Relevant bibliographies by topics / TMEM16B

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Academic literature on the topic 'TMEM16B'

Author: Grafiati
Published: 14 March 2023

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Journal articles on the topic "TMEM16B"

1

Pedemonte, Nicoletta, and Luis J. V. Galietta. "Structure and Function of TMEM16 Proteins (Anoctamins)." Physiological Reviews 94, no. 2 (April 2014): 419–59. http://dx.doi.org/10.1152/physrev.00039.2011.

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TMEM16 proteins, also known as anoctamins, are involved in a variety of functions that include ion transport, phospholipid scrambling, and regulation of other membrane proteins. The first two members of the family, TMEM16A (anoctamin-1, ANO1) and TMEM16B (anoctamin-2, ANO2), function as Ca2+-activated Cl−channels (CaCCs), a type of ion channel that plays important functions such as transepithelial ion transport, smooth muscle contraction, olfaction, phototransduction, nociception, and control of neuronal excitability. Genetic ablation of TMEM16A in mice causes impairment of epithelial Cl−secretion, tracheal abnormalities, and block of gastrointestinal peristalsis. TMEM16A is directly regulated by cytosolic Ca2+as well as indirectly by its interaction with calmodulin. Other members of the anoctamin family, such as TMEM16C, TMEM16D, TMEM16F, TMEM16G, and TMEM16J, may work as phospholipid scramblases and/or ion channels. In particular, TMEM16F (ANO6) is a major contributor to the process of phosphatidylserine translocation from the inner to the outer leaflet of the plasma membrane. Intriguingly, TMEM16F is also associated with the appearance of anion/cation channels activated by very high Ca2+concentrations. Furthermore, a TMEM16 protein expressed in Aspergillus fumigatus displays both ion channel and lipid scramblase activity. This finding suggests that dual function is an ancestral characteristic of TMEM16 proteins and that some members, such as TMEM16A and TMEM16B, have evolved to a pure channel function. Mutations in anoctamin genes ( ANO3, ANO5, ANO6, and ANO10) cause various genetic diseases. These diseases suggest the involvement of anoctamins in a variety of cell functions whose link with ion transport and/or lipid scrambling needs to be clarified.
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Schreiber, Rainer, Jiraporn Ousingsawat, and Karl Kunzelmann. "Targeting of Intracellular TMEM16 Proteins to the Plasma Membrane and Activation by Purinergic Signaling." International Journal of Molecular Sciences 21, no. 11 (June 5, 2020): 4065. http://dx.doi.org/10.3390/ijms21114065.

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Anoctamins such as TMEM16A and TMEM16B are Ca2+-dependent Cl− channels activated through purinergic receptor signaling. TMEM16A (ANO1), TMEM16B (ANO2) and TMEM16F (ANO6) are predominantly expressed at the plasma membrane and are therefore well accessible for functional studies. While TMEM16A and TMEM16B form halide-selective ion channels, TMEM16F and probably TMEM16E operate as phospholipid scramblases and nonselective ion channels. Other TMEM16 paralogs are expressed mainly in intracellular compartments and are therefore difficult to study at the functional level. Here, we report that TMEM16E (ANO5), -H (ANO8), -J (ANO9) and K (ANO10) are targeted to the plasma membrane when fused to a C-terminal CAAX (cysteine, two aliphatic amino acids plus methionin, serine, alanin, cystein or glutamin) motif. These paralogs produce Ca2+-dependent ion channels. Surprisingly, expression of the TMEM16 paralogs in the plasma membrane did not produce additional scramblase activity. In contrast, endogenous scrambling induced by stimulation of purinergic P2X7 receptors was attenuated, in parallel with reduced plasma membrane blebbing. This could suggest that intracellular TMEM16 paralogs operate differently when compared to plasma membrane-localized TMEM16F, and may even stabilize intracellular membranes. Alternatively, CAAX tagging, which leads to expression in non-raft compartments of the plasma membrane, may antagonize phosphatidylserine exposure by endogenous raft-located TMEM16F. CAAX-containing constructs may be useful to further investigate the molecular properties of intracellular TMEM16 proteins.
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Thomas-Gatewood, Candice, Zachary P. Neeb, Simon Bulley, Adebowale Adebiyi, John P. Bannister, M. Dennis Leo, and Jonathan H. Jaggar. "TMEM16A channels generate Ca2+-activated Cl− currents in cerebral artery smooth muscle cells." American Journal of Physiology-Heart and Circulatory Physiology 301, no. 5 (November 2011): H1819—H1827. http://dx.doi.org/10.1152/ajpheart.00404.2011.

