Molecular Cloning and Characterization of a Novel Human G-protein-coupled Receptor, EDG7, for Lysophosphatidic Acid

Bandoh, Koji; Aoki, Junken; Hosono, Hiroyuki; Kobayashi, Susumu; Kobayashi, Tetsuyuki; Murakami‐Murofushi, Kimiko; Tsujimoto, Masafumi; Arai, Hiroyuki; Inoue, Kazuhide

doi:10.1074/jbc.274.39.27776

Cited by 480 publications

(449 citation statements)

References 36 publications

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“…Furthermore, HB‐EGF, COX‐2, and Wnt4 as well as Bmp2 have been shown to be risk factors for sex hormone‐dependent diseases, such as prostatic hyperplasia, breast cancer, and ovarian cancer (Bentley et al , 1992; Ferrandina et al , 2002; Levin, 2003; Zong et al , 2012). Since LPA 3 is highly expressed in the prostate, mammary gland, and ovary (Bandoh et al , 1999), LPA 3 signaling might contribute to the progression of such diseases.…”

Section: Discussionmentioning

confidence: 99%

Autotaxin–lysophosphatidic acid– LPA ₃ signaling at the embryo‐epithelial boundary controls decidualization pathways

et al. 2017

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During pregnancy, up‐regulation of heparin‐binding (HB‐) EGF and cyclooxygenase‐2 (COX‐2) in the uterine epithelium contributes to decidualization, a series of uterine morphological changes required for placental formation and fetal development. Here, we report a key role for the lipid mediator lysophosphatidic acid (LPA) in decidualization, acting through its G‐protein‐coupled receptor LPA 3 in the uterine epithelium. Knockout of Lpar3 or inhibition of the LPA‐producing enzyme autotaxin (ATX) in pregnant mice leads to HB‐EGF and COX‐2 down‐regulation near embryos and attenuates decidual reactions. Conversely, selective pharmacological activation of LPA 3 induces decidualization via up‐regulation of HB‐EGF and COX‐2. ATX and its substrate lysophosphatidylcholine can be detected in the uterine epithelium and in pre‐implantation‐stage embryos, respectively. Our results indicate that ATX–LPA–LPA 3 signaling at the embryo‐epithelial boundary induces decidualization via the canonical HB‐EGF and COX‐2 pathways.

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Section: Discussionmentioning

confidence: 99%

Autotaxin–lysophosphatidic acid– LPA ₃ signaling at the embryo‐epithelial boundary controls decidualization pathways

et al. 2017

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“…These responses are mediated by specific cell-surface G proteincoupled receptors, which are encoded by three cognate genes: lpa 1 /edg-2, lpa 2 /edg-4, and lpa 3 /edg-7 (Hecht et al, 1996;An et al, 1998;Contos and Chun, 1998;Bandoh et al, 1999;Chun, 1999;Chun et al, 1999;Fukushima et al, 2001). LPA 1 shares many downstream intracellular signaling pathways with LPA 2 , including inhibition of adenylyl cyclase (AC) and activation of phospholipase C (PLC) and the small GTPase Rho (Fukushima et al, 1998Ishii et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Dual Regulation of Actin Rearrangement through Lysophosphatidic Acid Receptor in Neuroblast Cell Lines: Actin Depolymerization by Ca²⁺-α-Actinin and Polymerization by Rho

Fukushima

Ishii²,

Habara

et al. 2002

MBoC

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Lysophosphatidic acid (LPA) is a potent lipid mediator with actions on many cell types. Morphological changes involving actin polymerization are mediated by at least two cognate G protein-coupled receptors, LPA 1 /EDG-2 or LPA 2 /EDG-4. Herein, we show that LPA can also induce actin depolymerization preceding actin polymerization within single TR mouse immortalized neuroblasts. Actin depolymerization resulted in immediate loss of membrane ruffling, whereas actin polymerization resulted in process retraction. Each pathway was found to be independent: depolymerization mediated by intracellular calcium mobilization, and ␣-actinin activity and polymerization mediated by the activation of the small Rho GTPase. ␣-Actininmediated depolymerization seems to be involved in growth cone collapse of primary neurons, indicating a physiological significance of LPA-induced actin depolymerization. Further evidence for dual regulation of actin rearrangement was found by heterologous retroviral transduction of either lpa 1 or lpa 2 in B103 cells that neither express LPA receptors nor respond to LPA, to confer both forms of LPA-induced actin rearrangements. These results suggest that diverging intracellular signals from a single type of LPA receptor could regulate actin depolymerization, as well as polymerization, within a single cell. This dual actin rearrangement may play a novel, important role in regulation of the neuronal morphology and motility during brain development.

