitor of the endoprotease furin but not of matrix metalloproteinases. These results raise the possibility that DREG plays a role in development, not only as a receptor or an adhesion molecule but also as a secreted ligand.

^aPresent address: Department of Molecular Cell Biology, Medical Research Institute, Tokyo Medical and Dental University, and Center of Excellence Program for Frontier Research on Molecular Destruction and Reconstruction of Tooth and Bone, Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062, Japan.

^* Correspondence: E-mail: akiyama{at}iam.u-tokyo.ac.jp

This article has been cited by other articles:

				K. R. Monk, S. G. Naylor, T. D. Glenn, S. Mercurio, J. R. Perlin, C. Dominguez, C. B. Moens, and W. S. Talbot A G Protein-Coupled Receptor Is Essential for Schwann Cells to Initiate Myelination Science, September 11, 2009; 325(5946): 1402 - 1405. [Abstract] [Full Text] [PDF]