Relevant bibliographies by topics / Kv3.3

Academic literature on the topic 'Kv3.3'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Kv3.3"

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Schwalbe, Ruth A., Melissa J. Corey, and Tara A. Cartwright. "Novel Kv3 glycoforms differentially expressed in adult mammalian brain contain sialylated N-glycans." Biochemistry and Cell Biology 86, no. 1 (February 2008): 21–30. http://dx.doi.org/10.1139/o07-152.

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The N-glycan pool of mammalian brain contains remarkably high levels of sialylated N-glycans. This study provides the first evidence that voltage-gated K+ channels Kv3.1, Kv3.3, and Kv3.4, possess distinct sialylated N-glycan structures throughout the central nervous system of the adult rat. Electrophoretic migration patterns of Kv3.1, Kv3.3, and Kv3.4 glycoproteins from spinal cord, hypothalamus, thalamus, cerebral cortex, hippocampus, and cerebellum membranes digested with glycosidases were used to identify the various glycoforms. Differences in the migration of Kv3 proteins were attributed to the desialylated N-glycans. Expression levels of the Kv3 proteins were highest in cerebellum, whereas those of Kv3.1 and Kv3.3 were much lower in the other 5 regions. The lowest level of Kv3.1 was expressed in the hypothalamus, whereas the lowest levels of Kv3.3 were expressed in both thalamus and hypothalamus. The other regions expressed intermediate levels of Kv3.3, with spinal cord expressing the highest. The expression level of Kv3.4 in the hippocampus was slightly lower than that in cerebellum, and was closely followed by the other 4 regions, with spinal cord expressing the lowest level. We suggest that novel Kv3 glycoforms may endow differences in channel function and expression among regions throughout the central nervous system.
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Xu, Chuanli, Yanjie Lu, Guanghua Tang, and Rui Wang. "Expression of voltage-dependent K+ channel genes in mesenteric artery smooth muscle cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 277, no. 5 (November 1, 1999): G1055—G1063. http://dx.doi.org/10.1152/ajpgi.1999.277.5.g1055.

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Molecular basis of native voltage-dependent K+(Kv) channels in smooth muscle cells (SMCs) from rat mesenteric arteries was investigated. The whole cell patch-clamp study revealed that a 4-aminopyridine-sensitive delayed rectifier K+ current ( I K) was the predominant K+ conductance in these cells. A systematic screening of the expression of 18 Kv channel genes using RT-PCR technique showed that six I K-encoding genes (Kv1.2, Kv1.3, Kv1.5, Kv2.1, Kv2.2, and Kv3.2) were expressed in mesenteric artery. Although no transient outward Kv currents ( I A) were recorded in the studied SMCs, transcripts of multiple I A-encoding genes, including Kv1.4, Kv3.3, Kv3.4, Kv4.1, Kv4.2, and Kv4.3 as well as I A-facilitating Kv β-subunits (Kvβ1, Kvβ2, and Kvβ3), were detected in mesenteric arteries. Western blot analysis demonstrated that four I K-related Kv channel proteins (Kv1.2, Kv1.3, Kv1.5, and Kv2.1) were detected in mesenteric artery tissues. The presence of Kv1.2, Kv1.3, Kv1.5, and Kv2.1 channel proteins in isolated SMCs was further confirmed by immunocytochemistry study. Our results suggest that the native I K in rat mesenteric artery SMCs might be generated by heteromultimerization of Kv genes.
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Paucar, Martin, Richard Ågren, Tianyi Li, Simon Lissmats, Åsa Bergendal, Jan Weinberg, Daniel Nilsson, et al. "V374A KCND3 Pathogenic Variant Associated With Paroxysmal Ataxia Exacerbations." Neurology Genetics 7, no. 1 (January 6, 2021): e546. http://dx.doi.org/10.1212/nxg.0000000000000546.

