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  • 1
    Keywords: Medicine ; Neurosciences ; Neurobiology ; Biology / Technique ; Biomedicine ; Neurosciences ; Neurobiology ; Biological Techniques ; Springer eBooks
    Description / Table of Contents: Preface -- Production of high-quality antibodies for the study of receptors and ion channels in brain -- Co-immunoprecipitation from brain -- Sub-synaptic membrane fractionation -- Investigation of ℗ neurotransmitter receptors in brain slices using cell surface biotinylation -- Single nanoparticle tracking of surface ion channels and receptors in brain cells -- Radioligand binding detection of receptors in brain membranes -- Recombinant Alphavirus-Mediated Expression of Ion Channels and Receptors in the Brain -- Fluorescent ligands and TR-FRET to study receptor-receptor interactions in the brain -- In situ Proximity Ligation Assay to study and understand the distribution and balance of GPCR homo- and heteroreceptor complexes in the brain -- Fluorescent in situ hybridization for sensitive and specific labeling -- Autoradiographic visualization of G protein-coupled receptors in brain -- Analysis of the expression profile and regional distribution of neurotransmitter receptors and ion channels in the central nervous system using histoblots -- Immunohistochemistry for ion channels and their interacting molecules: Tips for improving antibody accessibility -- Localization of GFP-tagged proteins at the electron microscope -- Pre-embedding methods in the localization of receptors and ion channels -- Post-embedding immunohistochemistry in the localization of receptors and ion channels -- High-Resolution localization of membrane proteins by SDS-digested freeze-fracture replica labelling (SDS-FRL) -- Application of virus vectors for anterograde tract-tracing and single-neuron labeling studies -- Analysis of synaptic connections using viral vectors at the electron microscopic level -- Morphological and neurochemical characterization of electrophysiologically identified cells -- Using electrophysiology to study synaptic and extrasynaptic ionotropic receptors in hippocampal neurons -- Biophysical methods to analyze direct G-protein regulation of neuronal voltage-gated calcium channels -- Electrophysiological recordings in behaving animals -- Voltammetry in behaving animals -- In vivo brain microdialysis of monoamines -- Calcium transients in single dendrites and spines of pyramidal neurons in vitro -- Dynamic recording of membrane potential from hippocampal neurons by using a FRET-based voltage biosensor -- Determination of GPCR-mediated cAMP accumulation in rat striatal synaptosomes -- GPCR-mediated MAPK/ERK cascade activation in brain slices -- Index
    Abstract: Receptor and Ion Channel Detection in the Brain provides state-of-the-art and up-to-date methodological information on molecular, neuroanatomical and functional techniques that are currently used to study neurotransmitter receptors and ion channels in the brain. The chapters have been contributed by world-wide recognized neuroscientists who explain in an easy and detailed way well established and tested protocols embracing molecular, cellular, subcellular, anatomical and electrophysiological aspects of the brain. This comprehensive and practical manual is presented in a simple, step-by-step manner for laboratory use, and also offers unambiguous detail and key implementation advice that proves essential for successful results and facilitate choosing the best method for the target proteins under study. This work serves as a useful guide for young researchers and students in training as well as for neurologists and established scientists who wish to extend their repertoire of techniques
    Pages: XVIII, 475 p. 84 illus., 57 illus. in color. : online resource.
    ISBN: 9781493930647
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  • 2
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Adenosine deaminase is an enzyme of purine metabolism that has largely been considered to be cytosolic. A few years ago, adenosine deaminase was reported to appear on the surface of cells. Recently, it has been demonstrated that adenosine deaminase interacts with a type II membrane protein known as either CD26 or dipeptidylpeptidase IV. In this study, by immunoprecipitation and affinity chromatography it is shown that adenosine deaminase and A1 adenosine receptors interact in pig brain cortical membranes. This is the first report in brain demonstrating an interaction between a degradative ectoenzyme and the receptor whose ligand is the enzyme substrate. By means of this interaction adenosine deaminase leads to the appearance of the high-affinity site of the receptor, which corresponds to the receptor-G protein complex. Thus, it seems that adenosine deaminase is necessary for coupling A1 adenosine receptors to heterotrimeric G proteins.