Association of Neuropeptide Receptors with Central Catecholamine Neurons: Light and Electron Microscopic Investigations

Beaudet, Alain; Moyse, Emmanuel; Szigethy, Eva; Marcel, Dominique; Leonard, Kathleen A.; Dana, C; Rostène, William

doi:10.1007/978-1-349-10726-1_10

Cited by 4 publications

(6 citation statements)

References 12 publications

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“…Indeed, -23% of shared grains were found at synapses, as compared with <l0o for , sites and 2% for 8 sites in the same region of rat brain (13)(14)(15). In fact, of all peptide receptors visualized to date by EM none has yet demonstrated a comparable concentration at synaptic junctions (16,23,41). The question arises whether terminals implicated in these synapses contain and release prodynorphin derivatives, which are currently recognized as most likely to act at central K sites (42)(43)(44).…”

Section: Discussionmentioning

confidence: 99%

“…Given the size of 125I-DPDYN-labeled perikarya and the frequent association of the label with dendritic spines, a proportion of K receptors is likely to be associated with medium spiny neurons. It is interesting in this regard that a subpopulation of medium spiny neurons in rat (16,(34)(35)(36)(37) and hamster (36) neostriatum contains peptides of the dynorphin family, suggesting that some of the labeled binding sites might represent autoreceptors.…”

Section: Discussionmentioning

confidence: 99%

“…Light microscopic and film radioautographic studies have demonstrated distinct distributional patterns for each opioid receptor type in mammalian brain (8)(9)(10)(11)(12). In contrast, EM data have shown ,u and 8 receptors to share similar distributional features, characterized by a fairly widespread dispersion along neuronal plasma membranes and a low synaptic incidence (13)(14)(15)(16). These findings raise the question whether K sites, which on biochemical (17), pharmacological (3), and electrophysiological (18) grounds appear further distinct from ,u and 8 sites than the latter two from one another, also differ in their ultrastructural distribution.…”

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confidence: 99%

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Synaptic localization of kappa opioid receptors in guinea pig neostriatum.

Jomary

Gairin

Beaudet

1992

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

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Distribution of K opioid receptors was examined by EM radioautography in sections of guinea pig neostriatum with the selective 12SI-labeled dynorphin analog . Most specifically labeled binding sites were found by probability circle analysis to be associated with neuronal membrane appositions. Because of limitations in resolution of the method, the radioactive sources could not be ascribed directly to either one of the apposed plasma membranes. Nevertheless, three lines of evidence favored a predominant association of ligand with dendrites of intrinsic striatal neurons: (i) the high frequency with which labeled interfaces implicated a dendrite, (il) the enrichment of dendrodendritic interfaces, and (iii) the occurrence of dendritic profiles labeled at several contact points along their plasma membranes. A small proportion of labeled sites was associated with axo-axonic interfaces, which may subserve the K opioidinduced regulation of presynaptic dopamine and acetylcholine release documented in guinea pig neostriatum. Although most membrane-associated K sites were found at extrasynaptic locations, -23% were associated with synaptic specializations. This proportion is markedly higher than that previously reported for either ,u or 6 sites in rat neostriatum. Whether labeled synapses represent preferential sites of action for K ligands remains to be established. In any event, these results support the hypothesis that in mammalian brain K opioid receptors are conformationally and functionally distinct from ,u and 6 types.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Synaptic localization of kappa opioid receptors in guinea pig neostriatum.

Jomary

Gairin

Beaudet

1992

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

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“…Furthermore, the "ζ opioid growth factor receptor" has been reported to be localized in nuclei of rat cerebellar cells (Zagon et al, 1993). EM-autoradiographic evidence for intracellular opioid sites was provided by Beaudet et al (1989). In subsequent experiments using a photoaffinity probe (azido-DTLET), the same group discovered only 44% of the labeled δ binding sites were on neuronal plasma membranes in rat neostriatum while the remainder was associated with the cytoplasm of axons (Pasquini et al, 1992).…”

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confidence: 99%

Agonist-Induced Desensitization and Down-Regulation of δ Opioid Receptors Alter the Levels of Their ¹²⁵I-β-Endorphin Cross-Linked Products in Subcellular Fractions from NG108-15 Cells

