Molecular and functional characterization of a partial cDNA encoding a novel chicken brain melatonin receptor

Liu, F.; He, Yuan; Sugamori, Kim S.; Hamadanizadeh, A.; Lee, Frank J.S.; Pang, S.F.; Brown, Gregory M.; Pristupa, Zdenek B.; Niznik, Hyman B.

doi:10.1016/0014-5793(95)01129-3

Cited by 49 publications

(29 citation statements)

References 41 publications

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“…The reaction was terminated by the addition of 0.5 ml of 0.2N HCl and incubation for 20 min at 4°C. Cellular debris was pelleted, and aliquots of the supernatant were used to determine the cAMP content via immunodetection (Amersham Biosciences, Oakville, Ontario, Canada) as described previously (Liu et al, 1995). To ensure equivalence of whole-cell cAMP assay comparisons, we monitored receptor densities for [ 3 H] SCH-23390 binding (3.0 nM final concentration).…”

Section: Methodsmentioning

confidence: 99%

“…COS-7 cells were transiently transfected as described above, placed into 150 mm plates, and cultured for 4 -5 d. COS-7 cells were maintained in Dulbecco's ␣-MEM supplemented with 10% fetal calf serum at 37°C and 5% CO 2 . Next the cells were collected, and membranes were prepared for binding assays as described previously (Liu et al, 1995). For saturation experiments 0.5 ml aliquots of tissue homogenate (ϳ50 -100 g of membrane protein) were incubated in duplicate with increasing concentrations of [ 3 H] SCH-23390 (85.5 Ci/ mmol; 30 -6800 pM final concentration) for 120 min at room temperature in a total volume of 1.5 ml.…”

Section: Methodsmentioning

confidence: 99%

“…Nonspecific binding was defined in the presence of 10 M (ϩ)-butaclamol. Binding data were analyzed by the nonlinear least-square curve-fitting program KaleidaGraph (Abelbeck Software, Synergy, Reading, PA) as described previously (Liu et al, 1995). Confocal imaging.…”

Section: Methodsmentioning

confidence: 99%

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Regulation of Dopamine D1 Receptor Function by Physical Interaction with the NMDA Receptors

Lin¹,

Lee²,

Moszczynska³

et al. 2004

J. Neurosci.

177

142

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Functional interactions between dopamine D1-like receptors and NMDA subtype glutamate receptors have been implicated in the maintenance of normal brain activity and neurological dysfunction. Although modulation of NMDA receptor functions by D1 receptor activation has been the subject of extensive investigation, little is known as to how the activation of NMDA receptors alters D1 function. Here we report that NMDA receptors regulate D1 receptor function via a direct protein-protein interaction mediated by the carboxyl tail regions of both receptors. In both cotransfected cells and cultured hippocampal neurons the activation of NMDA receptors increases the number of D1 receptors on the plasma membrane surface and enhances D1 receptor-mediated cAMP accumulation via a SNAREdependent mechanism. Furthermore, overexpression of mini-genes encoding either NR1 or D1 carboxyl tail fragments disrupts the D1-NR1 direct protein-protein interaction and abolishes NMDA-induced changes in both D1 cell surface expression and D1-mediated cAMP accumulation. Our results demonstrate that the D1-NR1 physical interaction enables NMDA receptors to increase plasma membrane insertion of D1 receptors and provides a novel mechanism by which the activation of NMDA receptors upregulates D1 receptor function. Understanding the molecular mechanisms by which D1 and NMDA receptors functionally interact may provide insight toward elucidating the molecular neurobiological mechanisms involved in many neuropsychiatric illnesses, such as schizophrenia.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Regulation of Dopamine D1 Receptor Function by Physical Interaction with the NMDA Receptors

Lin¹,

Lee²,

Moszczynska³

et al. 2004

J. Neurosci.

177

142

View full text Add to dashboard Cite

show abstract

“…Recent molecular studies (19,29) have led to the identification of three avian melatonin receptor subtypes, Mel 1a , Mel 1b , and Mel 1c , which comprise a distinct subfamily within the superfamily of G-protein-coupled receptors. Because Mel 1c mRNA is differentially expressed in the chicken hypothalamus (19), quail Mel 1c cDNA was cloned and used for in situ hybridization of Mel 1c mRNA, which was combined with GnIH immunocytochemistry.…”

Section: Figmentioning

confidence: 99%

Melatonin induces the expression of gonadotropin-inhibitory hormone in the avian brain

