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  1. Article: Glutamate heteroreceptor complexes in the brain.

    Borroto-Escuela, Dasiel O / Tarakanov, Alexander O / Brito, Ismel / Fuxe, Kjell

    Pharmacological reports : PR

    2018  Volume 70, Issue 5, Page(s) 936–950

    Abstract: The existence of mGluR, NMDAR, AMPAR and putative KAR heteroreceptor complexes in synaptic and extrasynaptic regions of brain glutamate synapses represents a major integrative mechanism. Our aim in the current article is to analyze if the formation of ... ...

    Abstract The existence of mGluR, NMDAR, AMPAR and putative KAR heteroreceptor complexes in synaptic and extrasynaptic regions of brain glutamate synapses represents a major integrative mechanism. Our aim in the current article is to analyze if the formation of the different types glutamate hetereceptor complexes involves the contribution of triplet amino acid homologies (protriplets) in a postulated receptor interface based on the triplet puzzle theory. Seven main sets (lists) of receptor pairs in databases were used containing various sets (lists) of human receptor heteromers and nonheteromers obtained from the available scientific publications including the publically available GPCR-hetnet database. Brain mGluR1-mGluR5 and mGluR2-mGluR4 isoreceptor complexes were demonstrated with a predominant extrasynaptic localization at a post- and prejunctional localization. The existence of putative mGluR4-mGluR7 heteroreceptor complexes in the basal ganglia is proposed. Metabotropic glutamate receptor subtypes also participated in the formation of a large number of heteroreceptor complexes like mGluR1-A1R, mGluR5-A2AR, mGluR5-D2R and D2R-A2AR-mGluR5, located in relation to glutamate synapses, especially in the basal ganglia. A putative mGluR1-GABAB1/2 heterocomplex may also exist. NMDAR heteroreceptor complexes were also demonstrated as a fundamental integrative mechanism in the glutamate synapse and its extrasynaptic membranes. It represented fundamental work on inter alia NMDAR-mGluR5, NMDAR-D1R and NMDAR-D2R heteroreceptor complexes involving both antagonistic and facilitatory allosteric receptor-receptor interactions. As to AMPA receptors, a heterocomplex was found for the interaction between IFNgR1 and the AMPAR mediated via the subunit GluA1 which may be of relevance for neuroinflammation. AMPAR-D2R heteroreceptor complexes were also demonstrated. Besides glutamate heteroreceptor complexes and their allosteric receptor-receptor interactions, a significant mechanism for the functional crosstalk can also be phosphorylation and/or reorganization of adapter proteins with dynamic binding to the two receptors modulating the allosteric receptor mechanism.
    MeSH term(s) Animals ; Brain/metabolism ; Humans ; Multiprotein Complexes/metabolism ; Protein Isoforms/metabolism ; Receptors, Glutamate/metabolism ; Sequence Homology, Amino Acid
    Chemical Substances Multiprotein Complexes ; Protein Isoforms ; Receptors, Glutamate
    Language English
    Publishing date 2018-04-11
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2186248-5
    ISSN 1734-1140
    ISSN 1734-1140
    DOI 10.1016/j.pharep.2018.04.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 861: Show issues Location:
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  2. Article ; Online: Receptor⁻Receptor Interactions in Multiple 5-HT1A Heteroreceptor Complexes in Raphe-Hippocampal 5-HT Transmission and Their Relevance for Depression and Its Treatment.

    Borroto-Escuela, Dasiel O / Narváez, Manuel / Ambrogini, Patrizia / Ferraro, Luca / Brito, Ismel / Romero-Fernandez, Wilber / Andrade-Talavera, Yuniesky / Flores-Burgess, Antonio / Millon, Carmelo / Gago, Belen / Narvaez, Jose Angel / Odagaki, Yuji / Palkovits, Miklos / Diaz-Cabiale, Zaida / Fuxe, Kjell

    Molecules (Basel, Switzerland)

    2018  Volume 23, Issue 6

    Abstract: Due to the binding to a number of proteins to the receptor protomers in receptor heteromers in the brain, the term "heteroreceptor complexes" was introduced. A number of serotonin 5-HT1A heteroreceptor complexes were recently found to be linked to the ... ...

