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Identification of farnesyl pyrophosphate and N-arachidonylglycine as endogenous ligands for GPR92

Authors
Oh, Da YoungYoon, Jung MinMoon, Mi JinHwang, Jong-IkChoe, HanLee, Ju YeonKim, Jae IlKim, SunohRhim, HyewhonO'Dell, David K.Walker, J. MichaelNa, Heung SikLee, Min GooKwon, Hyuk BangKim, KyungjinSeong, Jae Young
Issue Date
25-7월-2008
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.283, no.30, pp.21054 - 21064
Indexed
SCIE
SCOPUS
Journal Title
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume
283
Number
30
Start Page
21054
End Page
21064
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/123012
DOI
10.1074/jbc.M708908200
ISSN
0021-9258
Abstract
A series of small compounds acting at the orphan G protein-coupled receptor GPR92 were screened using a signaling pathway-specific reporter assay system. Lipid-derived molecules including farnesyl pyrophosphate (FPP), N-arachidonylglycine (NAG), and lysophosphatidic acid were found to activate GPR92. FPP and lysophosphatidic acid were able to activate both G(q/11)- and G(s)-mediated signaling pathways, whereas NAG activated only the G(q/11)-mediated signaling pathway. Computer-simulated modeling combined with site-directed mutagenesis of GPR92 indicated that Thr97, Gly98, Phe101, and Arg267 of GPR92 are responsible for the interaction of GPR92 with FPP and NAG. Reverse transcription-PCR analysis revealed that GPR92 mRNA is highly expressed in the dorsal root ganglia (DRG) but faint in other brain regions. Peripheral tissues including, spleen, stomach, small intestine, and kidney also expressed GPR92 mRNA. Immunohistochemical analysis revealed that GPR92 is largely co-localized with TRPV1, a nonspecific cation channel that responds to noxious heat, in mouse and human DRG. FPP and NAG increased intracellular Ca2+ levels in cultured DRG neurons. These results suggest that FPP and NAG play a role in the sensory nervous system through activation of GPR92.
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