Tesis sobre el tema "Cyclic nucleotide-gated channel"
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Cukkemane, Abhishek. "Structural and functional studies of a prokaryotic cyclic nucleotide gated channel /". Jülich : Forschungszentrum, Zentralbibliothek, 2008. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=016779692&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.
Texto completoSunderman, Elizabeth R. "Single-channel kinetic analysis of the allosteric transition of rod cyclic nucleotide-gated channels /". Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/10526.
Texto completoMatulef, Kimberly Irene. "Cysteine-scanning mutagenesis of the ligand-binding domain of cyclic nucleotide-gated channels /". Thesis, Connect to this title online; UW restricted, 2002. http://hdl.handle.net/1773/5032.
Texto completoLolicato, M. G. L. "STRUCTURAL STUDIES ON THE REGULATORY DOMAIN OF THREE HCN (HYPERPOLARIZATION-ACTIVATED CYCLIC NUCLEOTIDE-GATED) CHANNEL ISOFORMS". Doctoral thesis, Università degli Studi di Milano, 2012. http://hdl.handle.net/2434/168356.
Texto completoBecirovic, Elvir. "Role of the CNGB1a Subunit of the Rod Cyclic Nucleotide-Gated Channel in Channel Gating and Pathogenesis of Retinitis Pigmentosa". Diss., lmu, 2010. http://nbn-resolving.de/urn:nbn:de:bvb:19-119088.
Texto completoTanaka, Naoto. "A MISSENSE MUTATION IN CONE PHOTORECEPTOR CYCLIC NUCLEOTIDE-GATED CHANNELS ASSOCIATED WITH CANINE DAYLIGHT BLINDNESS OFFERS INSIGHT INTO CHANNEL STRUCTURE AND FUNCTION". Diss., Temple University Libraries, 2013. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/246634.
Texto completoPh.D.
Cone cyclic nucleotide-gated (CNG) channels are located in the retinal outer segments, mediating daylight color vision. The channel is a tetramer of A-type (CNGA3) and B-type (CNGB3) subunits. CNGA3 subunits are able to form homotetrameric channels, but CNGB3 exhibits channel function only when co-expressed with CNGA3. Mutations in the genes encoding these cone CNG subunits are associated with achromatopsia, an autosomal recessive genetic disorder which causes incomplete or complete loss of daylight and color vision. A missense mutation, aspartatic acid (Asp) to asparagine (Asn) at position 262 in the canine CNGB3 subunit (cB3-D262N), results in loss of cone function and therefore daylight blindness, highlighting the crucial role of this aspartic acid residue for proper channel biogenesis and/or function. Asp 262 is located in a conserved region of the second transmembrane segment containing three Asp residues designated the Tri-Asp motif. We exploit the conservation of these residues in CNGA3 subunits to examine the motif using a combination of experimental and computational approaches. Mutations of these conserved Asp residues result in a loss of nucleotide-activated currents and mislocalization in heterologous expression. Co-expressing CNGB3 Tri-Asp mutants with wild type CNGA3 results in functional channels, however, their electrophysiological characterization matches the properties of homomeric CNGA3 tetramers. This failure to record heteromeric currents implies that Asp/Asn mutations impact negatively both CNGA3 and CNGB3 subunits. A homology model of canine CNGA3 relaxed in a membrane using molecular dynamics simulations suggests that the Tri-Asp motif is involved in non-specific salt bridge pairings with positive residues of S3 - S4. We propose that the CNGB3-D262N mutation in daylight blind dogs results in the loss of these interactions and leads to an alteration of the electrostatic equilibrium in the S1 - S4 bundle. Because residues analogous to Tri-Asp residues in the voltage-gated Shaker K+ channel superfamily were implicated in monomer folding, we hypothesize that destabilizing these electrostatic interactions might impair the monomer folding state in D262N mutant CNG channels during biogenesis. Another missesnse sense mutation, Arginine (Arg) to tryptophan (Trp) at position 424 in the canine CNGA3 subunit (cA3-R424W), also results in loss of cone function. An amino acid sequence alignment with Shaker K+ channel superfamily indicates that this R424 residue is located in the C-terminal end of the sixth transmembrane segment. A3-R424W mutant channels resulted in no cyclic nucleotide-activated currents and mislocalization with intracellular aggregates. However, the localization of cA3-R424W mutant channels was not affected as severely as the Asp/Asn mutation in S2 Tri-Asp motif, showing a lot of cells with the proper localization of Golgi-like and membrane fluorescence. Moreover, the substitution of Arg 424 to Lysine (Lys), conserving the positive charge, preserved channel function in some cells, which is different from the results of the S2 Tri-Asp motif in which the Asp/Glu substitutions, conserving the negative charge, leads to loss of cyclic nucleotide-activated currents. Even though these missense mutations are both associated with canine daylight blindness, the Arg 424 residue might not be as critical for folding as the Tri-Asp residues in the S2 Tri-Asp motif and might be more of a problem in channel structure and function. The cA3 model relaxed with MD simulations indicated a possible interaction of Arg 424 with the Glu 304 residue in the S4-S5 linker. This hypothesis is supported by electrophysiological data in which the double mutation of reversing these residues, Glu 306 to Arg and Arg 424 to Glu (E306R-R424E) preserves channel function. In the model, this salt bridge appears to contribute to stabilization of the open pore state. The R424W mutation might disrupt the salt bridge formation, leading to deforming and closing the pore region.