    Abstract Due to the binding to a number of proteins to the receptor protomers in receptor heteromers in the brain, the term "heteroreceptor complexes" was introduced. A number of serotonin 5-HT1A heteroreceptor complexes were recently found to be linked to the ascending 5-HT pathways known to have a significant role in depression. The 5-HT1A⁻FGFR1 heteroreceptor complexes were involved in synergistically enhancing neuroplasticity in the hippocampus and in the dorsal raphe 5-HT nerve cells. The 5-HT1A protomer significantly increased FGFR1 protomer signaling in wild-type rats. Disturbances in the 5-HT1A⁻FGFR1 heteroreceptor complexes in the raphe-hippocampal 5-HT system were found in a genetic rat model of depression (Flinders sensitive line (FSL) rats). Deficits in FSL rats were observed in the ability of combined FGFR1 and 5-HT1A agonist cotreatment to produce antidepressant-like effects. It may in part reflect a failure of FGFR1 treatment to uncouple the 5-HT1A postjunctional receptors and autoreceptors from the hippocampal and dorsal raphe GIRK channels, respectively. This may result in maintained inhibition of hippocampal pyramidal nerve cell and dorsal raphe 5-HT nerve cell firing. Also, 5-HT1A⁻5-HT2A isoreceptor complexes were recently demonstrated to exist in the hippocampus and limbic cortex. They may play a role in depression through an ability of 5-HT2A protomer signaling to inhibit the 5-HT1A protomer recognition and signaling. Finally, galanin (1⁻15) was reported to enhance the antidepressant effects of fluoxetine through the putative formation of GalR1⁻GalR2⁻5-HT1A heteroreceptor complexes. Taken together, these novel 5-HT1A receptor complexes offer new targets for treatment of depression.
    MeSH term(s) Animals ; Depression/drug therapy ; Depression/metabolism ; Protein Binding ; Raphe Nuclei/metabolism ; Rats, Sprague-Dawley ; Receptor, Fibroblast Growth Factor, Type 1/metabolism ; Receptor, Serotonin, 5-HT1A/metabolism ; Serotonin/metabolism
    Chemical Substances Receptor, Serotonin, 5-HT1A (112692-38-3) ; Serotonin (333DO1RDJY) ; Fgfr1 protein, rat (EC 2.7.10.1) ; Receptor, Fibroblast Growth Factor, Type 1 (EC 2.7.10.1)
    Language English
    Publishing date 2018-06-03
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules23061341
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.MO 81: Show issues

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  3. Article ; Online: The G protein-coupled receptor heterodimer network (GPCR-HetNet) and its hub components.

    Borroto-Escuela, Dasiel O / Brito, Ismel / Romero-Fernandez, Wilber / Di Palma, Michael / Oflijan, Julia / Skieterska, Kamila / Duchou, Jolien / Van Craenenbroeck, Kathleen / Suárez-Boomgaard, Diana / Rivera, Alicia / Guidolin, Diego / Agnati, Luigi F / Fuxe, Kjell

    International journal of molecular sciences

    2014  Volume 15, Issue 5, Page(s) 8570–8590

    Abstract: G protein-coupled receptors (GPCRs) oligomerization has emerged as a vital characteristic of receptor structure. Substantial experimental evidence supports the existence of GPCR-GPCR interactions in a coordinated and cooperative manner. However, despite ... ...

