Document Detail


Agonism with the omega-3 fatty acids alpha-linolenic acid and docosahexaenoic acid mediates phosphorylation of both the short and long isoforms of the human GPR120 receptor.
MedLine Citation:
PMID:  20471368     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The newly discovered G protein-coupled receptor GPR120 has recently been shown to stimulate secretion of the gut hormones glucagon-like peptide-1 and cholecystokinin upon binding of free fatty acids, thrusting it to the forefront of drug discovery efforts for treatment of type 2 diabetes as well as satiety and obesity. Although sequences for two alternative splice variants of the human GPR120 receptor have been reported, there have been no studies which directly compare the signaling of these isoforms. We have identified an additional 16 amino acid gap containing four phospho-labile serine/threonine residues which is localized to the third intracellular loop of the GPR120-long (GPR120-L) isoform. Based on this finding, we hypothesized that the agonist-stimulated phosphorylation profiles of this isoform would be distinct from that of the short isoform (GPR120-S). Using a clonal HEK293 cell model, we examined agonist-mediated phosphorylation of GPR120-S and GPR120-L with the omega-3 fatty acids alpha-linolenic acid (ALA) and docosahexaenoic acid (DHA). Our results show rapid phosphorylation of both isoforms following agonism by either ALA or DHA. Moreover, we show no significant difference in the degree or rate of phosphorylation of both isoforms upon agonism with either ALA or DHA, suggesting that the additional gap in the longer variant is not phosphorylated. Importantly, our results demonstrate that the shorter variant exhibits significantly more pronounced basal phosphorylation in the absence of agonist, suggesting that the additional gap in the long variant may contribute to masking of constitutive phosphorylation sites. These are the first results which demonstrate specific phosphorylation of GPR120 isoforms upon agonism by free fatty acids and the first which distinguish the phosphorylation profiles of the two GPR120 isoforms.
Authors:
Rebecca N Burns; Nader H Moniri
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-05-13
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  396     ISSN:  1090-2104     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2010 Jun 
Date Detail:
Created Date:  2010-06-14     Completed Date:  2010-07-13     Revised Date:  2011-11-03    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1030-5     Citation Subset:  IM    
Copyright Information:
(c) 2010 Elsevier Inc. All rights reserved.
Affiliation:
Department of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, Mercer University, Atlanta, GA 30341, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Cell Line
Docosahexaenoic Acids / pharmacology*
Humans
Molecular Sequence Data
Phosphorylation
Protein Isoforms / agonists,  genetics,  metabolism
Receptors, G-Protein-Coupled / agonists*,  genetics,  metabolism*
alpha-Linolenic Acid / pharmacology*
Chemical
Reg. No./Substance:
0/O3FAR1 protein, human; 0/Protein Isoforms; 0/Receptors, G-Protein-Coupled; 25167-62-8/Docosahexaenoic Acids; 463-40-1/alpha-Linolenic Acid

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