Characterization of neuropeptide Y (NPY) receptors in human hippocampus

Li, Wei; Hexum, Terry D.

doi:10.1016/0006-8993(91)90246-r

Cited by 11 publications

(7 citation statements)

References 11 publications

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“…The present data also indicate that Y2 receptors are the major NPY binding sites in the nerve fibres in rat DRG, and normal rat and monkey spinal cord, since a marked reduction in PYY binding was observed after coincubation with the Y2 agonist NPY 13-36 (Wahlestedt et al, 1986Sheikh et a/., 1989;Dumont et al, 1990Dumont et al, , 1992Dumont et al, , 1993Fuhlendorff et al, 1990;Aicher et al, 1991;Li and Hexum, 1991;Krause et al, 1992;Larsen et al, 1993). This is in agreement with earlier results showing that Y2 receptors are important in rat DRG (Bleakman et al, 1991), but is somewhat surprising in view of the very strong expression of YI receptor mRNA in many DRG neurons in the rat (Jazin et a/., 1993;Zhang et al, 1994).…”

Section: Npy Binding Sites In Control Rat and Monkey Drg And Spinal Csupporting

confidence: 74%

“…Studies with peptide fragments of NPY and PYY have indicated that multiple NPY and PYY receptor subtypes exist (Wahlestedt et al, 1986;Sheikh et al, 1989;Dumont et al, 1990Dumont et al, , 1992Dumont et al, , 1993Fuhlendorff et al, 1990;Aicher et al, 1991;Li and Hexum, 1991;Krause et al, 1992;Larsen et al, 1993). The Y 1 receptor is considered to be a postjunctional and the Y2 a prejunctional receptor (Wahlestedt et al, 1986;Colmers et al, 1991;Potter and McCloskey, 1992).…”

Section: Introductionmentioning

confidence: 97%

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Neuropeptide Y and Galanin Binding Sites in Rat and Monkev Lumbar Dorsal Root Ganalia and Spinal Cord and Effect of Peripheral Axotomy

Nilsson

et al. 1995

Eur J of Neuroscience

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Using monoiodinated peptide YY (PYY) and galanin as radioligands, and neuropeptide Y (NPY) fragments, the distribution of NPY binding sites and its subtypes Y1 and Y2, and of galanin binding sites, was investigated in rat and monkey lumbar (L) 4 and L5 dorsal root ganglia (DRG) and spinal cord before and after a unilateral sciatic nerve cut, ligation or crush. Receptor autoradiography revealed that [125I]PYY bound to some DRG neurons and a few nerve fibres in normal rat DRG, and most of these neurons were small. NPY binding sites were observed in laminae I-IV and X of the rat dorsal horn and in the lateral spinal nucleus, with the highest density in laminae I-II. [125I]PYY binding was most strongly attenuated by NPY13-36, a Y2 agonist, and partially inhibited by [Leu31,Pro34]NPY, a Y1 agonist, in both rat DRG and the dorsal horn of the spinal cord. These findings suggest that Y2 receptors are the main NPY receptors in rat DRG and dorsal horn, but also that Y1 receptors exist. After sciatic nerve cut, PYY binding markedly increased in nerve fibres and neurons in DRG, especially in large neuron profiles, and in laminae III-IV of the dorsal horn, as well as in nerve fibres in dorsal roots and the sciatic nerve. Incubation with NPY13-36 completely abolished PYY binding, which was also reduced by [Leu31,Pro34] NPY. However, the increase in PYY binding seen in laminae I-IV of the ipsilateral dorsal horn after axotomy was not observed after coincubation with [Leu31,Pro34] NPY. NPY binding sites were seen in a few neurons in monkey DRG and in laminae I-II, X and IX of the monkey spinal cord. The intensity of PYY binding in laminae I-II of the dorsal horn was decreased after axotomy. Galanin receptor binding sites were not observed in rat DRG, but were observed in the superficial dorsal horn of the spinal cord, mainly in laminae I-II. Axotomy had no effect on galanin binding in rat DRG and dorsal horn. However, galanin receptor binding was observed in many neurons in monkey L4 and L5 DRG and in laminae I-IV and X of monkey L4 and L5 spinal cord, with the highest intensity in laminae I-II. No marked effect of axotomy was observed on the distribution and intensity of galanin binding in monkey DRG or spinal cord.(ABSTRACT TRUNCATED AT 400 WORDS)

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Section: Npy Binding Sites In Control Rat and Monkey Drg And Spinal Csupporting

confidence: 74%

Section: Introductionmentioning

confidence: 97%

Neuropeptide Y and Galanin Binding Sites in Rat and Monkev Lumbar Dorsal Root Ganalia and Spinal Cord and Effect of Peripheral Axotomy

