A prolactin-releasing peptide in the brain

Hinuma, Shuji; Habata, Yugo; Fujii, Ryo; Kawamata, Yuji; Hashimoto, Masaki; Fukusumi, Shoji; Kitada, Chieko; Masuo, Yoshinori; Asano, Tsuneo; Matsumoto, Hirokazu; Sekiguchi, Mutsuo; Kurokawa, Tsutomu; Nishimura, Osamu; Onda, Haruo; Fujino, Masahiko

doi:10.1038/28437

Cited by 78 publications

(169 citation statements)

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“…Both of these functions are probably required for maximally effective antimycobacterial immunity in mice 8 and in humans 9,10 . These responses are particularly favoured by DNA vaccines 11 .…”

Section: Methodsmentioning

confidence: 99%

“…The orphan GPCR SLC-1 (also called GPR24) 2,3 , exhibits about 40% amino-acid identity to ®ve known human somatostatin receptors (Ga i -linked). On the assumption that SLC-1 may also bind a peptidic ligand and couple to Ga i proteins, we collected different tissues that express SLC-1 and processed them for peptide extraction using different protocols 7,9,10 . Each chromatographic fraction was tested for its ability to induce a decrease in cyclic AMP in forskolin-stimulated, SLC-1-transfected Chinese hamster ovary (CHO) cells.…”

mentioning

confidence: 99%

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Molecular characterization of the melanin-concentrating-hormone receptor

Saito

Nothacker

Wang

et al. 1999

Nature

515

332

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Orphan G-protein-coupled receptors (GPCRs) are cloned proteins with structural characteristics common to the GPCRs but that bind unidentified ligands. Orphan GPCRs have been used as targets to identify novel transmitter molecules. Here we describe the isolation from brain extracts and the characterization of the natural ligand of a particular orphan GPCR (SLC-1) that is sequentially homologous to the somatostatin receptors. We show that the natural ligand of this receptor is the neuropeptide melanin-concentrating hormone (MCH). MCH is a cyclic peptide that regulates a variety of functions in the mammalian brain, in particular feeding behaviour. We demonstrate that nanomolar concentrations of MCH strongly activate SLC-1-related pathways through G(alpha)i and/or G(alpha)q proteins. We have analysed the tissue localization of the MCH receptor and find that it is expressed in several brain regions, in particular those involved in olfactory learning and reinforcement mechanisms, indicating that therapies targeting the MCH receptor should act on the neuronal regulation of food consumption.

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Molecular characterization of the melanin-concentrating-hormone receptor

Saito

Nothacker

Wang

et al. 1999

Nature

515

332

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“…For example, peptides that stimulate secretion include thyrotropin-releasing hormone (TRH), which acts through phospholipase C dependent 4 and other 5 pathways, vasoactive intestinal peptide, which activates adenylate cyclase 6 and the recently identified prolactin (PRL) releasing peptide, which elevates arachidonic acid, suggesting a role for phospholipase A 2 (ref. 7). Lactotrophs are also subject to inhibition, most notably by dopamine acting through D 2 receptors to inhibit adenylate cyclase 8 and phospholipase C 9 and to activate a G-protein-coupled K + channel 10 .…”

Section: Articlesmentioning

confidence: 99%

Regulation of dense core release from neuroendocrine cells revealed by imaging single exocytic events

et al. 1999

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Using FM1-43 fluorescence, we have optically detected single exocytic and endocytic events in rat pituitary lactotrophs. About fifty discrete fluorescent spots abruptly appear around the entire surface of a cell bathed in FM1-43 and high-potassium saline. The spots, which also immunostain for prolactin, reflect the labeling of dense cores as well as membranes of exocytosed secretory granules. Stained cores are not released, but remain attached to the cell and are eventually endocytosed. However, in cells exposed to dopamine (or an analog, bromocriptine), the cores dissolve and are secreted after several seconds. Solubilization of dense cores is mediated through a reduction in cytoplasmic cyclic AMP. Thus, the composition of secretions from individual secretory granules is regulated.

