Central melatonin receptors in red deer (Cervus elaphus)

Lynda Williams, L T Hannah, C E Kyle, Clare Lesley Adam

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Red deer display characteristic seasonal changes in appetite, growth, and reproduction which are mediated by the pineal hormone, melatonin, which provides a direct neuroendocrine transduction of the ambient photoperiod. To identify potential central sites of action for this hormone, [2-I-125]iodomelatonin binding sites were localized and characterized within the cervine brain and pituitary by in vitro autoradiography. Specific binding was distributed over a number of discrete regions of the brain, including the cortex, septum, putamen, hippocampus, cerebellum, and superior colliculus. The choroid plexus, the pars tuberalis, and the pars distalis of the pituitary were also specifically labeled. Specific binding was completely abolished in the presence of 10(-7) M melatonin and inhibited in the presence of 10(-4) M GTP gamma S (guanosine-5-O-(3-thiotriphosphate)), a nonhydrolysable analogue of GTP, in the pars tuberalis, pars distalis, choroid plexus, and all neuronal regions examined apart from the hippocampus and layer III of the cerebral cortex. Inhibition of [2-I-125]iodomelatonin binding by GTP gamma S is indicative that binding is representative of a G-protein-coupled receptor. Characterization studies showed that [2-I-125]iodomelatonin binding was time-dependent and saturable with a dissociation constant (K-d) in the low picomolar range (approximately 10 pM). Competition studies with iodomelatonin, melatonin, and N-acetylserotonin gave IC50 values similar to those previously characterized for the melatonin receptor in the ovine pars tuberalis. (C) 1996 Academic Press, Inc.

Original languageEnglish
Pages (from-to)1-6
Number of pages6
JournalGeneral and Comparative Endocrinology
Volume104
Issue number1
DOIs
Publication statusPublished - Oct 1996

Keywords

  • BINDING-SITES
  • PARS TUBERALIS
  • AUTORADIOGRAPHIC LOCALIZATION
  • GUANINE-NUCLEOTIDES
  • PITUITARY-GLAND
  • RAT
  • 2-<I-125>IODOMELATONIN
  • CYCLE
  • BRAIN
  • MINK

Cite this

Central melatonin receptors in red deer (Cervus elaphus). / Williams, Lynda; Hannah, L T ; Kyle, C E ; Adam, Clare Lesley.

In: General and Comparative Endocrinology, Vol. 104, No. 1, 10.1996, p. 1-6.

Research output: Contribution to journalArticle

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AB - Red deer display characteristic seasonal changes in appetite, growth, and reproduction which are mediated by the pineal hormone, melatonin, which provides a direct neuroendocrine transduction of the ambient photoperiod. To identify potential central sites of action for this hormone, [2-I-125]iodomelatonin binding sites were localized and characterized within the cervine brain and pituitary by in vitro autoradiography. Specific binding was distributed over a number of discrete regions of the brain, including the cortex, septum, putamen, hippocampus, cerebellum, and superior colliculus. The choroid plexus, the pars tuberalis, and the pars distalis of the pituitary were also specifically labeled. Specific binding was completely abolished in the presence of 10(-7) M melatonin and inhibited in the presence of 10(-4) M GTP gamma S (guanosine-5-O-(3-thiotriphosphate)), a nonhydrolysable analogue of GTP, in the pars tuberalis, pars distalis, choroid plexus, and all neuronal regions examined apart from the hippocampus and layer III of the cerebral cortex. Inhibition of [2-I-125]iodomelatonin binding by GTP gamma S is indicative that binding is representative of a G-protein-coupled receptor. Characterization studies showed that [2-I-125]iodomelatonin binding was time-dependent and saturable with a dissociation constant (K-d) in the low picomolar range (approximately 10 pM). Competition studies with iodomelatonin, melatonin, and N-acetylserotonin gave IC50 values similar to those previously characterized for the melatonin receptor in the ovine pars tuberalis. (C) 1996 Academic Press, Inc.

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KW - RAT

KW - 2-<I-125>IODOMELATONIN

KW - CYCLE

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KW - MINK

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