    Abstract G protein-coupled receptors (GPCRs) oligomerization has emerged as a vital characteristic of receptor structure. Substantial experimental evidence supports the existence of GPCR-GPCR interactions in a coordinated and cooperative manner. However, despite the current development of experimental techniques for large-scale detection of GPCR heteromers, in order to understand their connectivity it is necessary to develop novel tools to study the global heteroreceptor networks. To provide insight into the overall topology of the GPCR heteromers and identify key players, a collective interaction network was constructed. Experimental interaction data for each of the individual human GPCR protomers was obtained manually from the STRING and SCOPUS databases. The interaction data were used to build and analyze the network using Cytoscape software. The network was treated as undirected throughout the study. It is comprised of 156 nodes, 260 edges and has a scale-free topology. Connectivity analysis reveals a significant dominance of intrafamily versus interfamily connections. Most of the receptors within the network are linked to each other by a small number of edges. DRD2, OPRM, ADRB2, AA2AR, AA1R, OPRK, OPRD and GHSR are identified as hubs. In a network representation 10 modules/clusters also appear as a highly interconnected group of nodes. Information on this GPCR network can improve our understanding of molecular integration. GPCR-HetNet has been implemented in Java and is freely available at http://www.iiia.csic.es/~ismel/GPCR-Nets/index.html.
    MeSH term(s) Algorithms ; Cluster Analysis ; Databases, Protein ; Dimerization ; Humans ; Internet ; Metabolic Networks and Pathways ; Models, Molecular ; Receptors, G-Protein-Coupled/chemistry ; Receptors, G-Protein-Coupled/metabolism ; User-Computer Interface
    Chemical Substances Receptors, G-Protein-Coupled
    Language English
    Publishing date 2014-05-14
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms15058570
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Dopamine D2 receptor signaling dynamics of dopamine D2-neurotensin 1 receptor heteromers

    Borroto-Escuela, Dasiel O / Ravani, Annalisa / Tarakanov, Alexander O / Brito, Ismel / Narvaez, Manuel / Romero-Fernandez, Wilber / Corrales, Fidel / Agnati, Luigi F / Tanganelli, Sergio / Ferraro, Luca / Fuxe, Kjell

    Biochemical and biophysical research communications. 2013 May 24, v. 435, no. 1

    2013  

    Abstract: Biochemical, histochemical and coimmunoprecipitation experiments have indicated the existence of antagonistic dopamine D2 (D₂R) and neurotensin 1 (NTS1R) receptor–receptor interactions in the dorsal and ventral striatum indicating a potential role of ... ...

    Abstract Biochemical, histochemical and coimmunoprecipitation experiments have indicated the existence of antagonistic dopamine D2 (D₂R) and neurotensin 1 (NTS1R) receptor–receptor interactions in the dorsal and ventral striatum indicating a potential role of these receptor–receptor interactions in Parkinson’s disease and schizophrenia. By means of Bioluminiscence Resonance energy transfer (BRET²) evidence has for the first time been obtained in the current study for the existence of both D₂LR/NTS1R and D₂SR/NTS1R heteromers in living HEK293T cells. Through confocal laser microscopy the NTS1RᴳFᴾ² and D2RYFᴾ were also shown to be colocated in the plasma membrane of these cells. A bioinformatic analysis suggests the existence of a basic set of three homology protriplets (TVM, DLL and/or LRA) in the two participating receptors which may contribute to the formation of the D₂R/NTS1R heteromers by participating in guide–clasp interactions in the receptor interface. The CREB reporter gene assay indicated that the neurotensin receptor agonist JMV 449 markedly reduced the potency of the D₂R like agonist quinpirole to inhibit the forskolin induced increase of the CREB signal. In contrast, the neurotensin agonist was found to markedly increase the quinpirole potency to activate the MAPK pathway as also studied with luciferase reporter gene assay measuring the degree of SRE activity as well as with ERK1/2 phosphorylation assays. These dynamic changes in D₂R signaling produced by the neurotensin receptor agonist may involve antagonistic allosteric receptor–receptor interactions in the D₂LR–NTS1R heteromers at the plasma membrane level (CREB pathway) and synergistic interactions in PKC activation at the cytoplasmatic level (MAPK pathway).
    Keywords Parkinson disease ; agonists ; bioinformatics ; confocal laser scanning microscopy ; dopamine ; dopamine receptors ; energy transfer ; forskolin ; luciferase ; mitogen-activated protein kinase ; phosphorylation ; plasma membrane ; protein kinase C ; reporter genes ; schizophrenia
    Language English
    Dates of publication 2013-0524
    Size p. 140-146.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2013.04.058
    Database NAL-Catalogue (AGRICOLA)

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  5. Article ; Online: Dopamine D2 receptor signaling dynamics of dopamine D2-neurotensin 1 receptor heteromers.