Temple University--Theses
Schünke, Sven Verfasser], Dieter [Akademischer Betreuer] [Willbold y Lutz [Akademischer Betreuer] Schmitt. "NMR solution structures of the MloK1 cyclic nucleotide-gated ion channel binding domain / Sven Schünke. Gutachter: Lutz Schmitt. Betreuer: Dieter Willbold". Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2011. http://d-nb.info/1015434975/34.
Texto completoHundal, Sukhinder Paul Singh. "Molecular cloning, characterisation and function expression of cyclic nucleotide-gated ion channel genes expressed in sino-atrial node region of heart". Thesis, University of Leicester, 1994. http://hdl.handle.net/2381/35257.
Texto completoKimura, Koji. "Hyperpolarization-activated, cyclic nucleotide-gated HCN2 cation channel forms a protein assembly with multiple neuronal scaffold proteins in distinct modes of protein-protein interaction". Kyoto University, 2004. http://hdl.handle.net/2433/145287.
Texto completoArrigoni, C. "MODULATION OF PORE GATING BY ¿SENSOR¿ DOMAINS IN VOLTAGE-GATED K+ CHANNELS". Doctoral thesis, Università degli Studi di Milano, 2013. http://hdl.handle.net/2434/215591.
Texto completoTalke, Ina Nicola. "Cyclic nucleotide-gated channels in Arabidopsis thaliana". Thesis, University of York, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.274500.
Texto completoFLANNERY, RICHARD JOHN. "CLUSTERING OF CYCLIC-NUCLEOTIDE-GATED CHANNELS IN OLFACTORY CILIA". University of Cincinnati / OhioLINK, 2006. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1136913935.
Texto completoChow, Sarah Sue Wen. "Energetic and structural impact of cyclic nucleotide binding to hyperpolarization-activated cyclic nucleotide-gated channels". Thesis, University of British Columbia, 2013. http://hdl.handle.net/2429/44980.
Texto completoAdams, Nicolette. "Investigating the Role of Cyclic Nucleotide gated channels in Plant- Pathogen Interactions". Doctoral thesis, University of Cape Town, 2009. http://hdl.handle.net/11427/4236.
Texto completoPark, Graeme Jonathan. "A study of the physiological role of cyclic nucleotide gated channels in Arabidopsis thaliana". Thesis, University of York, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.440977.
Texto completoWeißgraeber, Stephanie [Verfasser], Kay [Akademischer Betreuer] Hamacher y Gerhard [Akademischer Betreuer] Thiel. "Hyperpolarization-Activated cyclic nucleotide-gated channels - structure and evolution / Stephanie Weißgraeber. Betreuer: Kay Hamacher ; Gerhard Thiel". Darmstadt : Universitäts- und Landesbibliothek Darmstadt, 2015. http://d-nb.info/1112143858/34.
Texto completoYamada, Rei. "Hyperpolarization-activated cyclic-nucleotide gated cation channels regulate auditory coincidence detection in nucleus laminaris of the chick". Kyoto University, 2005. http://hdl.handle.net/2433/144385.
