Identification and characterization of surrogate peptide ligand for orphan G protein-coupled receptor mas using phage-displayed peptide library
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AbstractIn the present study, a phage-displayed random peptide library was used to identify surrogate peptide ligands for orphan GPCR mas. Sequence analysis of the isolated phage clones indicated a selective enrichment of some peptide sequences. Moreover, multiple alignments of the isolated phage clones gave two conserved peptide motifs from which we synthesized peptide MBP7 for further evaluation. Characterization of the representative phage clones and the synthetic peptide MBP7 by immunocytochemistry revealed a strong punctate cell surface staining in CHO cells expressing mas-GFP fusion protein. The isolated phage clones and synthetic peptide MBP7 induced mas internalization in a stable CHO cell clone (MCOM80) over-expressing mas. In addition, MBP7-stimulated phospholipase C activity and intracellular calcium mobilization in these same cells. in summary, we have demonstrated a systematic approach to derive surrogate peptide ligands for orphan GPCRs. With this technique, we have identified two conserved peptide motifs which allow us to identify potential protein partners for mas, and have generated a peptide agonist MBP7 which will be invaluable for functional characterization of the mas oncogene. (c) 2005 Elsevier Inc. All rights reserved.
All Author(s) ListBikkavilli RK, Tsang SY, Tang WM, Sun JX, Ngai SM, Lee SST, Ko WH, Wise H, Cheung WT
Journal nameBiochemical Pharmacology
Year2006
Month1
Day12
Volume Number71
Issue Number3
PublisherPERGAMON-ELSEVIER SCIENCE LTD
Pages319 - 337
ISSN0006-2952
eISSN1873-2968
LanguagesEnglish-United Kingdom
Keywordsangiotensin; GPCR; mas; oncogene; peptide library; phage display
Web of Science Subject CategoriesPharmacology & Pharmacy; PHARMACOLOGY & PHARMACY

Last updated on 2020-13-09 at 01:21