A human gene that shows identity with the gene encoding the angiotensin receptor is located on chromosome 11

O’Dowd, Brian F.; Heiber, Michael; Chan, Audrey S.; Heng, Henry H.Q.; Tsui, Lap‐Chee; Kennedy, James L.; Shi, Xiaomei; Petronis, Artūras; George, Susan R.; Nguyen, Tuan

doi:10.1016/0378-1119(93)90495-o

Cited by 763 publications

(547 citation statements)

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“…Apelin receptor was originally identified as a receptor related to angiotensin II receptor 1, due to high homology between the two receptor proteins [38]. This receptor is 380 amino acids long, consists of seven transmembrane domains and also includes a signal sequence that allows agonist-independent nuclear localization, a feature that may be cell-specific [27].…”

Section: Introductionmentioning

confidence: 99%

The apelinergic system in the developing lung: Expression and signaling

et al. 2011

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a b s t r a c tApelin and its receptor APJ constitute a signaling pathway best recognized as an important regulator of cardiovascular homeostasis. This multifunctional peptidergic system is currently being described to be involved in embryonic events which extend into vascular, ocular and heart development. Additionally, it is highly expressed in pulmonary tissue. Therefore, the aim of this study was to investigate the role of apelinergic system during fetal lung development. Immunohistochemistry and Western blot analysis were used to characterize apelin and APJ expression levels and cellular localization in normal fetal rat lungs, at five different gestational ages as well as in the adult. Fetal rat lung explants were cultured in vitro with increasing doses of apelin. Treated lung explants were morphometrically analyzed and assessed for MAPK signaling modifications. Both components of the apelinergic system are constitutively expressed in the developing lung, with APJ exhibiting monomeric, dimeric and oligomeric forms in the pulmonary tissue. Pulmonary epithelium also displayed constitutive nuclear localization of the receptor. Fetal apelin expression is higher than adult expression. Apelin supplementation inhibitory effect on branching morphogenesis was associated with a dose dependent decrease in p38 and JNK phosphorylation. The results presented provide the first evidence of the presence of an apelinergic system operating in the developing lung. Our findings also suggest that apelin inhibits fetal lung growth by suppressing p38 and JNK signaling pathways.

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Section: Introductionmentioning

confidence: 99%

The apelinergic system in the developing lung: Expression and signaling

et al. 2011

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“…The apj receptor was cloned in 1993 and found to exhibit significant homology with the angiotensin II receptor type 1, although angiotensin is not a ligand of the apj receptor (1). The apj receptor was originally shown to be expressed in several regions in the CNS (1,2).…”

Section: Introductionmentioning

confidence: 99%

“…The apj receptor was originally shown to be expressed in several regions in the CNS (1,2). It was subsequently demonstrated to be ubiquitously expressed with high expression levels in the lung, heart, medial layer of vessels and endothelial cells (3,4).…”

Section: Introductionmentioning

confidence: 99%

“…It was subsequently demonstrated to be ubiquitously expressed with high expression levels in the lung, heart, medial layer of vessels and endothelial cells (3,4). The receptor is a G-protein coupled receptor signaling inhibition of adenylyl cyclase activity eliciting reduced cAMP formation (1,5) although also raise of intracellular calcium and activation of extracellularly regulated kinases (ERK) have been reported (6,7). The endogenous ligand for the apj receptor is apelin, which was initially demonstrated in stomach extracts in 1998 (8).…”

Section: Introductionmentioning

confidence: 99%

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The apj receptor is expressed in pancreatic islets and its ligand, apelin, inhibits insulin secretion in mice

Winzell

Magnusson

Åhrén

2005

Regulatory Peptides

177

114

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Apelin is the endogenous ligand of the G-protein coupled apj receptor. Apelin is expressed in the brain, the hypothalamus and the stomach and was recently shown also to be an adipokine secreted from the adipocytes. Although apelin has been suggested to be involved in the regulation of food intake, it is not known whether the peptide affects islet function and glucose homeostasis. We show here that the apj receptor is expressed in pancreatic islets and that intravenous administration of full-length apelin-36 (2 nmol/kg) inhibits the rapid insulin response to intravenous glucose (1g/kg) by 35% in C57BL/6J mice. Thus, the acute (1-5 min) insulin response to intravenous glucose was 682±23 pmol/l after glucose alone (n=17) and 445±58 pmol/l after glucose plus apelin-36 (n=18; P=0.017). This was associated with impaired glucose elimination (the 5-20 min glucose elimination was 2.9±0.1%/min after glucose alone versus 2.3±0.2%/min after glucose plus apelin-36, P=0.008). Apelin (2nmol/kg) also inhibited the insulin response to intravenous glucose in obese insulin resistant high-fat fed C57BL/6J mice (P=0.041). After 60 min incubation of isolated islets from normal mice, insulin secretion in the presence of 16.7 mmol/l glucose was inhibited by apelin-36 at 1 µmol/l, whereas apelin-36 did not significantly affect insulin secretion at 2.8 or 8.3 mmol/l glucose or after stimulation of insulin secretion by KCl. Islet glucose oxidation at 16.7 mmol/l was not affected by apelin-36. We conclude that the apj receptor is expressed in pancreatic islets and that apelin-36 inhibits glucose-stimulated insulin secretion both in vivo and in vitro.This may suggest that the islet beta-cells are targets for apelin-36.

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“…We have utilized several technical strategies to isolate novel members of this gene family, belonging to many diverse classes. During this process we reported the characterization of many human genes encoding GPCRs, namely APJ [1], GPRI, GPR2, and GPR3 [2], GPR4, GPR5, and GPR6 [3], GPR7, and GPR8 [4], GPR9, GPR10, and GPR14 [5], GPR15 [6], GPR20, 21, 22 and 23 [7]. In this report, we describe a novel human gene (presently named GPRI9) encoding a putative receptor which has significant amino acid sequence identity with the D2 dopamine and neuropeptide Y families of receptors.…”

Section: Introductionmentioning

confidence: 99%

A novel gene codes for a putative G protein‐coupled receptor with an abundant expression in brain

O’Dowd

Nguyen²,

Lynch

et al. 1996

FEBS Letters

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Following the cloning of the dopamine receptors we continued a search of the human genome for related genes. We searched an EST data base and discovered cDNA fragments encoding novel G protein-coupled receptor genes. The available GenBank sequence of one of these EST fragments showed that it encoded a receptor with closest similarity to the D2 dopamine and adrenergic receptors. This cDNA was used to isolate the gene (GPRI9), and the encoded receptor also demonstrated similarity with the neuropeptide Y receptor. The gene was mapped to chromosome 12, in region p13.2-12.3. Northern blot analysis revealed expression of GPRI9 in peripheral regions, and brain regions significantly overlapping with the D2 receptor gene expression. A sequence of the rat orthologue of GPRI9 was obtained and in situ hybridization analysis demonstrated a very abundant expression in rat brain.

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A human gene that shows identity with the gene encoding the angiotensin receptor is located on chromosome 11

Cited by 763 publications

References 19 publications

The apelinergic system in the developing lung: Expression and signaling

The apelinergic system in the developing lung: Expression and signaling

The apj receptor is expressed in pancreatic islets and its ligand, apelin, inhibits insulin secretion in mice

A novel gene codes for a putative G protein‐coupled receptor with an abundant expression in brain

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