Texto completo0048
新制・課程博士
博士(医学)
甲第11938号
医博第2920号
新制||医||911(附属図書館)
23727
UT51-2006-B117
京都大学大学院医学研究科脳統御医科学系専攻
(主査)教授 金子 武嗣, 教授 河野 憲二, 教授 伊藤 壽一
学位規則第4条第1項該当
Frietsch, Sabine. "The role of Cyclic Nucleotide-Gated Channels (CNGC) in plant development and stress responses in Arabidopsis thaliana". [S.l. : s.n.], 2006.
Buscar texto completoHua, Li. "Phosphatidylinositol (4,5)-bisphosphate (PIP2) modulation of TRPV1 and functional interactions between A' helices in the C-linkers of open CNG channels /". Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/10545.
Texto completoJunor, Roderick Walter John. "Fetal and postnatal lung liquid transport : the role of cyclic nucleotide gated cation channels and pulmonary blood flow". Thesis, St George's, University of London, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.313811.
Texto completoGonzalez, Amaliris. "EXPRESSION OF THE CNGB3 SUBUNIT IN RETINA OF ACHROMATOPSIA-AFFECTED DOGS". Diss., Temple University Libraries, 2015. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/337529.
Texto completoPh.D.
Light energy is converted into an electrical signal by a set of proteins in the phototransduction cascade in photoreceptors. In this work, I focus on two critical elements of the phototransduction cascade in canine, the opsin molecules and CNG channels of cone photoreceptors. Canines are dichromats possessing two types of cone photoreceptors with different opsin molecules that detect either long and medium wavelengths (L/M) or short wavelengths (S). The L/M- and S-opsin genes were cloned from an Alaskan Malamute and used to investigate key amino acids that are responsible for tuning the spectral properties of the 11-cis retinal chromophore. Cone CNG channels are composed of CNGA3 and CNGB3 subunits. I characterized antibodies to detect cone CNG channel subunits to investigate expression of mutations in CNGB3 subunit on two canine models for achromatopsia. One model contains a missense CNGB3 mutation D262N (CNGB3m/m) and the other is a complete deletion of all exons of the CNGB3 gene (CNGB3-/-). Studies presented in this thesis show CNGB3 is expressed later in cone during retinal development compared to CNGA3. It also presents evidence for the necessity of CNGB3 in cone outer segment targeting of CNGA3.
Temple University--Theses
Nakashima, Noriyuki. "Hyperpolarisation-activated cyclic nucleotide-gated channels regulate the spontaneous firing rate of olfactory receptor neurons and affect glomerular formation in mice". Kyoto University, 2013. http://hdl.handle.net/2433/174812.
Texto completoWongsamitkul, Nisa [Verfasser], Klaus [Akademischer Betreuer] Benndorf, Ingo [Akademischer Betreuer] Dahse y Stephan [Akademischer Betreuer] Frings. "Translation of ligand binding to activation in olfactory cyclic nucleotide-gated (CNG) channels / Nisa Wongsamitkul. Gutachter: Klaus Benndorf ; Ingo Dahse ; Stephan Frings". Jena : Thüringer Universitäts- und Landesbibliothek Jena, 2015. http://d-nb.info/1079217932/34.
Texto completoDeutsch, Matthias [Verfasser], Sigrun [Gutachter] Korsching, Arnd [Gutachter] Baumann y Guenter [Gutachter] Schwarz. "Role of Hyperpolarization activated and Cyclic Nucleotide gated (HCN) Channels in Hippocampal Neurons / Matthias Deutsch ; Gutachter: Sigrun Korsching, Arnd Baumann, Guenter Schwarz". Köln : Universitäts- und Stadtbibliothek Köln, 2020. http://d-nb.info/1207074314/34.
Texto completoKondapuram, Mahesh [Verfasser], Klaus [Gutachter] Benndorf, Heinrich [Gutachter] Terlau y Christoph [Gutachter] Fahlke. "Mechanisms underlying cAMP mediated gating in hyperpolarization-activated cyclic nucleotide-gated channels : interactions with-in HCN Channels / Mahesh Kondapuram ; Gutachter: Klaus Benndorf, Heinrich Terlau, Christoph Fahlke". Jena : Friedrich-Schiller-Universität Jena, 2021. http://d-nb.info/123814215X/34.