Belcheva

Ignatova²,

Young³

et al. 1996

Biochemistry

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The delta opioid binding sites in subcellular fractions from NG108-15 cells were characterized with respect to their relative molecular size and levels under conditions of receptor adaptation. 125I-beta-Endorphin was cross-linked to preparations enriched in plasma membranes (P20), nuclear membranes or nuclear matrices. Five cross-linked bands appear in all subcellular fractions. The largest molecular size reaction product in nuclear matrix preparations (approximately 72 kDa) differed from that in the other two fractions-(approximately 83 kDa). Immunoblot analyses with an antibody to the delta opioid receptor gave a P20 band pattern similar to that for the corresponding cross-linked products. To determine which cross-linked products in P20 are glycoproteins, labeled membranes were solubilized and purified by wheat germ agglutinin chromatography. The absence of a approximately 36 kDa band after purification suggests that this product is not a glycoprotein. The remaining four bands were present in N-acetyl-D-glucosamine eluates, although their % distribution changes in favor of the largest molecular size band (approximately 83 kDa). Immunoblotting of the eluate gave a single diffuse band at approximately 73 kDa, suggesting the native glycoprotein has a molecular size in the 70-80 kDa range. Etorphine-induced desensitization of cell surface receptors increased the amount of some cross-linked products associated with nuclear membranes. The same treatment did not affect the relative density of the four larger molecular size bands in P20, but increased the density of the approximately 26 kDa product two fold. Etorphine-induced down-regulation evoked an elevation of cross-linked products in nuclear matrix preparations, while all band densities of P20 were diminished. These results suggest that nuclear matrix associated opioid binding sites represent internalized, truncated forms of the glycosylated delta opioid receptor found in P20.

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“…Many studies have revealed that the nuclear envelope is functionally a specialized form of ER. Beaudet and coworkers (Hamel and Beaudet, 1987;Beaudet et al, 1989) provided EMautoradiographic data for the association of intracellular opioid binding sites with the ER and Golgi apparatus, while an additional contingent was associated with the nucleus or nuclear membrane. Nuclear opioid binding sites have also been invoked in a hypothesis on long-term memory (Laduron, 1987).…”

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Novel opioid binding sites associated with nuclei of NG108-15 neurohybrid cells

et al. 1993

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Nuclear opioid binding sites have been discovered in NG108-15 neurohybrid cells. Marker enzyme analyses as well as electron and fluorescence microscopy studies attested to the high degree of purity of the nuclear preparations. Immunohistochemical studies on cryostat sections of NG108-15 cells with an antibody to the opioid receptor corroborated a nuclear localization. 3H-[D-Pen2,D-Pen5]enkephalin (3H-DPDPE), 3H-[D-Ala2,D-Leu5]enkephalin (3H-DADLE), and 3H-diprenorphine binding parameters, Kd and Bmax values, and heterologous competition binding and stereospecificity data satisfied criteria for the presence of delta-opioid sites in purified nuclear preparations. Neither mu-([D-Ala2,mephe4,gly-ol5] enkephalin), dihydromorphine, nor kappa-(U69593) specific binding was detectable in purified nuclear preparations. Rates of association and dissociation of 3H-[D-Ser2,L-Leu5]enkephalyl-Thr were comparable to values obtained previously for opioid receptors. Opioid binding was also shown in subnuclear preparations from NG108-15 cell cultures. Agonists, 3H-DADLE and 3H-DPDPE, bind with high affinity to nuclear membranes and with lower affinity to chromatin. In contrast, partial agonist 3H-diprenorphine high-affinity binding sites were predominant in chromatin, while low-affinity binding was found in the nuclear membrane. Accordingly, 5'-guanylylimidodiphosphate sensitivity of 3H-DADLE binding was detected in nuclear membranes but not in chromatin. Both agonist and partial agonist opioid binding to nuclear membrane and chromatin were abolished upon cycloheximide treatment of NG108-15 cells. Taken together, the results suggest that NG108-15 cells contain newly synthesized GTP binding regulatory protein (G-protein)-coupled delta-opioid receptors in nuclear membranes and uncoupled opioid binding sites in chromatin.

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Association of Neuropeptide Receptors with Central Catecholamine Neurons: Light and Electron Microscopic Investigations

Cited by 4 publications

References 12 publications

Synaptic localization of kappa opioid receptors in guinea pig neostriatum.

Synaptic localization of kappa opioid receptors in guinea pig neostriatum.

Agonist-Induced Desensitization and Down-Regulation of δ Opioid Receptors Alter the Levels of Their ¹²⁵I-β-Endorphin Cross-Linked Products in Subcellular Fractions from NG108-15 Cells

Novel opioid binding sites associated with nuclei of NG108-15 neurohybrid cells

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Association of Neuropeptide Receptors with Central Catecholamine Neurons: Light and Electron Microscopic Investigations

Cited by 4 publications

References 12 publications

Synaptic localization of kappa opioid receptors in guinea pig neostriatum.

Synaptic localization of kappa opioid receptors in guinea pig neostriatum.

Agonist-Induced Desensitization and Down-Regulation of δ Opioid Receptors Alter the Levels of Their 125I-β-Endorphin Cross-Linked Products in Subcellular Fractions from NG108-15 Cells

Novel opioid binding sites associated with nuclei of NG108-15 neurohybrid cells

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Agonist-Induced Desensitization and Down-Regulation of δ Opioid Receptors Alter the Levels of Their ¹²⁵I-β-Endorphin Cross-Linked Products in Subcellular Fractions from NG108-15 Cells