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ObjectiveAtaxia channelopathies share common features such as slow motor progression and variable degrees of cognitive dysfunction. Mutations in potassium voltage-gated channel subfamily D member 3 (KCND3), encoding the K+ channel, Kv4.3, are associated with spinocerebellar ataxia (SCA) 19, allelic with SCA22. Mutations in potassium voltage-gated channel subfamily C member 3 (KCNC3), encoding another K+ channel, Kv3.3, cause SCA13. First, a comprehensive phenotype assessment was carried out in a family with autosomal dominant ataxia harboring 2 genetic variants in KCNC3 and KCND3. To evaluate the physiological impact of these variants on channel currents, in vitro studies were performed.MethodsClinical and psychometric evaluations, neuroimaging, and genotyping of a family (mother and son) affected by ataxia were carried out. Heterozygous and homozygous Kv3.3 A671V and Kv4.3 V374A variants were evaluated in Xenopus laevis oocytes using 2-electrode voltage-clamp. The influence of Kv4 conductance on neuronal activity was investigated computationally using a Purkinje neuron model.ResultsThe main clinical findings were consistent with adult-onset ataxia with cognitive dysfunction and acetazolamide-responsive paroxysmal motor exacerbations in the index case. Despite cognitive deficits, fluorodeoxyglucose (FDG)-PET displayed hypometabolism mainly in the severely atrophic cerebellum. Genetic analyses revealed the new variant c.1121T>C (V374A) in KCND3 and c.2012T>C (A671V) in KCNC3. In vitro electrophysiology experiments on Xenopus oocytes demonstrated that the V374A mutant was nonfunctional when expressed on its own. Upon equal co-expression of wild-type (WT) and V374A channel subunits, Kv4.3 currents were significantly reduced in a dominant negative manner, without alterations of the gating properties of the channel. By contrast, Kv3.3 A671V, when expressed alone, exhibited moderately reduced currents compared with WT, with no effects on channel activation or inactivation. Immunohistochemistry demonstrated adequate cell membrane translocation of the Kv4.3 V374A variant, thus suggesting an impairment of channel function, rather than of expression. Computational modeling predicted an increased Purkinje neuron firing frequency upon reduced Kv4.3 conductance.ConclusionsOur findings suggest that Kv4.3 V374A is likely pathogenic and associated with paroxysmal ataxia exacerbations, a new trait for SCA19/22. The present FDG PET findings contrast with a previous study demonstrating widespread brain hypometabolism in SCA19/22.
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Zagha, Edward, Satoshi Manita, William N. Ross, and Bernardo Rudy. "Dendritic Kv3.3 Potassium Channels in Cerebellar Purkinje Cells Regulate Generation and Spatial Dynamics of Dendritic Ca2+ Spikes." Journal of Neurophysiology 103, no. 6 (June 2010): 3516–25. http://dx.doi.org/10.1152/jn.00982.2009.

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Purkinje cell dendrites are excitable structures with intrinsic and synaptic conductances contributing to the generation and propagation of electrical activity. Voltage-gated potassium channel subunit Kv3.3 is expressed in the distal dendrites of Purkinje cells. However, the functional relevance of this dendritic distribution is not understood. Moreover, mutations in Kv3.3 cause movement disorders in mice and cerebellar atrophy and ataxia in humans, emphasizing the importance of understanding the role of these channels. In this study, we explore functional implications of this dendritic channel expression and compare Purkinje cell dendritic excitability in wild-type and Kv3.3 knockout mice. We demonstrate enhanced excitability of Purkinje cell dendrites in Kv3.3 knockout mice, despite normal resting membrane properties. Combined data from local application pharmacology, voltage clamp analysis of ionic currents, and assessment of dendritic Ca2+ spike threshold in Purkinje cells suggest a role for Kv3.3 channels in opposing Ca2+ spike initiation. To study the physiological relevance of altered dendritic excitability, we measured [Ca2+]i changes throughout the dendritic tree in response to climbing fiber activation. Ca2+ signals were specifically enhanced in distal dendrites of Kv3.3 knockout Purkinje cells, suggesting a role for dendritic Kv3.3 channels in regulating propagation of electrical activity and Ca2+ influx in distal dendrites. These findings characterize unique roles of Kv3.3 channels in dendrites, with implications for synaptic integration, plasticity, and human disease.
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Zhao, Jian, Jing Zhu, and William B. Thornhill. "Spinocerebellar ataxia-13 Kv3.3 potassium channels: arginine-to-histidine mutations affect both functional and protein expression on the cell surface." Biochemical Journal 454, no. 2 (August 9, 2013): 259–65. http://dx.doi.org/10.1042/bj20130034.

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The voltage-gated potassium channel Kv3.3 is the causative gene of SCA13 (spinocerebellar ataxia type 13), an autosomal dominant neurological disorder. The four dominant mutations identified to date cause Kv3.3 channels to be non-functional or have altered gating properties in Xenopus oocytes. In the present paper, we report that SCA13 mutations affect functional as well as protein expression of Kv3.3 channels in a mammalian cell line. The reduced protein level of SCA13 mutants is caused by a shorter protein half-life, and blocking the ubiquitin–proteasome pathway increases the total protein of SCA13 mutants more than wild-type. SCA13 mutated amino acids are highly conserved, and the side chains of these residues play a critical role in the stable expression of Kv3.3 proteins. In addition, we show that mutant Kv3.3 protein levels could be partially rescued by treatment with the chemical chaperone TMAO (trimethylamine N-oxide) and to a lesser extent with co-expression of Kv3.1b. Thus our results suggest that amino acid side chains of SCA13 positions affect the protein half-life and/or function of Kv3.3, and the adverse effect on protein expression cannot be fully rescued.
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Epperson, Anne, Helena P. Bonner, Sean M. Ward, William J. Hatton, Karri K. Bradley, Michael E. Bradley, James S. Trimmer, and Burton Horowitz. "Molecular diversity of KVα- and β-subunit expression in canine gastrointestinal smooth muscles." American Journal of Physiology-Gastrointestinal and Liver Physiology 277, no. 1 (July 1, 1999): G127—G136. http://dx.doi.org/10.1152/ajpgi.1999.277.1.g127.

