Localization of mGluR6 to dendrites of ON bipolar cells in primate retina

Vardi, Noga; Duvoisin, Robert M.; Wu, George Y.; Sterling, Peter

doi:10.1002/1096-9861(20000731)423:3<402::aid-cne4>3.0.co;2-e

Cited by 192 publications

(155 citation statements)

References 48 publications

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“…3, 4). In primates, mGluR6 is found on all ON-bipolar cell dendrites, at both rod spherules and cone pedicles (Vardi et al, 2000). In the OPL, all HR3-IR puncta associated with the rod spherules were closely associated with mGluR6-IR puncta, but the two proteins did not have precisely the same distribution (Fig.…”

Section: Light and Electron Microscopic Localization Of Hr3 In Monkeymentioning

confidence: 92%

“…All sections were incubated in primary antibody with 0.3% Triton for 3-6 days; flat mounts were incubated for 8-10 days at 4°C. The rabbit polyclonal antibodies were either neat antisera or affinity purified and diluted in PBSa:HR1C (1:2,000-1:5,000, AB5652P; Chemicon, Temecula, CA), HR1CL (1:500-1:2,000, AB5654P; Chemicon), HR2 (1:2,000, AB5656P; Chemicon), HR3C (1:5,000, AB5660P; Chemicon), HR3C (1:1,000-1:5,000 H3R31; ADI, San Antonio, TX), HR3N (1:1,000-1:5,000 H3R32; ADI), and human metabotropic glutamate receptor 6 (mGluR6; 1:1,000; Vardi et al, 2000). Affinity-purified secondary antibodies, biotinylated donkey anti-rabbit, and Cy3-conjugated streptavidin (1:100; Jackson Immunoresearch, West Grove, PA) were applied in succession for 1-2 days at 4°C.…”

Section: Light Microscopymentioning

confidence: 99%

“…Some sections and flat mounts were incubated in a second primary antibody: goat anticholine acetyltransferase (ChAT 1:200, AB144P; Chemicon), mouse anti-GABA A receptor (GABA A R) α-chain (MAB339, clone bd24; Chemicon), mouse anti-human mGluR6 (1:100; Vardi et al, 2000), or mouse anti-tyrosine hydroxylase (TH, 1:10,000; T2928 Sigma, St. Louis, MO). Affinity-purified secondary antibodies conjugated to Alexa 488, donkey antigoat or donkey anti-mouse (1:200; Molecular Probes, Eugene, OR), were applied for 1 day at 4°C.…”

Section: Double Labelingmentioning

confidence: 99%

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Histamine receptors in mammalian retinas