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Transmembrane protein (TMEM)16A channels are recently discovered membrane proteins that display electrophysiological properties similar to classic Ca2+-activated Cl− (ClCa) channels in native cells. The molecular identity of proteins that generate ClCa currents in smooth muscle cells (SMCs) of resistance-size arteries is unclear. Similarly, whether cerebral artery SMCs generate ClCa currents is controversial. Here, using molecular biology and patch-clamp electrophysiology, we examined TMEM16A channel expression and characterized Cl− currents in arterial SMCs of resistance-size rat cerebral arteries. RT-PCR amplified transcripts for TMEM16A but not TMEM16B–TMEM16H, TMEM16J, or TMEM16K family members in isolated pure cerebral artery SMCs. Western blot analysis using an antibody that recognized recombinant (r)TMEM16A channels detected TMEM16A protein in cerebral artery lysates. Arterial surface biotinylation and immunofluorescence indicated that TMEM16A channels are located primarily within the arterial SMC plasma membrane. Whole cell ClCa currents in arterial SMCs displayed properties similar to those generated by rTMEM16A channels, including Ca2+ dependence, current-voltage relationship linearization by an elevation in intracellular Ca2+ concentration, a Nerstian shift in reversal potential induced by reducing the extracellular Cl− concentration, and a negative reversal potential shift when substituting extracellular I− for Cl−. A pore-targeting TMEM16A antibody similarly inhibited both arterial SMC ClCa and rTMEM16A currents. TMEM16A knockdown using small interfering RNA also inhibited arterial SMC ClCa currents. In summary, these data indicate that TMEM16A channels are expressed, insert into the plasma membrane, and generate ClCa currents in cerebral artery SMCs.
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4

Gyobu, Sayuri, Haruhiko Miyata, Masahito Ikawa, Daiju Yamazaki, Hiroshi Takeshima, Jun Suzuki, and Shigekazu Nagata. "A Role of TMEM16E Carrying a Scrambling Domain in Sperm Motility." Molecular and Cellular Biology 36, no. 4 (December 14, 2015): 645–59. http://dx.doi.org/10.1128/mcb.00919-15.

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Transmembrane protein 16E (TMEM16E) belongs to the TMEM16 family of proteins that have 10 transmembrane regions and appears to localize intracellularly. Although TMEM16E mutations cause bone fragility and muscular dystrophy in humans, its biochemical function is unknown. In the TMEM16 family, TMEM16A and -16B serve as Ca2+-dependent Cl−channels, while TMEM16C, -16D, -16F, -16G, and -16J support Ca2+-dependent phospholipid scrambling. Here, we show that TMEM16E carries a segment composed of 35 amino acids homologous to the scrambling domain in TMEM16F. When the corresponding segment of TMEM16A was replaced by this 35-amino-acid segment of TMEM16E, the chimeric molecule localized to the plasma membrane and supported Ca2+-dependent scrambling. We next establishedTMEM16E-deficient mice, which appeared to have normal skeletal muscle. However, fertility was decreased in the males. We found that TMEM16E was expressed in germ cells in early spermatogenesis and thereafter and localized to sperm tail.TMEM16E−/−sperm showed no apparent defect in morphology, beating, mitochondrial function, capacitation, or binding to zona pellucida. However, they showed reduced motility and inefficient fertilization of cumulus-free but zona-intact eggsin vitro. Our results suggest that TMEM16E may function as a phospholipid scramblase at inner membranes and that its defect affects sperm motility.
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Scudieri, Paolo, Elvira Sondo, Emanuela Caci, Roberto Ravazzolo, and Luis J. V. Galietta. "TMEM16A–TMEM16B chimaeras to investigate the structure–function relationship of calcium-activated chloride channels." Biochemical Journal 452, no. 3 (May 31, 2013): 443–55. http://dx.doi.org/10.1042/bj20130348.