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“…We also designed primers and tested these cell lines for the non-EDG LPA GPCRs LPA 4 and LPA 5 , as well as the intracellular LPA receptor and transcription factor PPARγ. PPARγ transcripts were present in RH7777 and DKO cells, but not in B103 cells [21].…”

Section: Receptor Profilingmentioning

confidence: 99%

“…The other EDG family members were cloned based upon sequence homology shortly thereafter, including two more LPA-specific receptors, EDG-4 [4] and EDG-7 [5], as well as four more S1P-specific receptors, EDG-3 [6] EDG-5 [7], EDG-6 [8], and EDG-8 [9]. In 2001 the IUPHAR proposed that the EDG nomenclature of the receptors be changed to reflect the receptors natural ligand and the order of its identification, giving the current receptor nomenclature of LPA 1 -3 and S1P [1][2][3][4][5] .…”

Section: Introductionmentioning

confidence: 99%

“…More recently GPR23 [15] and GPR92 [16,17] have been identified as LPA receptors, and tentatively renamed LPA 4 and LPA 5 , respectively, awaiting the approval of the IUPHAR nomenclature committee. Phylogenetically, LPA 4 and LPA 5 form a subfamily of LPA receptors -they are distantly related to the EDG-family LPA receptors, sharing only 20-24% sequence amino acid homology with the EDGs [15,16], which are 50-57% homologous with each other [15].…”

Section: Introductionmentioning

confidence: 99%

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Lysophospholipid signaling: Beyond the EDGs

Valentine

Fujiwara

Tsukahara

et al. 2008

Biochimica et Biophysica Acta (BBA) - General Subjects

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As our understanding of the myriads of biological effects caused by lysophospholipids expands we become witnesses to another miracle of nature that has endowed the simplest lysophospholipids with functions seemingly ubiquitous to every mammalian cell. A decade after the discovery of the EDGfamily lysophospholipid receptors the field has gained unimaginable impetus explaining the biological effects of sphingosine-1-phoshate (S1P) and lysophosphatidic acid (LPA). The discovery of LPA receptors in the purinergic G protein-coupled receptor (GPCR) gene cluster refined this picture and added complexity to our concepts of lysophospholipid cell signaling. The intracellular lysophospholipid targets -identified and not yet identified -make us realize the dual -mediator and second messenger -roles of lysophospholipids. In this paper we provide new data obtained concerning LPA-elicited responses using cell lines naturally lacking or intentionally knocked out of many of the known LPA GPCR, widely used by investigators in the field as cells with LPA receptor "null background". Our observations raise caution about the lack of LPA responsiveness in these cells and underline the unprecedented complexity and redundancy of lysophospholipid-evoked cellular responses.

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Molecular Cloning and Characterization of a Novel Human G-protein-coupled Receptor, EDG7, for Lysophosphatidic Acid

Cited by 480 publications

References 36 publications

Autotaxin–lysophosphatidic acid– LPA ₃ signaling at the embryo‐epithelial boundary controls decidualization pathways

Autotaxin–lysophosphatidic acid– LPA ₃ signaling at the embryo‐epithelial boundary controls decidualization pathways

Dual Regulation of Actin Rearrangement through Lysophosphatidic Acid Receptor in Neuroblast Cell Lines: Actin Depolymerization by Ca²⁺-α-Actinin and Polymerization by Rho

Lysophospholipid signaling: Beyond the EDGs

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Molecular Cloning and Characterization of a Novel Human G-protein-coupled Receptor, EDG7, for Lysophosphatidic Acid

Cited by 480 publications

References 36 publications

Autotaxin–lysophosphatidic acid– LPA 3 signaling at the embryo‐epithelial boundary controls decidualization pathways

Autotaxin–lysophosphatidic acid– LPA 3 signaling at the embryo‐epithelial boundary controls decidualization pathways

Dual Regulation of Actin Rearrangement through Lysophosphatidic Acid Receptor in Neuroblast Cell Lines: Actin Depolymerization by Ca2+-α-Actinin and Polymerization by Rho

Lysophospholipid signaling: Beyond the EDGs

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Autotaxin–lysophosphatidic acid– LPA ₃ signaling at the embryo‐epithelial boundary controls decidualization pathways

Autotaxin–lysophosphatidic acid– LPA ₃ signaling at the embryo‐epithelial boundary controls decidualization pathways

Dual Regulation of Actin Rearrangement through Lysophosphatidic Acid Receptor in Neuroblast Cell Lines: Actin Depolymerization by Ca²⁺-α-Actinin and Polymerization by Rho