Gastinger

Barber

Vardi

et al. 2006

J of Comparative Neurology

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Mammalian retinas are innervated by histaminergic axons that originate from perikarya in the posterior hypothalamus. To identify the targets of these retinopetal axons, we localized histamine receptors (HR) in monkey and rat retinas by light and electron microscopy. In monkeys, puncta containing HR3 were found at the tips of ON-bipolar cell dendrites in cone pedicles and rod spherules, closer to the photoreceptors than the other neurotransmitter receptors. This is the first ultrastructural localization of any histamine receptor and the first direct evidence that HR3 is present on postsynaptic membranes in the central nervous system. In rat retinas, most HR1 were localized to dopaminergic amacrine cells. The differences in histamine receptor localization may reflect the differences in the activity patterns of the two species. Indexing termsretinopetal; centrifugal; bipolar; amacrine; primate; dopamine Vertebrate retinas receive input from the brain via retinopetal axons, and this pathway has important modulatory effects on retinal neurons in birds and fish, the groups that have been studied most intensively. The functions of retinopetal axons in mammalian retinas are not well understood, however (Uchiyama, 1989). Histamine has been localized to retinopetal axons in the guinea pig (Airaksinen and Panula, 1988), monkey (Gastinger et al., 1999), and rat (Gastinger et al., 2001) retinas. These axons originate from perikarya in the tuberomammillary nucleus of the posterior hypothalamus (Manning et al., 1996;Panula et al., 1989). Mast cells, another possible source of histamine, are not present in the retina (Smelser and Silver, 1963). With the identification of the neurotransmitter of these retinopetal axons, it is now possible to predict how these inputs contribute to information processing in mammalian retinas.These retinopetal axons are expected to be active at night in rats and during the day in monkeys. Histaminergic neurons play an important role in the ascending arousal system (Saper et al., 2001), firing at a steady rate during waking and becoming silent during sleep (Steininger et al., 1999;Vanni-Mercier et al., 2003). In rats, a nocturnal species, histaminergic neurons are most active at night, and the rate of histamine release in the posterior hypothalamus is higher at night than during the day (Prast et al., 1992). In macaques, a diurnal species, levels of histamine metabolites in the third ventricular cerebral spinal fluid are higher during the day than at night (Prell et al., 1989).In the central nervous system, histamine acts on three types of G-protein-coupled receptors: histamine receptor 1 (HR1), histamine receptor 2 (HR2) and histamine receptor 3 (HR3). Among these, only HR1 has been characterized previously in mammalian retinas (Nowak, 1993;Sawai et al., 1988). However, there is indirect evidence that HR2 and HR3 are also present in mammalian retinas. Histamine inhibits a forskolin-induced increase in cAMP in the rabbit retina via HR2 (Nowak, 1991;Nowak et al., 1989). Histamine also increa...

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Section: Light and Electron Microscopic Localization Of Hr3 In Monkeymentioning

confidence: 92%

Section: Light Microscopymentioning

confidence: 99%

Section: Double Labelingmentioning

confidence: 99%

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Histamine receptors in mammalian retinas

Gastinger

Barber

Vardi

et al. 2006

J of Comparative Neurology

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“…mGluR4, mGluR7, and mGluR8 (group III) are also negatively coupled to adenylyl cyclase and are primarily found at the active zone where they are suggested to function as glutamate auto-receptors (10,(11)(12)(13)(14)(15)(16). Of the group III mGluRs the expression of mGluR6 is restricted to the retina, where it is localized postsynaptically at retinal photoreceptor to bipolar cell synapses, transmitting the "light on" signal in visual signal transduction (17,18).…”

mentioning

confidence: 99%

Group I Metabotropic Glutamate Receptors Bind to Protein Phosphatase 1C

Croci

Sticht

Brandstätter

et al. 2003

Journal of Biological Chemistry

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The modulation of neurotransmitter receptors by kinases and phosphatases represents a key mechanism in controlling synaptic signal transduction. However, molecular determinants involved in the specific targeting and interactions of these enzymes are largely unknown. Here, we identified both catalytic ␥-isoforms of protein phosphatase 1C (PP1␥1 and PP1␥2) as binding partners of the group I metabotropic glutamate receptors type 1a, 5a, and 5b in yeast cells and pull-down assays, using recombinant and native protein preparations. The tissue distribution of interacting proteins was compared, and protein phosphatase 1C was detected in dendrites of retinal bipolar cells expressing the respective interacting glutamate receptors. We mapped interacting domains within binding partners and identified five amino acids in the intracellular C termini of the metabotropic glutamate receptors type 1a, 5a, 5b, and 7b being both necessary and sufficient to bind protein phosphatase 1C. Furthermore, we show a dose-dependent competition of these C termini in binding the enzyme. Based on our data, we investigated the structure of the identified amino acids bound to protein phosphatase 1C by homology-based molecular modeling. In summary, these results provide a molecular description of the interaction between protein phosphatase 1C and metabotropic glutamate receptors and thereby increase our understanding of glutamatergic signal transduction.The correct targeting and localization of proteins to synaptic specializations represents an important biological mechanism to regulate neuronal excitability. Increasing evidence underlines the importance of macromolecular signaling complexes, where functionally related proteins such as ion channels, neurotransmitters receptors, kinases, and phosphatases are arranged in close vicinity and are physically anchored to the synaptic cytoskeleton. Therefore, identification and characterization of interactions between synaptically localized proteins adds substantially to our understanding of molecular mechanisms of neurotransmission.Receptors for glutamate are divided in ion channel-associated (ionotropic) receptors of the AMPA-, Kainate-, and NMDAtype and in G-protein coupled (metabotropic) receptors. Although ionotropic glutamate receptors mediate fast synaptic transmission, metabotropic glutamate receptors (mGluRs) 1 modulate neuronal excitability and development, synaptic plasticity, transmitter release, and memory function using a variety of intracellular second messenger systems (1). The eight known members of this protein family are sub-divided into three groups, based on sequence homology, associated second messenger systems, and pharmacological properties (2). mGluR1 and mGluR5 (group I) stimulate phospholipase C, are selectively activated by quisqualate, and are generally expressed perisynaptically at postsynaptic sites (3-7). mGluR2 and mGluR3 (group II) are negatively coupled to adenylyl cyclase and do not show a specific preference for pre-or postsynaptic neurons (8 -10). mGluR4, mGluR7, and...