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TMEM16A and TMEM16B proteins are CaCCs (Ca2+-activated Cl− channels) with eight putative transmembrane segments. As shown previously, expression of TMEM16B generates CaCCs characterized by a 10-fold lower Ca2+ affinity and by faster activation and deactivation kinetics with respect to TMEM16A. To investigate the basis of the different properties, we generated chimaeric proteins in which different domains of the TMEM16A protein were replaced by the equivalent domains of TMEM16B. Replacement of the N-terminus, TMD (transmembrane domain) 1–2, the first intracellular loop and TMD3–4 did not change the channel's properties. Instead, replacement of intracellular loop 3 decreased the apparent Ca2+ affinity by nearly 8-fold with respect to wild-type TMEM16A. In contrast, the membrane currents derived from chimaeras containing TMD7–8 or the C-terminus of TMEM16B showed higher activation and deactivation rates without a change in Ca2+ sensitivity. Significantly accelerated kinetics were also found when the entire C-terminus of the TMEM16A protein (77 amino acid residues) was deleted. Our findings indicate that the third intracellular loop of TMEM16A and TMEM16B is the site involved in Ca2+-sensitivity, whereas the C-terminal part, including TMD7–8, affect the rate of transition between the open and the closed state.
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Agostinelli, Emilio, and Paolo Tammaro. "Polymodal Control of TMEM16x Channels and Scramblases." International Journal of Molecular Sciences 23, no. 3 (January 29, 2022): 1580. http://dx.doi.org/10.3390/ijms23031580.

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The TMEM16A/anoctamin-1 calcium-activated chloride channel (CaCC) contributes to a range of vital functions, such as the control of vascular tone and epithelial ion transport. The channel is a founding member of a family of 10 proteins (TMEM16x) with varied functions; some members (i.e., TMEM16A and TMEM16B) serve as CaCCs, while others are lipid scramblases, combine channel and scramblase function, or perform additional cellular roles. TMEM16x proteins are typically activated by agonist-induced Ca2+ release evoked by Gq-protein-coupled receptor (GqPCR) activation; thus, TMEM16x proteins link Ca2+-signalling with cell electrical activity and/or lipid transport. Recent studies demonstrate that a range of other cellular factors—including plasmalemmal lipids, pH, hypoxia, ATP and auxiliary proteins—also control the activity of the TMEM16A channel and its paralogues, suggesting that the TMEM16x proteins are effectively polymodal sensors of cellular homeostasis. Here, we review the molecular pathophysiology, structural biology, and mechanisms of regulation of TMEM16x proteins by multiple cellular factors.
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7

Betto, Giulia, O. Lijo Cherian, Simone Pifferi, Valentina Cenedese, Anna Boccaccio, and Anna Menini. "Interactions between permeation and gating in the TMEM16B/anoctamin2 calcium-activated chloride channel." Journal of General Physiology 143, no. 6 (May 26, 2014): 703–18. http://dx.doi.org/10.1085/jgp.201411182.

