Identification of GPR55 as a lysophosphatidylinositol receptor

Identification of GPR55 as a lysophosphatidylinositol receptor
复制标题

DOI:
10.1016/j.bbrc.2007.08.078
复制
发表时间:
2007-11-03
影响因子:
3.1
通讯作者:
Sugiura, Takayuki
Sugiura, Takayuki
中科院分区:
生物学4区
文献类型:
--
作者:
Oka, Saori;Nakajima, Keisuke;Sugiura, Takayuki

文献摘要

被引文献

相似文献

GPR 55是一种孤儿G蛋白偶联受体。在这项研究中,我们探索了一种可能的内源性配体GPR 55使用HEK 293细胞表达GPR 55。我们发现,溶血磷脂酰肌醇诱导细胞外信号调节激酶的快速磷酸化在瞬时或稳定GPR 55表达细胞。另一方面,溶血磷脂酰肌醇不诱导载体转染细胞中细胞外信号调节激酶的磷酸化。溶血磷脂酸和1-磷酸鞘氨醇也诱导GPR 55表达细胞中细胞外信号调节激酶的磷酸化。然而,这些脂质磷酸在载体转染的细胞中引起类似的反应。各种类型的其他溶血脂以及大麻素受体配体不诱导细胞外信号调节激酶的磷酸化。我们还发现,溶血磷脂酰肌醇引起了快速的Ca 2+瞬态GPR 55表达细胞。溶血磷脂酰肌醇还刺激GTP γ S与表达GPR 55的细胞膜的结合。这些结果有力地表明,GPR 55是溶血磷脂酰肌醇的特异性和功能性受体。(c)2007爱思唯尔公司All rights reserved.
GPR55 is an orphan G protein-coupled receptor. In this study, we explored a possible endogenous ligand for GPR55 using HEK293 cells which expressed GPR55. We found that lysophosphatidylinositol induced rapid phosphorylation of the extracellular signal-regulated kinase in transiently or stably GPR55-expressing cells. On the other hand, lysophosphatidylinositol did not induce phosphorylation of the extracellular signal-regulated kinase in vector-transfected cells. Lysophosphatidic acid and sphingosine 1-phosphate also induced phosphorylation of the extracellular signal-regulated kinase in GPR55-expressing cells. However, these lipid phosphoric acids elicited similar responses in vector-transfected cells. Various types of other lysolipids as well as the cannabinoid receptor ligands did not induce phosphorylation of the extracellular signal-regulated kinase. We also found that lysophosphatidylinositol elicited a rapid Ca2+ transient in GPR55-expressing cells. Lysophosphatidylinositol also stimulated the binding of GTP gamma S to the GPR55-expressing cell membranes. These results strongly suggest that GPR55 is a specific and functional receptor for lysophosphatidylinositol. (c) 2007 Elsevier Inc. All rights reserved.