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“…A novel candidate may be PRL-releasing peptide (PrRP) (223) that does stimulate PRL release in aggregate cell cultures (224). In both intact pituitary and aggregates, we recently found PrRP mRNA and PrRP-like immunoreactivity, particularly in gonadotrophs associated with cup-shaped lactotrophs (Swinnen and Denef, unpublished observations).…”

Section: Gonadotrophs Signal To Lactotrophs Somatotrophs and Corticomentioning

confidence: 99%

Endogenous Cannabinoids: Structure and Metabolism

Bisogno

2008

J Neuroendocrinology

144

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D9 -Tetrahydrocannabinol (THC), the main psychoactive compound extracted from Cannabis sativa, is the most representative component of the mixture of therapeutic substances that are communally referred to as cannabinoids (1). It acts as an agonist at specific G-protein-coupled receptors, cannabinoid receptor subtypes CB 1 and CB 2 (2). The discovery of cannabinoid receptors has driven the investigation of the existence of their natural ligands and, soon after, endocannabinoids were identified. N-arachidonoyl-ethanolamine (AEA, anandamide) and 2-arachidonoyl glycerol (2-AG) are the two most studied endocannabinoids. They are biosynthesised 'on demand' by cleavage of their membrane lipid precursors N-arachidonoyl-phosphatidylethanolamine (N-ArPE) and sn-1-acyl-2-arachidonoylglycerols (DAGs) respectively, and then inactivated by intracellular hydrolysing enzymes. Cannabinoid receptors, endocannabinoids and enzymes that biosynthesise [N-acyl-phosphatidylethanolamine-selective phospholipase D (NAPE-PLD) and diacylglycerol lipase (DAGL)] and degrade [fatty acid amide hydrolase (FAAH) and the monoacylglycerol lipases (MAGL)] AEA and 2-AG, respectively, are key components in the endocannabinoid system (3). Despite a large number of excellent studies having contributed to the current understanding of the endocannabinoid regulation and function, further efforts are necessary to fully comprehend this signalling system. Here, a review on the current knowledge on structure and metabolism of the best studied endogenous cannabinoids is presented. In particular, this review concentrates on the mechanisms responsible for the biosynthesis and inactivation of the endocannabinoids, as well as on the several inhibitors of their metabolism identified to date. Endocannabinoids and related N-acyl-ethanolaminesEndocannabinoids are defined as endogenous compounds capable of binding to and functionally activating cannabinoid receptors. At least five endocannabinoids have been identified to date (Fig. 1). Anandamide, the amide between arachidonic acid and ethanolamine, was the first endogenous ligand to be reported at the end of 1992 (4) and additional polyunsaturated ethanolamines that bind to cannabinoid receptors, homolinolenylethanolamide and docosatetraenylethanolamide, have been isolated in the brain. Other endocannabinoids, all derived from arachidonic acid, were identified. The identification of 2-AG, the ester of arachidonic acid with glycerol, isolated from canine gut and brain has also been reported (5, 6). Subsequently, the first endocannabinoid characterised by ether bond, 2-arachidonyl glyceryl ether or noladin ether, was isolated from porcine brain (7) and N-arachidonoyldopamine (NADA), a selective CB 1 agonist and a potent agonist of vanilloid receptors, was discovered (8, 9). O-arachidonoylethanolamine, the ester derivative of ethanolamine with arachidonic acid, with the same molecular weight as anandamide but with opposite orientation of the polar ethanolamine moiety, was named virodhamine from the Sanskrit word virodha, ...

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A prolactin-releasing peptide in the brain

Abstract: Improved methods for building protein models in electron-density and the location of errors in these models.

Cited by 78 publications

References 1 publication

Molecular characterization of the melanin-concentrating-hormone receptor

Molecular characterization of the melanin-concentrating-hormone receptor

Regulation of dense core release from neuroendocrine cells revealed by imaging single exocytic events

Endogenous Cannabinoids: Structure and Metabolism

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