Nilsson

et al. 1995

Eur J of Neuroscience

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“…The presented results are interesting in light of the reported existence of two receptor types for NPY, Y1, and Y2, each with specific biological properties (Sheikh et al, 1989(Sheikh et al, , 1990Wahlestedt et al, 1986Wahlestedt et al, , 1990. Since it is assumed that most of the NPY receptors in rat hippocampus are of the Y2-type (Dumont et al, 1993;Li and Hexum, 1991) and the short C-terminal fragment NPY( 13-36) has strong agonistic effects on the Y2-receptor while lacking effects on the post-junctional Y 1 receptor (Wahlestedt et al, 1986), it could be postulated that the increase in NPY-immunoreactive material found…”

Section: Discussionmentioning

confidence: 63%

“…Since it is assumed that most of the NPY receptors in rat hippocampus are of the Y2-type (Dumont et al, 1993;Li and Hexum, 1991) and the short C-terminal fragment NPY( 13-36) has strong agonistic effects on the Y2-receptor while lacking effects on the post-junctional Y 1 receptor (Wahlestedt et al, 1986), it could be postulated that the increase in NPY-immunoreactive material found…”

Section: Discussionmentioning

confidence: 99%

“…Interestingly, existence of not only several classes of receptors but also of several biologically active molecular forms have been demonstrated for many peptides. Since the NPY receptors in the rat hippocampus have primarily Y2 characteristics (Li and Hexum, 1991), we decided to investigate possible existence of molecular heterogeneity of endogenous NPY in the rat brain and, if existing, whether it would be affected by ECS. The present work attempts to address this issue, using different column chromatographic techniques combined with immunochemical methods based on antisera directed towards two different epitopes of the NPY molecule (N1 , directed towards the midportion of NPY and C 1, directed towards the C-terminal end of NPY).…”

Section: Introductionmentioning

confidence: 99%

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Chromatographic and immunochemical characterization of rat brain neuropeptide Y‐like immunoreactivity (NPY‐LI) following repeated electroconvulsive, stimuli

Stenfors

Mathé

Theodorsson

1995

J of Neuroscience Research

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The present work investigates the possible existence of molecular heterogeneity of endogenous neuropeptide Y (NPY) in the rat brain and, if existing, whether it is affected by repeated electroconvulsive stimuli (ECS). Different column chromatographic techniques (gel-permeation chromatography, HPLC, ion-pair reverse-phase HPLC) were used combined with immunochemical methods based on antisera directed towards two different epitopes of NPY (antiserum N1, directed towards the midportion of NPY, and antiserum C1, directed towards the C-terminal end of NPY). Following repeated ECS increased concentrations of NPY were seen in the occipital cortex and hippocampus (P < 0.001) when analyzed by direct radioimmunoassays (RIA). Chromatographic characterization showed that the NPY mainly consisted of intact NPY (1-36) and sulphoxidated form of NPY, no short C-terminal homologues were found. This is of importance since it has been shown that NPY (1-36) has different biological properties compared to C-terminal homologues.

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Biophysical methods to study ligand-receptor interactions of neuropeptide Y

Bettio

Beck‐Sickinger

2001

Biopolymers

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Neuropeptide Y (NPY) is a 36 amino acids peptide amide that was isolated for the first time almost 20 years ago from porcine brain. NPY displays a multiplicity of physiological effects that are transmitted by at least six G‐protein coupled receptors (GPCRs) named Y1, Y2, Y3, Y4, Y5, and y6. Because of the difficulty in obtaining high‐resolution crystallographic structures from GPCRs that all belong to seven transmembrane helices proteins, a variety of biophysical methods have been applied in order to characterize the interaction of ligand and receptor. In this review article we present the most relevant outcomes of the studies performed in this field by our group and others. The use of photoaffinity labeling allowed the molecular characterization of the Y2 receptor. The concerted application of molecular modeling and mutagenesis studies led to a model for the interaction of the natural agonist and nonpeptide antagonists with the Y1 receptor. The three‐dimensional (3D) structure and dynamics of micelle‐bound NPY and their implications for receptor selection have been studied by NMR. The characterization of the tertiary and quaternary structure of the NPY dimer in solution at millimolar concentrations has been performed by NMR and extended to physiologically relevant concentrations by fluorescence resonance energy transfer (FRET) experiments performed with fluorescence‐labeled analogues. © 2002 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 60: 420–437, 2001

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Characterization of neuropeptide Y (NPY) receptors in human hippocampus

Cited by 11 publications

References 11 publications

Neuropeptide Y and Galanin Binding Sites in Rat and Monkev Lumbar Dorsal Root Ganalia and Spinal Cord and Effect of Peripheral Axotomy

Neuropeptide Y and Galanin Binding Sites in Rat and Monkev Lumbar Dorsal Root Ganalia and Spinal Cord and Effect of Peripheral Axotomy

Chromatographic and immunochemical characterization of rat brain neuropeptide Y‐like immunoreactivity (NPY‐LI) following repeated electroconvulsive, stimuli

Biophysical methods to study ligand-receptor interactions of neuropeptide Y

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