TMEM16A-encoded anoctamin 1 inhibition contributes to chrysin-induced coronary relaxation
نویسندگان
چکیده
منابع مشابه
Anoctamin 1 (TMEM16A) is essential for testosterone-induced prostate hyperplasia.
Benign prostatic hyperplasia (BPH) is characterized by an enlargement of the prostate, causing lower urinary tract symptoms in elderly men worldwide. However, the molecular mechanism underlying the pathogenesis of BPH is unclear. Anoctamin1 (ANO1) encodes a Ca(2+)-activated chloride channel (CaCC) that mediates various physiological functions. Here, we demonstrate that it is essential for testo...
متن کاملAnoctamin 1 contributes to inflammatory and nerve-injury induced hypersensitivity
BACKGROUND Various pathological conditions such as inflammation or injury can evoke pain hypersensitivity. That represents the response to innocuous stimuli or exaggerated response to noxious stimuli. The molecular mechanism based on the pain hypersensitivity is associated with changes in many of ion channels in dorsal-root ganglion (DRG) neurons. Anoctamin 1 (ANO1/TMEM16A), a Ca2+ activated ch...
متن کاملChronic proteasome inhibition contributes to coronary atherosclerosis.
The proteasome is responsible for the degradation of oxidized proteins, and proteasome inhibition has been shown to generate oxidative stress in vitro. Atherosclerosis is thought to be initiated as a consequence of increased endogenous oxidative stress. The current study was designed to assess whether chronic proteasome inhibition is associated with early coronary atherosclerosis. Female pigs, ...
متن کاملAnoctamin-1/TMEM16A is the major apical iodide channel of the thyrocyte.
Iodide 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. Here, we show that a recently discovered Ca(2+)-activated a...
متن کاملTMEM16A(a)/anoctamin-1 Shares a Homodimeric Architecture with CLC Chloride Channels*
TMEM16A/anoctamin-1 has been identified as a protein with the classic properties of a Ca(2+)-activated chloride channel. Here, we used blue native polyacrylamide gel electrophoresis (BN-PAGE) and chemical cross-linking to assess the quaternary structure of the mouse TMEM16A(a) and TMEM16A(ac) splice variants as well as a genetically concatenated TMEM16A(a) homodimer. The constructs carried hexa...
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ژورنال
عنوان ژورنال: Biomedicine & Pharmacotherapy
سال: 2020
ISSN: 0753-3322
DOI: 10.1016/j.biopha.2020.110766