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Voltage-activated K+(KV) channels play an important role in regulating the membrane potential in excitable cells. In gastrointestinal (GI) smooth muscles, these channels are particularly important in modulating spontaneous electrical activities. The purpose of this study was to identify the molecular components that may be responsible for the KV currents found in the canine GI tract. In this report, we have examined the qualitative expression of eighteen different KV channel genes in canine GI smooth muscle cells at the transcriptional level using RT-PCR analysis. Our results demonstrate the expression of KV1.4, KV1.5, KV1.6, KV2.2, and KV4.3 transcripts in all regions of the GI tract examined. Transcripts encoding KV1.2, KVβ1.1, and KVβ1.2 subunits were differentially expressed. KV1.1, KV1.3, KV2.1, KV3.1, KV3.2, KV3.4, KV4.1, KV4.2, and KVβ2.1 transcripts were not detected in any GI smooth muscle cells. We have also determined the protein expression for a subset of these KV channel subunits using specific antibodies by immunoblotting and immunohistochemistry. Immunoblotting and immunohistochemistry demonstrated that KV1.2, KV1.4, KV1.5, and KV2.2 are expressed at the protein level in GI tissues and smooth muscle cells. KV2.1 was not detected in any regions of the GI tract examined. These results suggest that the wide array of electrical activity found in different regions of the canine GI tract may be due in part to the differential expression of KV channel subunits.
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Platoshyn, Oleksandr, Carmelle V. Remillard, Ivana Fantozzi, Mehran Mandegar, Tiffany T. Sison, Shen Zhang, Elyssa Burg, and Jason X. J. Yuan. "Diversity of voltage-dependent K+ channels in human pulmonary artery smooth muscle cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 287, no. 1 (July 2004): L226—L238. http://dx.doi.org/10.1152/ajplung.00438.2003.

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Electrical excitability, which plays an important role in excitation-contraction coupling in the pulmonary vasculature, is regulated by transmembrane ion flux in pulmonary artery smooth muscle cells (PASMC). This study examined the heterogeneous nature of native voltage-dependent K+ channels in human PASMC. Both voltage-gated K+ (KV) currents and Ca2+-activated K+ (KCa) currents were observed and characterized. In cell-attached patches of PASMC bathed in Ca2+-containing solutions, depolarization elicited a wide range of K+ unitary conductances (6–290 pS). When cells were dialyzed with Ca2+-free and K+-containing solutions, depolarization elicited four components of KV currents in PASMC based on the kinetics of current activation and inactivation. Using RT-PCR, we detected transcripts of 1) 22 KV channel α-subunits (KV1.1–1.7, KV1.10, KV2.1, KV3.1, KV3.3–3.4, KV4.1–4.2, KV5.1, KV 6.1–6.3, KV9.1, KV9.3, KV10.1, and KV11.1), 2) three KV channel β-subunits (KVβ1–3), 3) four KCa channel α-subunits ( Slo-α1 and SK2–SK4), and 4) four KCa channel β-subunits (KCaβ1–4). Our results show that human PASMC exhibit a variety of voltage-dependent K+ currents with variable kinetics and conductances, which may result from various unique combinations of α- and β-subunits forming the native channels. Functional expression of these channels plays a critical role in the regulation of membrane potential, cytoplasmic Ca2+, and pulmonary vasomotor tone.
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Zhang, Yalan, and Leonard K. Kaczmarek. "Kv3.3 potassium channels and spinocerebellar ataxia." Journal of Physiology 594, no. 16 (November 15, 2015): 4677–84. http://dx.doi.org/10.1113/jp271343.

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Ghanshani, Sanjiv, Michael Pak, John D. McPherson, Michael Strong, Brent Dethlefs, John J. Wasmuth, Lawrence Salkoff, George A. Gutman, and K. George Chandy. "Genomic organization, nucleotide sequence, and cellular distribution of a Shaw-related potassium channel gene, Kv3.3, and mapping of Kv3.3 and Kv3.4 to human chromosomes 19 and 1." Genomics 12, no. 2 (February 1992): 190–96. http://dx.doi.org/10.1016/0888-7543(92)90365-y.

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Espinosa, F., M. A. Torres-Vega, G. A. Marks, and R. H. Joho. "Ablation of Kv3.1 and Kv3.3 Potassium Channels Disrupts Thalamocortical Oscillations In Vitro and In Vivo." Journal of Neuroscience 28, no. 21 (May 21, 2008): 5570–81. http://dx.doi.org/10.1523/jneurosci.0747-08.2008.

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Dissertations / Theses on the topic "Kv3.3"

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Kemp, Laurens [Verfasser], Tobias [Akademischer Betreuer] Huth, and Tobias [Gutachter] Huth. "Elektrophysiologische Untersuchung von Kv3.3/Kv3.4 Kanalkomplexen und deren Interaktion mit der β-Sekretase BACE1 / Laurens Kemp ; Gutachter: Tobias Huth ; Betreuer: Tobias Huth." Erlangen : Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), 2021. http://d-nb.info/1228627606/34.

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Vallejo, Gracia Albert. "Kv1.3 and Kv1.5 channels in leukocytes." Doctoral thesis, Universitat de Barcelona, 2016. http://hdl.handle.net/10803/397797.