Texto completoShah, Nikhil N. "SH3 AND MULTIPLE ANKYRIN REPEAT DOMAIN 3 (SHANK3) AFFECTS THE EXPRESSION OF HYPERPOLARIZATION-ACTIVATED CYCLIC NUCLEOTIDE-GATED (HCN) CHANNELS IN MOUSE MODELS OF AUTISM". VCU Scholars Compass, 2017. http://scholarscompass.vcu.edu/etd/4997.
Texto completoSmith, Trevor. "An investigation into the role of the hyperpolarisation-activated cyclic nucleotide-gated on channels in dorsal root ganglion neurons in rat models of chronic inflammatory and neuropathic pain". Thesis, University of Liverpool, 2012. http://livrepository.liverpool.ac.uk/9093/.
Texto completoAbdel, Hamid Huda. "Structural - functional Analysis of Plant Cyclic Nucleotide Gated Ion Channels". Thesis, 2013. http://hdl.handle.net/1807/35761.
Texto completoDose, Andrea Christina. "Molecular characterization of the cyclic nucleotide-gated cation channel of bovine rod outer segments". Thesis, 1995. http://hdl.handle.net/2429/4785.
Texto completoBaxter, Joyce. "Identification of a functionally essential amino acid for an Arabidopsis cyclic nucleotide-gated ion channel". 2007. http://link.library.utoronto.ca/eir/EIRdetail.cfm?Resources__ID=788863&T=F.
Texto completoDoheny, Jason. "Trigeminal neuropathic pain in rats: a role for thalamic hyperpolarization-activated cyclic nucleotide-gated channel activity". Thesis, 2020. https://hdl.handle.net/2144/41212.
Texto completoChin, Kimberley. "Investigation of Structure-function and Signal Transduction of Plant Cyclic Nucleotide-gated Ion Channels". Thesis, 2013. http://hdl.handle.net/1807/43505.
Texto completoLiu, Kao-Chao y 劉高超. "The stability of Calmodulin and the effect of Calmodulin binding site of cyclic-nucleotide-gated olfactory ion channel". Thesis, 2002. http://ndltd.ncl.edu.tw/handle/00576445818853029884.
Texto completo國立東華大學
化學系
90
Abstract Calmodulin (CaM) is a 148-residue protein which serves as the promary receptor for intracellular Ca2+. The structure of CaM contains two globular domains and a long sentral helix. In the first part of the thesis, we have performed the chemical denaturation experiments to determine the stability of wild type, three point-mutated, and the N-terminal domain of CaMs. Based on the two-state and three-state unfolding model, the free energy of unfolding (ΔGo) and the transition midpoint of CaM and its mutants have been calculated. The stability of apo and holo Y99W, Y138W was almost unchanged compared to wild type CaM. Interestingly, the stability of Y99WY1338W was decreased slightly in the holo form however, increased by about 0.5 kcal/mol compared to wild type CaM and Y99W and Y138W. The N-terminal domain of CaM is more stable than the C-domain in their apo-forms. However, upon binding to Ca2+, the C-terminal domain is more stable than the N-terminal one. In the second part of the thesis, we have investigated the structural change and the binding stoichiometric ratio of CaM with the binding domain of a nucleotide-gated ion channel. We have found that the peptide adopted α-helical structure upon binding to CaM and that the binding stoichiometric ratio is 1:1.
Guo, Jhao-Heng y 郭肇恆. "Structural Study of Calmodulin Complexed with Calmodulin Binding Domain of Mutated Cyclic Nucleotide-Gated Ion Channel by NMR". Thesis, 2009. http://ndltd.ncl.edu.tw/handle/48416763339931417372.
Texto completoBecirovic, Elvir [Verfasser]. "Role of the CNGB1a subunit of the rod cyclic nucleotide gated channel in channel gating and pathogenesis of retinitis pigmentosa / Elvir Becirovic". 2010. http://d-nb.info/1006625305/34.
Texto completoHuang, Po-Chaung y 黃柏川. "Purification, crystallization and preliminary x-ray crystallographic analysis of a hybrid molecule of calmodulin and calmodulin binding domain of olfactory cyclic nucleotide-gated ion channel". Thesis, 2004. http://ndltd.ncl.edu.tw/handle/18787375825063015418.
