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J Recept Signal Transduct Res ; 23(1): 83-97, 2003 Feb.
Article in English | MEDLINE | ID: mdl-12680591

ABSTRACT

Mouse prostacyclin (mIP) receptors transiently expressed in Chinese hamster ovary (CHO) cells activated both adenylyl cyclase and phospholipase C, with a 33-fold preference for signaling through Gs. The prostacyclin (IP) receptor agonists cicaprost, iloprost, carbacyclin, and prostaglandin E1 showed a similar order of potency for activation of both signaling pathways in cells transiently transfected with the mIP and the chimeric prostacyclin/prostaglandin D2 (IPN-VII/DPC and IPN-V/DPVI-C) receptors. Substitution of the carboxyl-terminal tail of the prostacyclin receptor with the corresponding region of the mDP receptor (IPN-VII/DPC) produced a receptor with increased coupling to both Gs and Gq. However, this increased G-protein coupling was lost in the IPN-V/DPVI-C receptor. The observation that both these chimeric receptors can activate phospholipase C indicates that the carboxyl-terminal tail of the IP receptor is not entirely responsible for its ability to couple to Gq. Site-directed mutagenesis studies suggest that isoleucine at position 323 in the IPN-VII/DPC receptor plays an important role in mediating the increased potency of this chimeric receptor.


Subject(s)
Receptors, Epoprostenol/chemistry , Receptors, Epoprostenol/genetics , Receptors, Immunologic , Receptors, Prostaglandin/chemistry , Receptors, Prostaglandin/genetics , Adenylyl Cyclases/metabolism , Amino Acid Sequence , Amino Acid Substitution , Animals , CHO Cells , Cricetinae , Enzyme Activation , Iloprost/metabolism , In Vitro Techniques , Isoleucine/chemistry , Mice , Molecular Sequence Data , Mutagenesis, Site-Directed , Receptors, Epoprostenol/metabolism , Receptors, Prostaglandin/metabolism , Recombinant Fusion Proteins/chemistry , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Signal Transduction , Transfection , Type C Phospholipases/metabolism
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