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At least two members of the TMEM16/anoctamin family, TMEM16A (also known as anoctamin1) and TMEM16B (also known as anoctamin2), encode Ca2+-activated Cl− channels (CaCCs), which are found in various cell types and mediate numerous physiological functions. Here, we used whole-cell and excised inside-out patch-clamp to investigate the relationship between anion permeation and gating, two processes typically viewed as independent, in TMEM16B expressed in HEK 293T cells. The permeability ratio sequence determined by substituting Cl− with other anions (PX/PCl) was SCN− > I− > NO3− > Br− > Cl− > F− > gluconate. When external Cl− was substituted with other anions, TMEM16B activation and deactivation kinetics at 0.5 µM Ca2+ were modified according to the sequence of permeability ratios, with anions more permeant than Cl− slowing both activation and deactivation and anions less permeant than Cl− accelerating them. Moreover, replacement of external Cl− with gluconate, or sucrose, shifted the voltage dependence of steady-state activation (G-V relation) to more positive potentials, whereas substitution of extracellular or intracellular Cl− with SCN− shifted G-V to more negative potentials. Dose–response relationships for Ca2+ in the presence of different extracellular anions indicated that the apparent affinity for Ca2+ at +100 mV increased with increasing permeability ratio. The apparent affinity for Ca2+ in the presence of intracellular SCN− also increased compared with that in Cl−. Our results provide the first evidence that TMEM16B gating is modulated by permeant anions and provide the basis for future studies aimed at identifying the molecular determinants of TMEM16B ion selectivity and gating.
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Shimizu, Takahiro, Takahiro Iehara, Kaori Sato, Takuto Fujii, Hideki Sakai, and Yasunobu Okada. "TMEM16F is a component of a Ca2+-activated Cl− channel but not a volume-sensitive outwardly rectifying Cl− channel." American Journal of Physiology-Cell Physiology 304, no. 8 (April 15, 2013): C748—C759. http://dx.doi.org/10.1152/ajpcell.00228.2012.

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TMEM16 (transmembrane protein 16) proteins, which possess eight putative transmembrane domains with intracellular NH2- and COOH-terminal tails, are thought to comprise a Cl− channel family. The function of TMEM16F, a member of the TMEM16 family, has been greatly controversial. In the present study, we performed whole cell patch-clamp recordings to investigate the function of human TMEM16F. In TMEM16F-transfected HEK293T cells but not TMEM16K- and mock-transfected cells, activation of membrane currents with strong outward rectification was found to be induced by application of a Ca2+ ionophore, ionomycin, or by an increase in the intracellular free Ca2+ concentration. The free Ca2+ concentration for half-maximal activation of TMEM16F currents was 9.6 μM, which is distinctly higher than that for TMEM16A/B currents. The outwardly rectifying current-voltage relationship for TMEM16F currents was not changed by an increase in the intracellular Ca2+ level, in contrast to TMEM16A/B currents. The Ca2+-activated TMEM16F currents were anion selective, because replacing Cl− with aspartate− in the bathing solution without changing cation concentrations caused a positive shift of the reversal potential. The anion selectivity sequence of the TMEM16F channel was I− > Br− > Cl− > F− > aspartate−. Niflumic acid, a Ca2+-activated Cl− channel blocker, inhibited the TMEM16F-dependent Cl− currents. Neither overexpression nor knockdown of TMEM16F affected volume-sensitive outwardly rectifying Cl− channel (VSOR) currents activated by osmotic swelling or apoptotic stimulation. These results demonstrate that human TMEM16F is an essential component of a Ca2+-activated Cl− channel with a Ca2+ sensitivity that is distinct from that of TMEM16A/B and that it is not related to VSOR activity.
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Cenedese, Valentina, Giulia Betto, Fulvio Celsi, O. Lijo Cherian, Simone Pifferi, and Anna Menini. "The voltage dependence of the TMEM16B/anoctamin2 calcium-activated chloride channel is modified by mutations in the first putative intracellular loop." Journal of General Physiology 139, no. 4 (March 12, 2012): 285–94. http://dx.doi.org/10.1085/jgp.201110764.