Texto completo國立東華大學
化學系
92
Calmodulin (CaM) is a ubiquitous calcium sensor, which binds to and regulates many proteins in a Ca2+-dependent manner. Calmodulin has been shown to bind directly to the olfactory channels and to modulate their sensitivity to cyclic nucleotides and appears to play a role in the termination of the signal-transduction pathway in olfactory neurons. In this study, a hybrid molecule, which consists of CaM and CaM-binding domain of olfactory nucleotide gated ion channel, was purified and crystallized. Preliminary crystallographic analysis was achieved. The crystals diffracted to a maximum resolution of 1.85 Å at a cryogenic temperature (100K) using X-rays from a rotating copper tube (1.54 Å wavelength). The crystal belonged to a monoclinic system, and the space group was C2 with unit cell dimensions of a=64.76 Å, b=36.23 Å, c=70.96 Å, α=γ=90˚, β=109.4˚. Each asymmetric unit contained one CaM-OLFp hybrid molecule, which gave rise to a specific volume (VM) of 1.94 Å3Da-1 based on the calculated molecular mass of 20 kDa for a CaM-OLFp hybrid molecule and an estimated solvent content of 36.42%, indicating that our crystal is suitable for further structure analysis.
Weißgraeber, Stephanie. "Hyperpolarization-Activated cyclic nucleotide-gated channels - structure and evolution". Phd thesis, 2015. http://tuprints.ulb.tu-darmstadt.de/4212/1/diss_tuprints2015.pdf.
Texto completoRato, Claudia. "Regulation of pollen tube growth by calmodulin, cyclic nucleotides and cyclic nucleotide-gated channels". Doctoral thesis, 2007. http://sibul.reitoria.ul.pt/F/?func=item-global&doc_library=ULB01&type=03&doc_number=000511486.
Texto completoPollen tube growth plays an essential role in fertilization of flowering plants. Several signalling pathways were identified during pollen tube growth, including Ca2+, CaM and 3',5'-cyclic adenosine monophosphate (cAMP). These constitute a complex web of signalling networks that intersect at various levels (reviewed in Chapter I). In order to elucidate the role of CaM we mapped its activity in growing pollen tubes. We found that CaM activity exhibits a tip-focused gradient, similar to the distribution of cytosolic free Ca2+ ([Ca2+]c), and that it oscillates with a period similar to [Ca2+]c . Moreover, we show that CaM is also involved in the guidance mechanism and has its activity strongly modulated by intracellular changes in cAMP. A putative target of the crosstalk between CaM and cAMP is the secretory machinery as observed in pollen tubes loaded with the FM 1-43 dye. Our data thus suggest that pollen tube growth and orientation depends on an intricate crosstalk between multiple signalling pathways in which CaM is a key element (Chapter II). In Chapter III we study two possible targets of CaM, CNGC7 and CNGC8. These proteins are both expressed in pollen and show strong homology, suggesting functional redundancy. To gain insights into the biological function of CNGC7 and CNGC8, we used reverse-genetics. Neither CNGC7 nor CNGC8 was found to be essential, but CNGC7 appears to play a role in fertilization. To further address a possible redundancy between CNGC7 and CNGC8, we generated a double-mutant and the double knockout was found to be gametophyte lethal. These results provide the first genetic evidence for redundancy among CNGCs in fertilization. Plant CNGCs contain a C-terminal cyclic nucleotide binding domain with an overlapping CaM binding site. Cyclic nucleotides induce channel opening, while CaM mediates the feed-back inhibition of the channel. To gain insights into the structure-function relationship of plant CNGCs, we used a site-directed mutagenesis technique coupled with complementation assays of cngc18 mutants. Amino acid substitutions E520A, F565A and F565W provided partial complementation. Taken together, these results show that F565 and E520 are key amino acid residues for cyclic nucleotide binding and that changes in the cyclic nucleotide binding domain are capable of disrupting protein function (Chapter IV). In Chapter V all results obtained were discussed.
Ullmer, Wendy Elizabeth. "Expression and sub-cellular localization of cyclic nucleotide-gated ion channels in Arabidopsis thaliana". Thesis, 2007. http://hdl.handle.net/10125/20744.
