Results 171 to 180 of about 4,623 (196)

TMEM16A Mediates Mucus Production in Human Airway Epithelial Cells

open access: yesAmerican Journal of Respiratory Cell and Molecular Biology, 2021
TMEM16A is a Ca2+-activated chloride channel that was shown to enhance production and secretion of mucus in inflamed airways. It is, however, not clear whether TMEM16A directly supports mucus production, or whether mucin and TMEM16A are upregulated ...
Inés Cabrita   +2 more
exaly   +2 more sources

Pharmacological characterization of TMEM16A currents [PDF]

open access: yesChannels, 2014
Recent studies have shown that transmembrane protein 16 A (TMEM16A) is a subunit of calcium-activated chloride channels (CACCs). Pharmacological agents have been used to probe the functional role of CACCs, however their effect on TMEM16A currents has not been systematically investigated.
Timothy I Webb   +2 more
exaly   +3 more sources
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Emerging Modulators of TMEM16A and Their Therapeutic Potential

The Journal of Membrane Biology, 2021
Calcium-activated chloride channels (CaCCs) are widespread chloride channels which rely on calcium activation to perform their functions. In 2008, TMEM16A (also known as anoctamin1, ANO1) was identified as the molecular basis of the CaCCs, which provided the possibility to study the physiological function of CaCCs.
Anqi Hao   +6 more
openaire   +2 more sources

Mucus Release and Airway Constriction by TMEM16A May Worsen Pathology in Inflammatory Lung Disease [PDF]

open access: yesInternational Journal of Molecular Sciences, 2021
Activation of the Ca2+ activated Cl- channel TMEM16A is proposed as a treatment in inflammatory airway disease. It is assumed that activation of TMEM16A will induce electrolyte secretion, and thus reduce airway mucus plugging and improve mucociliary ...
Raquel Centeio   +2 more
exaly   +2 more sources

Paving the way for designing drugs targeting TMEM16A

Trends in Pharmacological Sciences, 2021
The calcium-activated chloride channel TMEM16A is involved in several physiological processes and is an important pharmacological target. Dinsdale and colleagues recently unveiled several residues in the outer pore region that constitute a critical site for the design of drugs that modulate TMEM16A channels.
Simone Pifferi, Anna Menini
openaire   +2 more sources

Dysregulation of TMEM16A impairs oviductal transport of embryos

American Journal of Physiology-Cell Physiology, 2023
The ion channel protein TMEM16A is expressed in the epithelium and smooth muscle of the human fallopian tube and is upregulated in patients with tubal pregnancy. TMEM16A is involved in regulating the smooth muscle contraction and the cilia beating. Dysregulated TMEM16A may result in embryo retention in the oviduct and delayed early embryo development.
Nannan Ning   +8 more
openaire   +2 more sources

An outer-pore gate modulates the pharmacology of the TMEM16A channel [PDF]

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2021
Significance The TMEM16A calcium-gated chloride channels participate in a range of vital physiological functions. TMEM16A channels are desirable new drug targets as their dysfunction can lead to pathology. In spite of this, their pharmacology is still in its infancy. Gaining insight into the mode of action and binding sites for test compounds
Ria L Dinsdale   +2 more
exaly   +4 more sources

Downregulation of Ca2+-Activated Cl− Channel TMEM16A by the Inhibition of Histone Deacetylase in TMEM16A-Expressing Cancer Cells

The Journal of Pharmacology and Experimental Therapeutics, 2014
The Ca(2+)-activated Cl(-) channel transmembrane proteins with unknown function 16 A (TMEM16A; also known as anoctamin 1 or discovered on gastrointestinal stromal tumor 1) plays an important role in facilitating the cell growth and metastasis of TMEM16A-expressing cancer cells.
Sayo, Matsuba   +9 more
openaire   +2 more sources

Recent advances in TMEM16A: Structure, function, and disease

Journal of Cellular Physiology, 2018
AbstractTMEM16A (also known as anoctamin 1, ANO1) is the molecular basis of the calcium‐activated chloride channels, with ten transmembrane segments. Recently, atomic structures of the transmembrane domains of mouse TMEM16A (mTMEM16A) were determined by single‐particle electron cryomicroscopy.
Qiushuang Ji   +6 more
openaire   +2 more sources

Relationship between TMEM16A/anoctamin 1 and LRRC8A

Pflügers Archiv - European Journal of Physiology, 2016
TMEM16A/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

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