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Voltage dependent potassium channels are a group of plasma membrane ion channels with a key role in the immune system as the predominant ion channels controlling the resting membrane potential and tuning intracellular Ca2+ signaling in lymphocytes, monocytes, macrophages, and dendritic cells. Leukocytes present a limited Kv repertoire, including Kv1.3 and Kv1.5 channel isoforms. Kv1.3 is expressed in the immune system, and the blockade of this channel is associated with selective inhibition of T cell activation and proliferation. A functional Kv channel is an oligomeric complex composed of pore-forming and ancillary subunits. The KCNE gene family (KCNE1-5) is a novel group of modulatory Kv channel elements expressed in several tissues including leukocytes. KCNE peptides are small single spanning membrane proteins known to modulate Kv channels trafficking and biophysical properties. The hypothesis of the present PhD thesis entitled “Kv1.3 and Kv1.5 channels in leukocytes” was that changes in the channelosome composition by modulating the heterooligomeric combinations of the Kv1.3 channelosome control physiological and neoplastic cell growth as well as leukocyte responses. Evidence suggests that Kv channels are involved in cell differentiation and cell cycle control (because non-specific drugs, such as 4-AP and TEA, impaire proliferation), and they are also known to be remodeled during carcinogenesis. Thus, we elucidated the role of Kv1.3 and Kv1.5 channels in cell growth and their relationship with cancer, in models such as B lymphocytes and lymphomas (non-Hodgkin lymphomas), pancreatic ductal adenocarcinoma (PDAC) and glioblastomas. In spite of its significance, the mechanisms that regulate Kv1.3 and its role in the T cell activation are not well known. To that end, we analyzed the expression of KCNEs ancillary subunits upon different states of activation and proliferation of leukocytes (macrophages, T and B lymphocytes). In addition, recent data from our laboratory demonstrate that KCNE4, acting as a dominant negative ancillary subunit, physically interacts with Kv1.3 inhibiting K+ currents and retaining the channel intracellularly. Therefore, we studied the Kv1.3 modulation by the auxiliary subunit KCNE4 in leukocytes.
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Roig, Merino Sara Raquel. "Heteroligomeric interactions of the Kv1.3 channelosome." Doctoral thesis, Universitat de Barcelona, 2017. http://hdl.handle.net/10803/404756.

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Voltage-gated potassium channels are proteins that allow the flux of potassium ions across the plasma membrane in response to a voltage stimulus. Those proteins were initially described in nervous system as the repolarization entities posterior to a depolarization. However, several different roles have been discovered to be enhanced, mediated or influenced by those entities. Cell cycle progression, homeostasis, proliferation or activation and apoptosis program are some of those functions. Kv1.3 is the third member of the first family of voltage-gated potassium channels in humans. This specific entity is mainly expressed in nervous and immune system. It has been associated with the repolarization of neurons, the activation and proliferation of leukocytes and apoptosis. Moreover, its dysfunctionality has been related to some autoimmune disease. The fine-tunning of the channel is highly relevant to control the final cell decision. The subunits that accompany the channel were classically named as β- subunits. Several different families have been described to modulate some channel features. Kvβ family are cytoplasmic proteins that can enhance the traffic to the plasma membrane and promote a switch towards negative voltages of the channel activation. However, few are known about alternative locations and Kv1.3 modulation. KCNE family are single spanning proteins highly promiscuous that modulate several different Kvα-subunits. Depending on the KCNE subtype, the effect on the channels can present different natures. This dissertation is focused on KCNE4 member, a peptide which generally negatively regulates Kv channels. This thesis described the positioning of Kvβ2.1, but not Kvβ1.1, in specific regions of the plasma membrane: lipid raft microdomains. Those are considered as signalling platforms at the plasma membrane highly relevant for several cellular processes. The possible mechanism that drives Kvβ2.1 is the palmitoylation of its amino acidic sequence; even other causes are not discarded. Proliferation signals are enhancing this localization while PMA treatment generates the opposite effect. This protein, as well as its partner Kvβ1.1, can form homo and heteroligomers. Their affinity and stoichiometry was addressed. Furthermore, multiprotein complexes were detected at membrane associated environments. Traffic and electrophysiological consequences on the channel were analysed upon coexpression with those subunits. Kv1.3 was removed from lipid raft microdomains and Kvβs prevented partially its PMA-dependent internalization. The molecular determinants involved in the Kv1.3 traffic to the plasma membrane were localised at the C-terminal domain. Previous results from the laboratory determined that KCNE4 is impairing the traffic of the channel. This thesis deciphered the molecular mechanisms involved in this effect concluding a bipartite system: (i) the masking of Kv1.3 export signal and (ii) the transference of a retention signal to the channelosome. Moreover, the specific domains of Kv1.3 and KCNE4 implicated in their interaction were mapped and pointed out to the C-terminal regions of both peptides. KCNE4 was also found to form oligomers and present several signals for its retention at the endoplasmic reticulum. Finally, the combination of both subunits (Kvβ2.1 and KCNE4) on the channel showed a dominance of KCNE4 effects, but an electrophysiological function of Kvβ2.1 on Kv1.3 kept preserved. Thus, the present thesis brought light to the comprehension of Kv1.3 channelosome.
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Solé, i. Codina Laura. "Role of KCN E4 on the voltage gated potassium channel Kv1.3 = Paper de KCNE4 en el canal de potassi dependent de voltage Kv1.3." Doctoral thesis, Universitat de Barcelona, 2013. http://hdl.handle.net/10803/129685.

