Results 171 to 180 of about 27,267,955 (206)
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Altered anoctamin-1 and tyrosine phosphorylation in congenital ureteropelvic junction obstruction.
Journal of Pediatric Surgery, 2020PURPOSE Ureteropelvic junction (UPJ) obstruction is the most common cause of congenital hydronephrosis in children. The pathophysiology of UPJ obstruction and the exact mechanism of pelviureteral peristalsis are poorly understood.
M. Hunziker +4 more
semanticscholar +3 more sources
Function and Regulation of the Calcium-Activated Chloride Channel Anoctamin 1 (TMEM16A).
Handbook of Experimental Pharmacology, 2022Various human tissues express the calcium-activated chloride channel Anoctamin 1 (ANO1), also known as TMEM16A. ANO1 allows the passive chloride flux that controls different physiological functions ranging from muscle contraction, fluid and hormone secretion, gastrointestinal motility, and electrical excitability.
J. Arreola +5 more
semanticscholar +3 more sources
Cancer Biotherapy and Radiopharmaceuticals, 2018
G. Lu, Wanling Shi, Hongyu Zheng
exaly +2 more sources
G. Lu, Wanling Shi, Hongyu Zheng
exaly +2 more sources
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
openaire +2 more sources
A Ca2+‐activated Cl‐ Channel Anoctamin‐1 Regulates Mitochondrial Morphology
The FASEB Journal, 2022The Ca2+‐activated Cl‐ channel Anoctamin‐1 (Ano1) regulates multiple cell functions including cell proliferation, survival, and migration. We previously reported that overexpression of Ano1 is associated with hyperproliferation of pulmonary artery ...
Isabel Chaput +7 more
semanticscholar +1 more source
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
openaire +2 more sources
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
openaire +2 more sources
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
exaly +3 more sources
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
openaire +2 more sources
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
openaire +4 more sources