Texto completoRESTA, FRANCESCO. "Hyperpolarization-activated Cyclic Nucleotide gated (HCN) channels as promising new target for neuropathic pain treatment". Doctoral thesis, 2016. http://hdl.handle.net/2158/1049658.
Texto completoChiang, Wei-Che y 蔣惟哲. "NMR structural study of binding specificity of calmodulin to mutant olfactory cyclic nucleotide-gated ion channels". Thesis, 2014. http://ndltd.ncl.edu.tw/handle/60411804119080908559.
Texto completo國立東華大學
化學系
102
Calmodulin (CaM), the primary intracellular Ca2+ receptor, regulates a large number of key enzymes and controls a wide spectrum of important biological responses. The structure of CaM and its target sequence in rat olfactory nucleotide gated ion channel (OLFp) was characterized by NMR spectroscopy. Our previous data indicated that distinct CaM/OLFp complexes (mode I and II) existed simultaneously with stable structures that were not inter-exchangeable within the NMR time scale. The NMR structures of these two CaM/OLFp complexes showed that the helical OLFp with C2 symmetry bound to CaM in two orientations and the palindromic sequence of OLFp (F1QRIVRLVGVIRDW14) is crucial for its targeting orientation to CaM. In order to further support this hypothesis, we investigated the interaction of CaM with a series of mutated OLFp with less palindromic feature by NMR. We found that the Valine residue in the position 5 is the most important residue for the orientation-specific targeting to CaM. Only one complex structure was detected when CaM in association with the mutated OLFp_V5A. The complex structure of CaM/OLFp_V5A was determined. It shows that the subtle change of the side chain strongly affects the stability of the weak interactions between OLFp and CaM.
El-Kholy, Wasim. "The role of hyperpolarization activated cyclic nucleotide modulated and voltage gated potassium channels in pancreatic beta-cell function". 2007. http://link.library.utoronto.ca/eir/EIRdetail.cfm?Resources__ID=478866&T=F.
Texto completoFrietsch, Sabine [Verfasser]. "The role of cyclic nucleotide gated channels (CNGC) in plant development and stress responses in Arabidopsis thaliana / vorgelegt von Sabine Frietsch". 2006. http://d-nb.info/995451265/34.
Texto completo"Expressions of cyclic nucleotide-gated ionic conductances in rat cerebellar purkinje neurons =: 大鼠小腦浦肯野細胞環核苷酸門控離子通道的表達". 2005. http://library.cuhk.edu.hk/record=b5892479.
Texto completoThesis (M.Phil.)--Chinese University of Hong Kong, 2005.
Includes bibliographical references (leaves 82-104).
Text in English; abstracts in English and Chinese.
Tsoi Sze Man.
Chapter Chapter 1 --- Introduction --- p.1
Chapter 1.1 --- Overview of study --- p.1
Chapter 1.2 --- Cerebellum --- p.2
Chapter 1.2.1 --- General Structure of cerebellum --- p.3
Chapter 1.2.2 --- Cell types of cerebellar cortex --- p.4
Chapter 1.2.2.1 --- Basket cells --- p.5
Chapter 1.2.2.2 --- Stellate cells --- p.6
Chapter 1.2.2.3 --- Purkinje cells --- p.6
Chapter 1.2.2.4 --- Granule cells --- p.7
Chapter 1.2.2.5 --- Golgi cells --- p.8
Chapter 1.2.2.6 --- Unipolar brush cells --- p.9
Chapter 1.2.2.7 --- Deep cerebellar nuclear neurons --- p.11
Chapter 1.2.3 --- The neuronal circuitry of the cerebellum --- p.12
Chapter 1.2.4 --- Cerebellar function --- p.14
Chapter 1.3 --- Cyclic nucleotide-gated (CNG) channels --- p.16
Chapter 1.3.1 --- Molecular characterization of CNG channels --- p.16
Chapter 1.3.2 --- Functional properties of CNG channels --- p.19
Chapter 1.3.3 --- Expression of CNG channels in brain --- p.21