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Ca2+-activated Cl− channels (CaCCs) are involved in several physiological processes. Recently, TMEM16A/anoctamin1 and TMEM16B/anoctamin2 have been shown to function as CaCCs, but very little information is available on the structure–function relations of these channels. TMEM16B is expressed in the cilia of olfactory sensory neurons, in microvilli of vomeronasal sensory neurons, and in the synaptic terminals of retinal photoreceptors. Here, we have performed the first site-directed mutagenesis study on TMEM16B to understand the molecular mechanisms of voltage and Ca2+ dependence. We have mutated amino acids in the first putative intracellular loop and measured the properties of the wild-type and mutant TMEM16B channels expressed in HEK 293T cells using the whole cell voltage-clamp technique in the presence of various intracellular Ca2+ concentrations. We mutated E367 into glutamine or deleted the five consecutive glutamates 386EEEEE390 and 399EYE401. The EYE deletion did not significantly modify the apparent Ca2+ dependence nor the voltage dependence of channel activation. E367Q and deletion of the five glutamates did not greatly affect the apparent Ca2+ affinity but modified the voltage dependence, shifting the conductance–voltage relations toward more positive voltages. These findings indicate that glutamates E367 and 386EEEEE390 in the first intracellular putative loop play an important role in the voltage dependence of TMEM16B, thus providing an initial structure–function study for this channel.
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10

Davis, Alison J., Abigail S. Forrest, Thomas A. Jepps, Maria L. Valencik, Michael Wiwchar, Cherie A. Singer, William R. Sones, Iain A. Greenwood, and Normand Leblanc. "Expression profile and protein translation of TMEM16A in murine smooth muscle." American Journal of Physiology-Cell Physiology 299, no. 5 (November 2010): C948—C959. http://dx.doi.org/10.1152/ajpcell.00018.2010.

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Recently, overexpression of the genes TMEM16A and TMEM16B has been shown to produce currents qualitatively similar to native Ca2+-activated Cl− currents ( IClCa) in vascular smooth muscle. However, there is no information about this new gene family in vascular smooth muscle, where Cl− channels are a major depolarizing mechanism. Qualitatively similar Cl− currents were evoked by a pipette solution containing 500 nM Ca2+ in smooth muscle cells isolated from BALB/c mouse portal vein, thoracic aorta, and carotid artery. Quantitative PCR using SYBR Green chemistry and primers specific for transmembrane protein (TMEM) 16A or the closely related TMEM16B showed TMEM16A expression as follows: portal vein > thoracic aorta > carotid artery > brain. In addition, several alternatively spliced variant transcripts of TMEM16A were detected. In contrast, TMEM16B expression was very low in smooth muscle. Western blot analysis with different antibodies directed against TMEM16A revealed a number of products with a consistent band at ∼120 kDa, except portal vein, where an 80-kDa band predominated. TMEM16A protein was identified in the smooth muscle layers of 4-μm-thick slices of portal vein, thoracic aorta, and carotid artery. In isolated myocytes, fluorescence specific to a TMEM16A antibody was detected diffusely throughout the cytoplasm, as well as near the membrane. The same antibody used in Western blot analysis of lysates from vascular tissues also recognized an ∼147-kDa mouse TMEM16A-green fluorescent protein (GFP) fusion protein expressed in HEK 293 cells, which correlated to a similar band detected by a GFP antibody. Patch-clamp experiments revealed that IClCa generated by transfection of TMEM16A-GFP in HEK 293 cells displayed remarkable similarities to IClCa recorded in vascular myocytes, including slow kinetics, steep outward rectification, and a response similar to the pharmacological agent niflumic acid. This study shows that TMEM16A expression is robust in murine vascular smooth muscle cells, consolidating the view that this gene is a viable candidate for the native Ca2+-activated Cl− channel in this cell type.
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Dissertations / Theses on the topic "TMEM16B"

1

Suzuki, Takayuki. "Functional Swapping between Transmembrane Proteins TMEM16A and TMEM16F." Kyoto University, 2014. http://hdl.handle.net/2433/188693.

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Ishihara, Kenji. "Role of Ca2+ in the Stability and Function of TMEM16F and 16K." Kyoto University, 2016. http://hdl.handle.net/2433/217141.

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Lancien, Mélanie. "Etude du rôle des gènes homologues Tmem176a et Tmem176b dans le système immunitaire : immunité de type 17 et biologie des cellules dendritiques." Thesis, Nantes, 2019. http://www.theses.fr/2019NANT1011.

