Relevant bibliographies by topics / Tandem Pore Domain

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  2. Dissertations / Theses

Academic literature on the topic 'Tandem Pore Domain'

Author: Grafiati
Published: 4 June 2021
Last updated: 7 February 2022

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Journal articles on the topic "Tandem Pore Domain"

1

Yost, C. "Update on Tandem Pore (2P) Domain K+ Channels." Current Drug Targets 4, no. 4 (May 1, 2003): 347–51. http://dx.doi.org/10.2174/1389450033491091.

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2

Kindler, Christoph H., Spencer C. Yost, and Andrew T. Gray. "Local Anesthetic Inhibition of Baseline Potassium Channels with Two Pore Domains in Tandem." Anesthesiology 90, no. 4 (April 1, 1999): 1092–102. http://dx.doi.org/10.1097/00000542-199904000-00024.

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Background Recently, a new structural family of potassium channels characterized by two pore domains in tandem within their primary amino acid sequence was identified. These tandem pore domain potassium channels are not gated by voltage and appear to be involved in the control of baseline membrane conductances. The goal of this study was to identify mechanisms of local anesthetic action on these channels. Methods Oocytes of Xenopus laevis were injected with cRNA from five cloned tandem pore domain baseline potassium channels (TASK, TREK-1, TOK1, ORK1, and TWIK-1), and the effects of several local anesthetics on the heterologously expressed channels were assayed using two-electrode voltage-clamp and current-clamp techniques. Results Bupivacaine (1 mM) inhibited all studied tandem pore potassium channels, with TASK inhibited most potently. The potency of inhibition was directly correlated with the octanol: buffer distribution coefficient of the local anesthetic, with the exception of tetracaine, to which TASK is relatively insensitive. The approximate 50% inhibitory concentrations of TASK were 709 microM mepivacaine, 222 microM lidocaine, 51 microM R(+)-ropivacaine, 53 microM S(-)-ropivacaine, 668 microM tetracaine, 41 microM bupivacaine, and 39 microM etidocaine. Local anesthetics (1 mM) significantly depolarized the resting membrane potential of TASK cRNA-injected oocytes compared with saline-injected control oocytes (tetracaine 22+/-6 mV rs. 7+/-1 mV, respectively, and bupivacaine 31+/-7 mV vs. 6+/-4 mV). Conclusions Local anesthetics inhibit tandem pore domain baseline potassium channels, and they could depolarize the resting membrane potential of cells expressing these channels. Whether inhibition of these channels contributes to conduction blockade or to the adverse effects of local anesthetics remains to be determined.
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3

Rajan, Sindhu, Erhard Wischmeyer, Gong Xin Liu, Regina Preisig-Müller, Jürgen Daut, Andreas Karschin, and Christian Derst. "TASK-3, a Novel Tandem Pore Domain Acid-sensitive K+Channel." Journal of Biological Chemistry 275, no. 22 (March 27, 2000): 16650–57. http://dx.doi.org/10.1074/jbc.m000030200.

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4

Gray, Andrew T., Byron B. Zhao, Christoph H. Kindler, Bruce D. Winegar, Matthew J. Mazurek, Jie Xu, Raymond A. Chavez, John R. Forsayeth, and C. Spencer Yost. "Volatile Anesthetics Activate the Human Tandem Pore Domain Baseline K+Channel KCNK5." Anesthesiology 92, no. 6 (June 1, 2000): 1722–30. http://dx.doi.org/10.1097/00000542-200006000-00032.

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Background Previous studies have identified a volatile anesthetic-induced increase in baseline potassium permeability and concomitant neuronal inhibition. The emerging family of tandem pore domain potassium channels seems to function as baseline potassium channels in vivo. Therefore, we studied the effects of clinically used volatile anesthetics on a recently described member of this family. Methods A cDNA clone containing the coding sequence of KCNK5 was isolated from a human brain library. Expression of KCNK5 in the central nervous system was determined by Northern blot analysis and reverse-transcription polymerase chain reaction. Functional expression of the channel was achieved by injection of cRNA into Xenopus laevis oocytes. Results Expression of KCNK5 was detected in cerebral cortex, medulla, and spinal cord. When heterologously expressed in Xenopus oocytes, KCNK5 currents exhibited delayed activation, outward rectification, proton sensitivity, and modulation by protein kinase C. Clinical concentrations of volatile general anesthetics potentiated KCNK5 currents by 8-30%. Conclusion Human KCNK5 is a tandem pore domain potassium channel exhibiting delayed activation and sensitivity to volatile anesthetics and may therefore have a role in suppressing cellular excitability during general anesthesia.
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Yost, C. "Tandem Pore Domain K Channels An Important Site of Volatile Anesthetic Action." Current Drug Targets 1, no. 2 (September 1, 2000): 207–17. http://dx.doi.org/10.2174/1389450003349335.