Chapter 1.3.4 --- CNG channel and neuronal plasticity --- p.23
Chapter 1.4 --- Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels --- p.26
Chapter 1.4.1 --- Molecular characterization of HCN channels --- p.27
Chapter 1.4.2 --- Functional properties of HCN channels and Ih current --- p.29
Chapter 1.4.3 --- Modulation by cyclic nucleotides --- p.31
Chapter 1.4.4 --- Expression of HCN channels in brain --- p.33
Chapter 1.4.5 --- Physiological roles of Ih current in central nervous system --- p.35
Chapter 1.5 --- Aims of study --- p.38
Chapter Chapter 2 --- Material and Methods --- p.39
Chapter 2.1 --- Immunohistochemistry Experiments --- p.39
Chapter 2.1.1 --- Animal preparation --- p.39
Chapter 2.1.2 --- Tissue preparation --- p.39
Chapter 2.1.3 --- Primary and secondary antibodies --- p.40
Chapter 2.1.4 --- Immunofluroescence staining --- p.41
Chapter 2.1.5 --- Confocal laser scanning microscopy and data processing --- p.41
Chapter 2.2 --- Whole cell patch clamp recordings --- p.42
Chapter 2.2.1 --- Brain slice preparation and identification of the cerebellar Purkinje neurons --- p.42
Chapter 2.2.2 --- Whole cell voltage- and current-clamp recordings --- p.43
Chapter 2.2.3 --- Drug solutions and delivery --- p.44
Chapter 2.2.4 --- Statistical analysis --- p.45
Chapter Chapter 3 --- Expression of Various Cyclic Nucleotide-Gated (CNG) Channel Subunits in Rat Cerebellum --- p.46
Chapter 3.1 --- Introduction --- p.46
Chapter 3.2 --- Results --- p.46
Chapter 3.2.1 --- Immunoreactivity of CNGA1 in cerebellum --- p.46
Chapter 3.2.2 --- Immunoreactivity of CNGA2 in cerebellum --- p.47
Chapter 3.2.3 --- Immunoreactivity of CNGA3 in cerebellum --- p.47
Chapter 3.3 --- Discussion --- p.48
Chapter Chapter 4 --- Expression of Various Hyperpolarization-Activated Cyclic Nucleotide-Gated (HCN) Channel Subunits in Rat Cerebellum --- p.53
Chapter 4.1 --- Introduction --- p.53
Chapter 4.2 --- Results --- p.53
Chapter 4.2.1 --- Immunoreactivity of HCN 1 in cerebellum --- p.53
Chapter 4.2.2 --- Immunoreactivity of HCN2 in cerebellum --- p.55
Chapter 4.2.3 --- Immunoreactivity of HCN3 in cerebellum --- p.55
Chapter 4.2.4 --- Immunoreactivity of HCN4 in cerebellum --- p.55
Chapter 4.3 --- Discussion --- p.55
Chapter Chapter 5 --- Electrophysiological Recordings of Cyclic Nucleotide-Gated Ionic Conductance in Rat Cerebellar Purkinje Neurons --- p.59
Chapter 5.1 --- Introduction --- p.59
Chapter 5.2 --- Results --- p.59
Chapter 5.2.1 --- Effect of cyclic nucleotides on the membrane potential of cerebellar Purkinje neurons --- p.59
Chapter 5.2.2 --- Ionic conductance of the cyclic nucleotide-induced inward current --- p.61
Chapter 5.2.3 --- The mechanism of the cyclic nucleotide-induced inward current --- p.61
Chapter 5.2.3.1 --- Site of action --- p.62
Chapter 5.2.3.2 --- Involvement of CNG channels and HCN channels --- p.63
Chapter 5.2.3.3 --- Involvement of protein kinase A (PKA) and protein kinase G (PKG) --- p.65
Chapter 5.2.3.4 --- Involvement of inwardly rectifying potassium (Kir) channels and transient receptor potential (TRP) channels --- p.65
Chapter 5.2.4 --- Effect of cyclic nucleotides on Ih current in Purkinje neurons --- p.67
Chapter 5.3 --- Discussion --- p.68
Chapter Chapter 6 --- Concluding remarks References --- p.78
References --- p.82
Urquhart, William. "Characterization of AtCNGC11/12-induced Cell Death and the Role of AtCNGC11 and AtCNGC12 in Ca2+ Dependent Signalling Pathways". Thesis, 2011. http://hdl.handle.net/1807/29897.
Texto completo