Results 161 to 170 of about 5,018 (188)
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Pflugers Archiv European Journal of Physiology, 2015
The P2X7 receptor (P2X7R) is a ligand-gated ion channel that conducts Na(+), K(+), and Ca(2+) when activated by extracellular ATP. In various cell types, such as secretory epithelia, the P2X7R is co-expressed with Ca(2+)-dependent Cl(-) channels of the TMEM16/anoctamin family. Here, we studied whether the P2X7R and TMEM16A/anoctamin-1 (Ano1) or TMEM16F/
Silvia Detro-Dassen, Fritz Markwardt
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The P2X7 receptor (P2X7R) is a ligand-gated ion channel that conducts Na(+), K(+), and Ca(2+) when activated by extracellular ATP. In various cell types, such as secretory epithelia, the P2X7R is co-expressed with Ca(2+)-dependent Cl(-) channels of the TMEM16/anoctamin family. Here, we studied whether the P2X7R and TMEM16A/anoctamin-1 (Ano1) or TMEM16F/
Silvia Detro-Dassen, Fritz Markwardt
exaly +3 more sources
Advances in Anoctamin 1: A Potential New Drug Target in Medicinal Chemistry
Current Topics in Medicinal Chemistry, 2021ANO1, anoctamin 1(also known as TMEM16A), is the molecular basis of calcium-activated chloride channels with ten transmembrane segments which are widely expressed in mammalian cells, including epithelial cells, vascular smooth muscle tissues, electro-excitatory cells, and some tumor cells.
Junjie Zhong, Xiaosheng Qu, Xin Cao
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Anoctamin 1 in secretory epithelia
Cell Calcium, 2014Fluid and electrolyte releasing from secretory epithelia are elaborately regulated by orchestrated activity of ion channels. The activity of chloride channel at the apical membrane decides on the direction and the rate of secretory fluid and electrolyte.
Yongwoo, Jang, Uhtaek, Oh
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Expression patterns of anoctamin 1 and anoctamin 2 chloride channels in the mammalian nose
Cell and Tissue Research, 2012Calcium-activated chloride channels are expressed in chemosensory neurons of the nose and contribute to secretory processes and sensory signal transduction. These channels are thought to be members of the family of anoctamins (alternative name: TMEM16 proteins), which are opened by micromolar concentrations of intracellular Ca(2+).
Kristin, Dauner +4 more
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Relationship between TMEM16A/anoctamin 1 and LRRC8A
Pflügers Archiv - European Journal of Physiology, 2016TMEM16A/anoctamin 1/ANO1 and VRAC/LRRC8 are independent chloride channels activated either by increase in intracellular Ca(2+) or cell swelling, respectively. In previous studies, we observed overlapping properties for both types of channels. (i) TMEM16A/ANO1 and LRRC8 are inhibited by identical compounds, (ii) the volume-regulated anion channel VRAC ...
Roberta, Benedetto +8 more
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Anoctamin 1 expression in the mouse auditory brainstem
Cell and Tissue Research, 2014Calcium-activated chloride channels (CaCCs) are involved in numerous physiological functions, including the epithelial movement of fluid. Anoctamin 1 (ANO1) has recently been cloned and characterized as a CaCC and is known to be expressed in various secretory epithelia and in nervous tissues such as the dorsal root ganglia and retina.
Sang Jae, Cho +4 more
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Blockade of anoctamin-1 in injured and uninjured nerves reduces neuropathic pain
Brain Research, 2018The aim of this study was to determine the participation of anoctamin-1 in 2 models of neuropathic pain in rats (L5/L6 spinal nerve ligation [SNL] and L5 spinal nerve transection [SNT]). SNL and SNT diminished withdrawal threshold in rats. Moreover, SNL up-regulated anoctamin-1 protein expression in injured L5 and uninjured L4 DRG whereas that it ...
Guadalupe Garcia +2 more
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Protons inhibit anoctamin 1 by competing with calcium
Cell Calcium, 2015Cl(-) efflux through Ca(2+)-activated Cl(-) channels (CaCCs) in secretory epithelial cells plays a key role in the regulation of fluid secretion. The fluid and electrolyte secretion is closely related to intracellular pH. CaCCs have been known to be inhibited by intracellular acid.
Hyeyeon, Chun +6 more
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Anoctamin-1/TMEM16A is the major apical iodide channel of the thyrocyte
American Journal of Physiology-Cell Physiology, 2014Iodide is captured by thyrocytes through the Na+/I− symporter (NIS) before being released into the follicular lumen, where it is oxidized and incorporated into thyroglobulin for the production of thyroid hormones. Several reports point to pendrin as a candidate protein for iodide export from thyroid cells into the follicular lumen.
Twyffels, L. +10 more
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