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Voltage gated potassium channels (Kv) play important roles in different biological process such as generation and propagation of the nerve pulse and the cardiac action potential, promotion of insulin secretion, cell volume control, induction of cell proliferation, apoptosis, migration and initiation of many signaling pathways. Kv channels can homo- or hetero- tetramerize. The composition of the channel modulates their surface expression and serves as a mechanism for regulating channel activity. Kv channel interaction with accessory subunits provides mechanisms for channels to respond to stimuli beyond changes in membrane potential. The present dissertation is focused in the analysis of the effect of one regulatory subunits family (KCNEs) on different Kv channels. The first channel analyzed is Kv7.1, which is one of the most well-known channels to interact with all the KCNE family members. In fact KCNE1-Kv7.1 complex is focus of a huge number of studies, due to its important role in heart. Most of the studies though are focused to their electrophysiological properties and molecular determinants involved in the interaction. We performed traffic analysis experiments of Kv7.1 in the present of KCNE1-5 and demonstrated that Kv7.1 membrane surface localization is modified by some of them. Next, analysis was expanded to another channel from the same family, less characterized: Kv7.5. We demonstrated that from the five KCNEs members, only KCNE1 and KCNE3 modulate Kv7.5 activity. Furthermore, we demonstrated that Kv7.5 association to KCNE3 modifies the targeting of the regulatory subunit. Next, we moved to a non-related Kv channel such as Kv1.3, which plays a crucial role in the immune system. We first focused into characterizing the modulation of Kv1.3. We demonstrated that KCNE4, but not KCNE2, functions as an inhibitory Kv1.3 partner. Kv1.3 trafficking, targeting and activity are altered by the presence of KCNE4. Furthermore, by the combination of a plethora of approaches such as electrophysiological experiments from chimeric proteins and GFP single bleaching counting steps methodology we deciphered the stoichiometry of the Kv1.3-KCNE4 complex. Next, by immunoprecipitation experiments, traffic analysis and electrophysiological experiments, we analyzed the molecular determinants involved in the association between Kv1.3 and KCNE4. We have map a domain of Kv1.3 and a specific motif of KCNE4 involved in the formation of Kv1.3-KCNE4 complex, but not in the modulation of the channel. We also proposed a 3D docking model of Kv1.3 and KCNE4. Finally, due to the importance of Kv1.3 in the immune system, the expression of all the KCNE family has been analyzed in several cell lines of leukocytes. We have demonstrated that all KCNEs suffer a differential regulation among proliferation of leukocytes. Furthermore, a different regulation can be observed, depend on the mode of leukocytes’ activation. Our results further suggest a new and yet unidentified physiological role for KCNE subunits in the immune system. Putative associations of these ancillary proteins with Kv channels would yield a wide variety of biophysically and pharmacologically distinct channels that fine-tune the immunological response.
Els canals de potassi dependents de voltatge (Kv) juguen un paper molt important tant en cèl•lules excitables com no excitables. La possibilitat de formar hetero-oligomers i la d’associació amb subunitats reguladores són uns dels mecanismes que existeixen per tal de proveir de diferents mecanismes per a respondre de manera diferent enfront a canvis en el potencial de membrana. La composició del canalosoma modula tant la seva expressió a superfície com l’activitat d’aquests. Aquesta tesi es centra en l’estudi de l’efecte del la família de les subunitats reguladores KCNE sobre diferents Kv. Primerament s’estudià l’efecte que causaven en el tràfic del canal Kv7.1 (canal model per a l’estudi dels KCNEs) i posteriorment s’amplià l’estudi a un altre membre de la mateixa família, Kv7.5. A continuació s’estudià un canal d’elevada importància per a l’activació i proliferació leucocitària: Kv1.3, centrant-nos sobretot en l’efecte causat per un dels KCNEs: KCNE4. Aquesta subunitat no només inhibeix dràsticament el corrent del canal Kv1.3, sinó que a més a més, modifica el seu tràfic i localització. Aquests canvis són deguts a una interacció directa entre ambdues proteïnes. A continuació s’estudià en detall el complex Kv1.3-KCNE4. Mitjançant la combinació d’experiments d’electrofisiologia i monitorització de fluorescència de molècules individuals en la membrana, es va poder establir l’estequiometria d’aquest complex. Posteriorment, mitjançant l’anàlisi de diverses proteïnes quimèriques i mutants, tant del canal com de la subunitat reguladora, es van cercar els determinants moleculars implicats en l’associació entre ambdues proteïnes. S’han pogut determinar els motius claus en KCNE4 i Kv1.3 implicats en la formació del complex, però no en la modulació del canal. Finalment, degut a la importància de Kv1.3 en el sistema immunitari, s’han analitzat els nivells d’expressió dels KCNEs en diferents línies leucocitàries. S’ha observat que aquestes subunitats pateixen una regulació diferencial en funció de la manera d’activació i al llarg de la proliferació del leucòcits, suggerint un possible paper en la regulació precisa de la resposta immunològica.
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Schilling, Tom. "Morphologische, immunphänotypische und elektrophysiologische Eigenschaften deaktivierter muriner Mikroglia in vitro." Doctoral thesis, Humboldt-Universität zu Berlin, Medizinische Fakultät - Universitätsklinikum Charité, 2001. http://dx.doi.org/10.18452/14649.