Ubuka

Bentley

Ukena

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

297

251

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We recently identified a novel hypothalamic neuropeptide inhibiting gonadotropin release in quail and termed it gonadotropininhibitory hormone (GnIH). Cell bodies and terminals containing the dodecapeptide GnIH are localized in the paraventricular nucleus (PVN) and median eminence, respectively. To understand the physiological role of GnIH, we investigated the mechanisms that regulate GnIH expression. In this study, we show that melatonin originating from the pineal gland and eyes induces GnIH expression in the quail brain. Pinealectomy (Px) combined with orbital enucleation (Ex) (Px plus Ex) decreased the expression of GnIH precursor mRNA and content of mature GnIH peptide in the diencephalon, which includes the PVN and median eminence. Melatonin administration to Px plus Ex birds caused a dosedependent increase in expression of GnIH precursor mRNA and production of mature peptide. The expression of GnIH was photoperiodically controlled and increased under short-day photoperiods, when the duration of melatonin secretion increases. To identify the mode of melatonin action on GnIH induction, we investigated the expression of Mel 1c, a melatonin receptor subtype, in GnIH neurons. In situ hybridization of Mel1c mRNA combined with immunocytochemistry for GnIH revealed that Mel 1c mRNA was expressed in GnIH-immunoreactive neurons in the PVN. Melatonin receptor autoradiography further revealed specific binding of melatonin in the PVN. These results indicate that melatonin is a key factor for GnIH induction. Melatonin appears to act directly on GnIH neurons through its receptor to induce GnIH expression. This is the first demonstration, to our knowledge, of a direct action of melatonin on neuropeptide induction in any vertebrate class. melatonin receptor ͉ photoperiod ͉ reproduction

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“…When expressed in mammalian cells, the complementary DNA (cDNA) encodes a specific melatonin receptor which, like the native receptor, is negatively coupled to adenylyl cyclase through a pertussis toxin-sensitive G-protein . By using degenerate primers designed from the sequence of the melanophore receptor, three distinct subtypes of the melatonin receptor 1995a,b;Liu et al, 1995 (Reppert et al, 1995a,b).…”

Section: Introductionmentioning

confidence: 99%

Analogues of diverse structure are unable to differentiate native melatonin receptors in the chicken retina, sheep pars tuberalis and Xenopus melanophores

Pickering¹,

Sword²,

Vonhoff³

et al. 1996

British J Pharmacology

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1 The pineal hormone melatonin exerts its biological effects through specific, high affinity G-protein coupled receptors. Recently, three melatonin receptor subtypes (Mella, Mellb and Mel,c) have been cloned. Neither the cloned subtypes, nor the native receptors have yet been compared in a detailed pharmacological analysis. 2 The present study examined the structure-activity relationships of a series of 21 melatonin analogues, by comparing their potency on the pigment aggregation response in Xenopus laevis melanophores with their affinity in radioligand binding competition studies in chicken retina and sheep pars tuberalis (PT), two tissues in which melatonin is known to mediate a biological response. 3 All but four of the analogues were full melatonin receptor agonists producing a concentration-related redistribution of pigment granules in cultured Xenopus melanophores. The remaining analogues produced little pigment aggregation at 10 gM. 4 Saturation studies with 2-[1251]-iodomelatonin identified a single binding site in the chicken retina and sheep PT membranes, with a KD of 36.6 + 2.8 and 37.3 + 4.3 pM, and a maximal number of binding sites (Bmax) of 16.6 + 0.5, and 40.1 + 1.7 fmol mg-' protein, respectively. 5 Comparison of the potency/affinity of the analogues for the binding sites gave a highly significant correlation in each case, retina/melanophore, r=0.97 (P<0.001, n= 17), PT/melanophore, r=0.97 (P<0.001, n=17) and PT/retina, r=0.98 (P<0.001, n=21). 6 Despite their large range in affinity and structural diversity these melatonin agonists were unable to distinguish between melatonin receptors in the chicken retina, sheep pars tuberalis and Xenopus melanophores.

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Molecular and functional characterization of a partial cDNA encoding a novel chicken brain melatonin receptor

Cited by 49 publications

References 41 publications

Regulation of Dopamine D1 Receptor Function by Physical Interaction with the NMDA Receptors

Regulation of Dopamine D1 Receptor Function by Physical Interaction with the NMDA Receptors

Melatonin induces the expression of gonadotropin-inhibitory hormone in the avian brain

Analogues of diverse structure are unable to differentiate native melatonin receptors in the chicken retina, sheep pars tuberalis and Xenopus melanophores

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