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Adenosine, by acting on adenosine A1 and A2A receptors, exerts opposite modulatory roles on striatal extracellular levels of glutamate and dopamine, with activation of A1 inhibiting and activation of A2A receptors stimulating glutamate and dopamine release. Adenosine-mediated modulation of striatal dopaminergic neurotransmission could be secondary to changes in glutamate neurotransmission, in view of evidence for a preferential colocalization of A1 and A2A receptors in glutamatergic nerve terminals. By using in vivo microdialysis techniques, local perfusion of NMDA (3, 10 µm), the selective A2A receptor agonist 2-p-(2-carboxyethyl)phenethylamino-5′-N-ethylcarboxamidoadenosine (CGS 21680; 3, 10 µm), the selective A1 receptor antagonist 8-cyclopentyl-1,3-dimethylxanthine (CPT; 300, 1000 µm), or the non-selective A1-A2A receptor antagonist in vitro caffeine (300, 1000 µm) elicited significant increases in extracellular levels of dopamine in the shell of the nucleus accumbens (NAc). Significant glutamate release was also observed with local perfusion of CGS 21680, CPT and caffeine, but not NMDA. Co-perfusion with the competitive NMDA receptor antagonist dl-2-amino-5-phosphonovaleric acid (APV; 100 µm) counteracted dopamine release induced by NMDA, CGS 21680, CPT and caffeine. Co-perfusion with the selective A2A receptor antagonist MSX-3 (1 µm) counteracted dopamine and glutamate release induced by CGS 21680, CPT and caffeine and did not modify dopamine release induced by NMDA. These results indicate that modulation of dopamine release in the shell of the NAc by A1 and A2A receptors is mostly secondary to their opposite modulatory role on glutamatergic neurotransmission and depends on stimulation of NMDA receptors. Furthermore, these results underscore the role of A1 vs. A2A receptor antagonism in the central effects of caffeine.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Recent evidence suggest that many G protein-coupled receptors (GPCR) and signalling molecules localize in microdomains of the plasma membrane. In this study, flotation gradient analysis in the absence of detergents demonstrated the presence of the metabotropic glutamate receptor type 1α (mGlu1α) in low-density caveolin-enriched membrane fractions (CEMF) in permanently transfected BHK cells. BHK-1α cells exhibit a similar pattern of staining for caveolin-1 and caveolin-2, and these two proteins show a high degree of co-localization with mGlu1α receptor as demonstrated by immunogold and confocal laser microscopy. The presence of mGlu1α in CEMF was also demonstrated by co-immunoprecipitation of mGlu1α receptor using antibodies against caveolin proteins. Activation of the mGlu1α receptor by agonist increased extracellular signal-regulated kinases phosphorylation in CEMF and not in high-density membrane fractions (HDMF), suggesting that mGlu1α receptor-mediated signal transduction could occur in caveolae-like domains. Overall, these results clearly show a molecular and functional association of mGlu1α receptor with caveolins.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The results presented in this paper show that adenosine A2A receptor (A2AR) form homodimers and that homodimers but not monomers are the functional species at the cell surface. Fluorescence resonance energy transfer (FRET) and bioluminescence resonance energy transfer (BRET) techniques have been used to demonstrate in transfected HEK293 cells homodimerization of A2AR, which are heptaspanning membrane receptors with enriched expression in striatum. The existence of homodimers at the cell surface was demonstrated by time-resolved FRET. Although agonist activation of the receptor leads to the formation of receptor clusters, it did not affect the degree of A2AR–A2AR dimerization. Both monomers and dimers were detected by immunoblotting in cell extracts. However, cell surface biotinylation of proteins has made evident that more than 90% of the cell surface receptor is in its dimeric form. Thus, it seems that homodimers are the functional form of the receptor present on the plasma membrane. A deletion mutant version of the A2A receptor, lacking its C-terminal domain, was also able to form both monomeric and dimeric species when cell extracts from transfected cells were analyzed by immunoblotting. This suggests that the C-terminal tail does not participate in the dimerization. This is relevant as the C-terminal tail of A2AR is involved in heteromers formed by A2AR and dopamine D2 receptors. BRET ratios corresponding to A2AR–A2AR homodimers were higher than those encountered for heterodimers formed by A2AR and dopamine D2 receptors. As A2AR and dopamine D2 receptors do indeed interact, these results indicate that A2AR homodimers are the functional species at the cell surface and that they coexist with A2AR/D2 receptor heterodimers.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Metabotropic glutamate receptors (mGlu receptors) are coupled to G-protein second messenger pathways and modulate glutamate neurotransmission in the brain, where they are targeted to specific synaptic locations. Very recently, we identified tubulin as an interacting partner of the mGlu1α receptor in rat brain. Using BHK-570 cells permanently expressing the receptor we have shown that this interaction occurs predominantly with soluble tubulin, following its translocation to the plasma membrane. In addition, treatment of the cells with the agonist quisqualic acid induce tubulin depolimerization and its translocation to the plasma membrane. Immunofluorescence detection of both the receptor and tubulin in agonist-treated cells reveals a disruption of the microtubule network and an increased clustering of the receptor. Collectively these data demonstrate that the mGlu1α receptor interacts with soluble tubulin and that this association can take place at the plasma membrane.
    Type of Medium: Electronic Resource
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