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Murine Mikrogliakulturen wurden mit Astrozyten-konditioniertem Medium (ACM) in einen deaktivierten Zustand überführt. Dies wurde anhand morphologischer (Grad der Ramifizierung) und immunologischer (Expression von Adhäsionsmolekülen) Parameter verifiziert. Durch den Einsatz von Makrophagen-koloniestimulierenden Faktor (M-CSF), Granulozyten/Makrophagen-koloniestimulierenden Faktor (GM-CSF), transformierenden Wachstumsfaktor beta (TGF-beta) und den gegen sie gerichteten Antikörpern wurde gezeigt, daß alle untersuchten Zytokine in unterschiedlichem Maße an der Deaktivierung der Mikrogliazellen durch ACM beteiligt sind. Außerdem wurde nach Stimulation mit ACM an murinen Mikrogliazellen eine transiente Hochregulation eines Kaliumauswärtsstromes beobachtet Das Auftreten dieses Kalium-stromes nach Inkubation der Mikrogliazellen mit ACM konnte auf die Wirkung von TGF-beta, welches im ACM enthalten ist, zurückgeführt werden. Der durch ACM in deaktivierter Mikroglia induzierte Kaliumkanal entsprach in seinen kinetischen und pharma-kologischen Eigenschaften am ehesten dem klonierten Kanal Kv1.3. Die Kv1.3 Expression durch TGF-beta oder ACM war durch den unspezifischen Proteinkinaseinhibitor H7 unterdrückbar. Diese Ergebnisse zeigen, daß die Expression des Kv1.3 Kanals nicht, wie bisher angenommen, ein Indikator für aktivierte Mikroglia ist.
Murine microglial cultures were deactivated with astrocyte-conditioned medium (ACM). The deactivation process was verified measuring morphological (ramification index) and immunological (expression level of adhesion molecules) parameters. By using macrophage-colony stimulating factor (M-CSF), granulocyte/macrophage-colony stimulating factor (GM-CSF), transforming growth factor beta (TGF-beta) and their corresponding antibodies it was shown, that to a different extent all of these cytokines influence the deactivation process of microglial cells by ACM. ACM treatment of microglial cultures also lead to a transient upregulation of a delayed potassium outward current. This upregulation was due to the impact of TGF-beta contained in ACM. The ACM induced potassium channel resembled in its kinetic and pharmacological properties the cloned Kv1.3 channel. Expression of Kv1.3 in microglial cells by TGF-beta or ACM was inhibited by the unspecific protein kinase inhibitor H7. These results show, that expression of Kv1.3 channels is not a special feature of activated microglia, which has been proposed in recent publications.
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Arnoux, Isabelle. "Rôles et caractérisation de la microglie dans le développement du néocortex somatosensoriel de la souris." Phd thesis, Université René Descartes - Paris V, 2014. http://tel.archives-ouvertes.fr/tel-01070271.

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Les cellules microgliales, qui sont les macrophages du système nerveux central, ont été principalement étudiées en conditions pathologiques. Néanmoins, l'étude de la microglie aux stades périnataux indique qu'elle influence le développement normal du système nerveux central. Des interactions directes et indirectes entre la microglie et les synapses existent mais les mécanismes par lesquels ces cellules immunitaires ciblent les synapses et modulent leur maturation fonctionnelle durant le développement postnatal sont peu connus. Au cours de mon travail de thèse, je me suis intéressée aux cellules microgliales et à leurs fonctions dans le développement postnatal du cortex somato-sensoriel de la souris. Dans une première étude, nous avons montré qu'au cours de la première semaine post-natale le recrutement des cellules microgliales aux sites synaptiques en maturation met en jeu une voie de signalisation impliquant la chimiokine neuronale fractalkine et de son récepteur microglial CX3CR1. En effet, un défaut d'expression de ce récepteur retarde le recrutement des cellules microgliales aux sites synaptiques et entraine un retard de maturation fonctionnelle des synapses thalamocorticales. Dans une seconde étude, nous avons caractérisé le phénotype des cellules microgliales lors de la maturation fonctionnelle des réseaux synaptiques corticaux. Nous avons montré que les cellules microgliales adoptent un phénotype particulier lorsqu'elles sont recrutées aux synapses en maturation. Ce phénotype diffère de celui exprimé par la microglie adulte en conditions physiologiques et pathologiques et pourrait permettre aux cellules microgliales d'accomplir des fonctions spécifiques nécessaires à la maturation synaptique. Dans une troisième étude, nous avons testé les effets de la minocycline sur le développement cortical. Cette tétracycline est connue pour bloquer l'activation microgliale chez l'adulte. De façon surprenante, nous avons observé que pendant une période critique se situant à la fin de la première semaine post-natale la minocycline induit une importante mort cellulaire qui s'accompagne d'une altération de la distribution des cellules microgliales et déclenche leur activation. L'ensemble de mes données montrent que les cellules microgliales sont très sensibles aux changements de leur environnement, que leur phénotype fonctionnel change en conditions physiologiques en fonction de cet environnement et que des interactions réciproques entre neurones et microglie influencent la maturation fonctionnelle des réseaux synaptiques corticaux lors du développement postnatal.
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7