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“…Tracing the connections of this bipolar cell was further assisted by its affinity for an antibody against cholecystokinin Marshak, 1992, 1997;Wässle et al, 1994), showing that the dendritic tips of this bipolar cell are central elements that invaginate S cones; indeed, this type of bipolar cell provides all the central elements of the S cone . Invaginating central elements express the mGluR6 receptor that depolarizes bipolar cells at light onset (Vardi et al, 2000). Thus, this cell is an ON bipolar cell; in agreement, its axon descends to the ON half of the inner synaptic layer (Mariani, 1984;Marshak, 1992, 1997;Dacey, 1993).…”

Section: Introductionmentioning

confidence: 83%

Evidence That Each S Cone in Macaque Fovea Drives One Narrow-Field and Several Wide-Field Blue-Yellow Ganglion Cells

Schein¹,

Sterling²,

Ngo³

et al. 2004

J. Neurosci.

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A rule of retinal wiring is that many receptors converge onto fewer bipolar cells and still fewer ganglion cells. However, for each S cone in macaque fovea, there are two S-cone ON bipolar cells and two blue-yellow (BY) ganglion cells. To understand this apparent rule reversal, we reconstructed synaptic patterns of divergence and convergence and determined the basic three-tiered unit of connectivity that repeats across the retina. Each foveal S cone diverges to four S-cone ON bipolar cells but contacts them unequally, providing 1-16 ribbon synapses per cell. Next, each bipolar cell diverges to two BY ganglion cells and also contacts them unequally, providing ϳ14 and ϳ28 ribbon synapses per cell. Overall, each S cone diverges to approximately six BY ganglion cells, dominating one and contributing more modestly to the others. Conversely, of each pair of BY ganglion cells, one is dominated by a single S cone and one is diffusely driven by several. This repeating circuit extracts blue/yellow information on two different spatiotemporal scales and thus parallels the circuits for achromatic, spatial vision, in which each cone dominates one narrow-field ganglion cell (midget) and contributes some input to several wider-field ganglion cells (parasol). Finally, because BY ganglion cells have coextensive ϩS and Ϫ(LϩM) receptive fields, and each S cone contributes different weights to different BY ganglion cells, the coextensive receptive fields must be already present in the synaptic terminal of the S cone. The S-cone terminal thus constitutes the first critical locus for BY color vision.

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Localization of mGluR6 to dendrites of ON bipolar cells in primate retina

Cited by 192 publications

References 48 publications

Histamine receptors in mammalian retinas

Histamine receptors in mammalian retinas

Group I Metabotropic Glutamate Receptors Bind to Protein Phosphatase 1C

Evidence That Each S Cone in Macaque Fovea Drives One Narrow-Field and Several Wide-Field Blue-Yellow Ganglion Cells

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