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6

Bina, Robert Wagner, and Steven C. Hempleman. "Evidence for TREK-like tandem-pore domain channels in intrapulmonary chemoreceptor chemotransduction." Respiratory Physiology & Neurobiology 156, no. 2 (May 2007): 120–31. http://dx.doi.org/10.1016/j.resp.2006.09.005.

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7

Kananura, Colette, Thomas Sander, Sindhu Rajan, Regina Preisig-Müller, Karl-Heinz Grzeschik, Jürgen Daut, Christian Derst, and Ortrud K. Steinlein. "Tandem pore domain K+-channel TASK-3 (KCNK9) and idiopathic absence epilepsies." American Journal of Medical Genetics 114, no. 2 (January 9, 2002): 227–29. http://dx.doi.org/10.1002/ajmg.10201.

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8

Johnson, Rosalyn P., Ita M. O'Kelly, and Ian M. Fearon. "System-specific O2 sensitivity of the tandem pore domain K+ channel TASK-1." American Journal of Physiology-Cell Physiology 286, no. 2 (February 2004): C391—C397. http://dx.doi.org/10.1152/ajpcell.00401.2003.

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Hypoxic inhibition of TASK-1, a tandem pore domain background K+ channel, provides a critical link between reduced O2 levels and physiological responses in various cell types. Here, we examined the expression and O2 sensitivity of TASK-1 in immortalized adrenomedullary chromaffin (MAH) cells. In physiological (asymmetrical) K+ solutions, 3 μM anandamide or 300 μM Zn2+ inhibited a strongly pH-sensitive current. Under symmetrical K+ conditions, the anandamide- and Zn2+-sensitive K+ currents were voltage independent. These data demonstrate the functional expression of TASK-1, and cellular expression of this channel was confirmed by RT-PCR and Western blotting. At concentrations that selectively inhibit TASK-1, anandamide and Zn2+ were without effect on the magnitude of the O2-sensitive current or the hypoxic depolarization. Thus TASK-1 does not contribute to O2 sensing in MAH cells, demonstrating the failure of a known O2-sensitive K+ channel to respond to hypoxia in an O2-sensing cell. These data demonstrate that, ultimately, the sensitivity of a particular K+ channel to hypoxia is determined by the cell, and we propose that this is achieved by coupling distinct hypoxia signaling systems to individual channels. Importantly, these data also reiterate the indirect O2 sensitivity of TASK-1, which appears to require the presence of an intracellular mediator.
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9

Skatchkov, S. N., M. J. Eaton, Y. M. Shuba, Y. V. Kucheryavykh, C. Derst, R. W. Veh, A. Wurm, et al. "Tandem-pore domain potassium channels are functionally expressed in retinal (Müller) glial cells." Glia 53, no. 3 (2005): 266–76. http://dx.doi.org/10.1002/glia.20280.

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10

Ji, Xin-cai, Wan-hong Zhao, Dong-xu Cao, Qiao-qiao Shi, and Xiao-liang Wang. "Novel neuroprotectant chiral 3-n-butylphthalide inhibits tandem-pore-domain potassium channel TREK-1." Acta Pharmacologica Sinica 32, no. 2 (February 2011): 182–87. http://dx.doi.org/10.1038/aps.2010.210.

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Dissertations / Theses on the topic "Tandem Pore Domain"

1

Gabriel, Luke R. "Dynamic Regulation at the Neuronal Plasma Membrane: Novel Endocytic Mechanisms Control Anesthetic-Activated Potassium Channels and Amphetamine-Sensitive Dopamine Transporters: A Dissertation." eScholarship@UMMS, 2013. http://escholarship.umassmed.edu/gsbs_diss/725.

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Endocytic trafficking dynamically regulates neuronal plasma membrane protein presentation and activity, and plays a central role in excitability and plasticity. Over the course of my dissertation research I investigated endocytic mechanisms regulating two neuronal membrane proteins: the anesthetic-activated potassium leak channel, KCNK3, as well as the psychostimulant-sensitive dopamine transporter (DAT). My results indicate that KCNK3 internalizes in response to Protein Kinase C (PKC) activation, using a novel pathway that requires the phosphoserine binding protein, 14-3-3β, and demonstrates for the first time regulated KCNK3 channel trafficking in neurons. Additionally, PKC-mediated KCNK3 trafficking requires a non-canonical endocytic motif, which is shared exclusively between KCNK3 and sodium-dependent neurotransmitter transporters, such as DAT. DAT trafficking studies in intact ex vivo adult striatal slices indicate that DAT endocytic trafficking has both dynamin-dependent and –independent components. Moreover, DAT segregates into two populations at the neuronal plasma membrane: trafficking-competent and -incompetent. Taken together, these results demonstrate that novel, non-classical endocytic mechanisms dynamically control the plasma membrane presentation of these two important neuronal proteins.
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