Serrano, Albarrás Antonio. "Heteromeric composition of the Kv 1.3 channelosome = Composició heteromèrica del canalosoma Kv1.3." Doctoral thesis, Universitat de Barcelona, 2018. http://hdl.handle.net/10803/665245.

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Ion channels are transmembrane proteins containing aqueous pores which, once open, permit the pass of ions through the plasma membrane. This ion flux takes places following the electrochemical gradient for the specific ion. Kv1.3 is a voltage-gated potassium channel which is member of the Shaker superfamily. Its basic structure consists in a protein with six transmembrane domains, while the functional channel is formed by 4 copies of this protein. Kv1.3 participates in a great amount of physiological functions: nervous system, immune system, insulin signaling or cell proliferation. In the immune system, Kv1.3 is highly expressed both in lymphocytes as well as in mononuclear phagocytes. In both cell types, Kv1.3 regulates the immune activation and cell proliferation. Moreover, Kv1.3 is coexpressed with other ion channel proteins like Kv1.5 or KCNE4 in the immune cells. Kv1.5 is able to heteromerize with Kv1.3, generating heterotetramers with variable stoichiometries. Those heterotetramers produce intermediate phenotypes depending on the ratio of the subunits that generate them. On the other side, KCNE4 may interact with Kv1.3, but not with Kv1.5. Kv1.3 is greatly inhibited by the association with either of the two proteins. In the present thesis we focus in characterizing these interactions and the importance of stoichiometry in their effects. We demonstrate that the associations between Kv1.3 and Kv1.5; and between Kv1.3 and KCNE4 take place in immune cells. Moreover, by using a fusion protein we get to fix the stoichiometry of the Kv1.3-Kv1.5 complex to 1:1. With this stoichiometry, Kv1.5 acts as a dominant negative toward Kv1.3 in the complex. Further interactions are characterized by using several chimeric proteins. By using those chimaeras, it is revealed that the carboxyterminal domain is necessary for the correct function of the channel. On the other hand, we demonstrate that KCNE4 is able to interact with Kv1.3 regardless of Kv1.5 presence. Furthermore, the presence of Kv1.5 in the Kv1.3-KCNE4 interaction results in this association potentiating the function of the channel, instead of inhibiting it. These results are replicated both in heterologous systems as well as in native cells. This discovery presents a new paradigm by which the association with several modulatory proteins may result in the modification of the effect of each one of them. Taking into account the sheer number of different ion channel subunits, the number of different potential phenotypes is increased by a huge margin. KCNE1 is a regulatory subunit, as well as KCNE4. Unlike KCNE4, though, KCNE1 can interact with Kv1.5. In the present thesis we demonstrate for the first time that KCNE1 is not only able to associate with Kv1.5, but to potentiate its activity by a huge amount. This interaction also seems to affect the membrane microdomain targeting of Kv1.5 Finally, the 4 studied proteins are expressed in T lymphocytes, which are the main actors in the pathogenicity of autoimmune diseases. Therefore, we genotyped those genes in multiple sclerosis patients to identify different polymorphisms which could be linked to immune overactivity. After analyzing the different polymorphisms, we located some which could be of special relevance for the physiopathology of autoimmune diseases.
Los canales iónicos son proteínas transmembrana que contienen poros acuosos que permiten el paso de iones a través de la membrana plasmática a favor de gradiente electroquímico. Kv1.3 es un canal de potasio dependiente de voltaje de la superfamilia Shaker. La estructura básica consiste en una proteína con seis dominios transmembrana y el canal funcional está formado por cuatro copias de esta proteína. Kv1.3 participa en multitud de funciones del organismo: sistema nervioso, sistema inmunitario, señalización de la insulina o proliferación celular. En el sistema inmunitario está altamente expresado tanto en linfocitos como en fagocitos mononucleares. En ambos tipos celulares regula la activación inmunitaria y la proliferación celular. Además, se ve coexpresado con otras proteínas de relevancia como Kv1.5 o KCNE4. Kv1.5 puede heteromerizar con Kv1.3, dando lugar a heterotrámeros de estequiometrias variables. Por otro lado, KCNE4 puede interaccionar con Kv1.3, pero no con Kv1.5. Kv1.3 se ve potentemente inhibido por ambas asociaciones. En la presente tesis nos centramos en caracterizar estas interacciones y el peso de la estequiometría en sus efectos. Demostramos que ambas asociaciones tienen lugar en células del sistema inmunitario. Además, mediante una proteína de fusión logramos fijar la estequiometría del complejo Kv1.3-Kv1-5 en 1:1. Así, Kv1.5 demuestra ejercer como dominante negativo respecto a Kv1.3 en el complejo. Estas interacciones intramoleculares son estudiadas mediante el uso de diversas proteínas quiméricas para dilucidar el peso de los extremos carboxiterminales en la formación del canal y su función. Por otro lado, demostramos que KCNE4 afecta el canal de estequiometría 1:1 aumentado su actividad, en lugar de reducirla. Este descubrimiento presenta un nuevo paradigma en que la asociación con varias proteínas reguladoras puede resultar en la modificación del efecto de cada una de ellas. KCNE1 es una proteína reguladora al igual que KCNE4, pero que interactúa con Kv1.5. En la presente tesis demostramos como KCNE1 no solo interacciona con Kv1.5, sino que aumenta en gran medida su actividad. Finalmente, también genotipamos estos genes en pacientes de una enfermedad autoinmune como es la esclerosis múltiple, llegando a localizar diversos polimorfismos de posible interés fisiopatológico.
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Venturini, Elisa [Verfasser], and Erich [Akademischer Betreuer] Gulbins. "Kv1.3 inhibitors in the treatment of glioma and melanoma / Elisa Venturini. Betreuer: Erich Gulbins." Duisburg, 2015. http://d-nb.info/108047885X/34.