    Borroto-Escuela, Dasiel O / Ravani, Annalisa / Tarakanov, Alexander O / Brito, Ismel / Narvaez, Manuel / Romero-Fernandez, Wilber / Corrales, Fidel / Agnati, Luigi F / Tanganelli, Sergio / Ferraro, Luca / Fuxe, Kjell

    Biochemical and biophysical research communications

    2013  Volume 435, Issue 1, Page(s) 140–146

    Abstract: Biochemical, histochemical and coimmunoprecipitation experiments have indicated the existence of antagonistic dopamine D2 (D2R) and neurotensin 1 (NTS1R) receptor-receptor interactions in the dorsal and ventral striatum indicating a potential role of ... ...

    Abstract Biochemical, histochemical and coimmunoprecipitation experiments have indicated the existence of antagonistic dopamine D2 (D2R) and neurotensin 1 (NTS1R) receptor-receptor interactions in the dorsal and ventral striatum indicating a potential role of these receptor-receptor interactions in Parkinson's disease and schizophrenia. By means of Bioluminiscence Resonance energy transfer (BRET(2)) evidence has for the first time been obtained in the current study for the existence of both D2LR/NTS1R and D2SR/NTS1R heteromers in living HEK293T cells. Through confocal laser microscopy the NTS1R(GFP2) and D2R(YFP) were also shown to be colocated in the plasma membrane of these cells. A bioinformatic analysis suggests the existence of a basic set of three homology protriplets (TVM, DLL and/or LRA) in the two participating receptors which may contribute to the formation of the D2R/NTS1R heteromers by participating in guide-clasp interactions in the receptor interface. The CREB reporter gene assay indicated that the neurotensin receptor agonist JMV 449 markedly reduced the potency of the D2R like agonist quinpirole to inhibit the forskolin induced increase of the CREB signal. In contrast, the neurotensin agonist was found to markedly increase the quinpirole potency to activate the MAPK pathway as also studied with luciferase reporter gene assay measuring the degree of SRE activity as well as with ERK1/2 phosphorylation assays. These dynamic changes in D2R signaling produced by the neurotensin receptor agonist may involve antagonistic allosteric receptor-receptor interactions in the D2LR-NTS1R heteromers at the plasma membrane level (CREB pathway) and synergistic interactions in PKC activation at the cytoplasmatic level (MAPK pathway).
    MeSH term(s) Bioluminescence Resonance Energy Transfer Techniques/methods ; Cell Membrane/metabolism ; Dopamine Agonists/pharmacology ; Dopamine Antagonists/pharmacology ; Dose-Response Relationship, Drug ; HEK293 Cells ; Humans ; Kinetics ; Luminescent Proteins/genetics ; Luminescent Proteins/metabolism ; Microscopy, Confocal ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 3/metabolism ; Models, Molecular ; Oligopeptides/pharmacology ; Phosphorylation/drug effects ; Protein Binding/drug effects ; Protein Multimerization ; Protein Structure, Tertiary ; Pyrazoles/pharmacology ; Quinolines/pharmacology ; Quinpirole/pharmacology ; Raclopride/pharmacology ; Receptors, Dopamine D2/chemistry ; Receptors, Dopamine D2/genetics ; Receptors, Dopamine D2/metabolism ; Receptors, Neurotensin/chemistry ; Receptors, Neurotensin/genetics ; Receptors, Neurotensin/metabolism ; Signal Transduction
    Chemical Substances Dopamine Agonists ; Dopamine Antagonists ; Luminescent Proteins ; Oligopeptides ; Pyrazoles ; Quinolines ; Receptors, Dopamine D2 ; Receptors, Neurotensin ; SR 142948 ; neurotensin type 1 receptor ; JMV 449 (139026-66-7) ; Quinpirole (20OP60125T) ; Raclopride (430K3SOZ7G) ; MAPK1 protein, human (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase 1 (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase 3 (EC 2.7.11.24)
    Language English
    Publishing date 2013-05-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2013.04.058
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 116: Show issues Location:
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