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Martel, Julie. "Expression et caractérisation du canal potassique voltage-dépendant lymphocytaire Kv1.3 chez les cellules HEK 293." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq26390.pdf.

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Martel, Julie. "Expression et caractérisation du canal potassique voltage-dépendant lymphocytaire Kv1.3 chez les cellules HEK 293." Sherbrooke : Université de Sherbrooke, 1997.

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Books on the topic "Kv3.3"

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Cayabyab, Francisco Sandoval. Kv1.3 and erg K+ channels in microglia: Regulation by tyrosine phosphorylation. 2002.

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Ahmed, Ishtiaq. Ensnaring the pancreatic alpha-cell, and, Syntaxin 1A modulation of the alpha-cell Kv4.3 channel. 2006.

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Chung, In Duk. Modulation of the Kv1.3 channel by protein phosphorylation in human T lymphocytes: A patch-clamp study. 1996.

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Amadeus, Mozart Wolfgang. Music Minus One Flute: Mozart Concerto No. 1 in G major, KV313 (KV285c) (Book & Digitally Remastered 2 CD Set). Music Minus One, 1997.

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Book chapters on the topic "Kv3.3"

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Feofanov, Alexey V., Kseniya S. Kudryashova, Anastasiya A. Ignatova, and Oksana V. Nekrasova. "Recombinant Fluorescent Ligand of Potassium Kv1.1 and Kv1.3 Channels: Design, Properties and Applications." In Springer Proceedings in Physics, 11–16. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-46601-9_2.

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"Kv6.3." In Encyclopedia of Signaling Molecules, 2802. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_102013.

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Mak, Tak W., Josef Penninger, John Roder, Janet Rossant, and Mary Saunders. "Kv3.1." In The Gene Knockout FactsBook, 655–57. Elsevier, 1998. http://dx.doi.org/10.1016/b978-012466044-1/50366-5.

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Conference papers on the topic "Kv3.3"

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Hinkle, Andrew, Megan Yuasa, David Peckham, Craig Phillips, Shawn Iadonato, Peter Probst, Keith Elkon, and Anne M. Stevens. "AI-01 Kv1.3 expression on systemic lupus erythematosus (SLE) urinary leukocytes." In LUPUS 21ST CENTURY 2018 CONFERENCE, Abstracts of the Fourth Biannual Scientific Meeting of the North and South American and Caribbean Lupus Community, Armonk, New York, USA, September 13 – 15, 2018. Lupus Foundation of America, 2018. http://dx.doi.org/10.1136/lupus-2018-lsm.1.

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Estrada, Rosendo, Redwan Huq, Rajeev Tajhya, Satendra Chauhan, Christine Beeton, and Michael W. Pennington. "Kv1.3 Selective Peptides Based Upon N-Terminal Extension and Internal Substitutions of ShK Toxin." In The 24th American Peptide Symposium. Prompt Scientific Publishing, 2015. http://dx.doi.org/10.17952/24aps.2015.238.

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Li, Weiwei, Gregory Wilson, Magdalena Bachmann, Jiang Wang, Michael Edwards, Ildiko Szabo, Erich Gulbins, Syed Ahmad, and Sameer Patel. "Abstract 2742: The role and mechanism of voltage-gated potassium channel, Kv1.3, in pancreatic ductal adenocarcinoma (PDAC)." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-2742.

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Stafford, Lewis J., Sharon Willis, Joseph Rucker, Benjamin Doranz, and Ross Chambers. "Abstract 527: Isolation of large and diverse monoclonal antibody panels against the multipass membrane protein targets Kv1.3, P2X7, and Claudin 18.2." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-527.

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