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Notre système immunitaire assure la protection et régule l'homéostasie de l'organisme. Pour cela, il se compose d'une réponse immune innée et d'une réponse adaptative. Notre équipe a identifié TMEM176A et TMEM176B, deux protéines transmembranaires de structure et de fonction identiques. Ces protéines sont des canaux ioniques intracellulaires qui ont la particularité d'être fortement exprimés à la fois dans les cellules RORyt+ et dans les cellules dendritiques. La génération d'une souris déficiente pour ces deux gènes nous a permis d'étudier leur rôle. Nous avons mis en évidence que l'absence de Tmem176a et b n'impacte pas la génération des cellules RORyt+, ni leur capacité à sécréter des cytokines. L'étude de deux modèles de colite nous a permis de confirmer que Tmem176a et b ne semblent pas avoir un rôle majeur dans ces cellules. A l'inverse l'étude épigénétique des cellules dendritiques déficientes a mis en évidence une dérégulation de la voie de présentation du CMH de classe If. Nous avons mis en évidence une diminution de leur prolifération des lymphocytes T CD4*. En utilisant une technique de microscopie innovante, nous avons observé une localisation préférentielle de TMEM176A et B dans la voie endolysosomale et notamment dans le compartiment MIIC impliqué dans la présentation des antigènes par la voie du CMH de classe 11. Ainsi ces résultats suggèrent que dans les cellules dendritiques, Tmem176a et b participent à la présentation des antigènes et à l'activation des lymphocytes T CD4* naïfs
Our immune system provides protection and regulates the homeostasis of the organism. For this, it consists of an innate immune response and an adaptive response. Our team has identified TMEM176A and TMEM176B. These proteins are intracellular ion channels that are particularly expressed both in RORyt+ cells and in dendritic cells. The generation of a deficient mouse for these two genes allowed us to study their role. We have demonstrated that the absence of Tmem 176a and b does not affect the generation of RORyt+ cells, neither their ability to secrete cytokines. The study of two models of colitis allowed us to confirm that Tmem176a and b seem to be dispensable in these cells. However, the epigenetic study of deficient dendritic cells put in evidence a deregulation of the MHC class li presentation pathway. We have detected a decrease of the proliferation of CD4+ T. Using an innovative microscopy technique, we have observed a preferential localization of TMEM176A and B in the endo-lysosomal pathway and in particular in the MIIC compartment involved in the presentation of antigens by the MHC class li pathway. Thus, these results suggest that in dendritic cells, Tmem 176a and b are involved in the presentation of antigens and activation of naïve CD4* T cells
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Ubby, Ifeoma. "Regulation of TMEM16A altrenatice splincing." Doctoral thesis, Scuola Normale Superiore, 2012. http://hdl.handle.net/11384/85994.

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TMEM16A/Anoctamin1 is a novel calcium-­‐activated chloride channel involved in neuronal and cardiac excitation, vascular tone, pain perception and olfactory and sensory signal transduction and GI tract motility. It is also associated to diverse type of cancer including breast cancer malignancy. Alternative splicing (AS) of exons 6b, 13 and 15 generates functionally distinct TMEM16A isoforms with different electrophysiological properties. To study their splicing regulation, I performed in minigene system a systematic analysis of exonic and intronic regulatory elements followed by co-­‐transfection of a panel of splicing regulatory factors. Analysis of TMEM16A pre-­‐mRNA splicing supports a model in which each exon is regulated by different cis-­‐ and trans-­‐acting elements. Exon 6b inclusion is regulated primarily by SRSF9 and TRA2B, through a unique GAA-­‐rich ESE element. Exon 15 is enhanced only by TIA1 and FOX1 and this effect is mediated by downstream intronic sequences. On the other hand, the small exon 13, included in most human tissues, was mainly skipped in the minigene and only FOX1 and U2AF65 enhanced its inclusion. To understand if there is any preferential association between three AS exons, I have evaluated TMEM16A isoforms using a long range RT-­‐PCR assay that amplifies transcripts across the AS events. Coordination between distant alternative spliced exons in the same gene has been suggested to be an important mechanism to regulate gene expression but very few genes have been studied in detail. I observed that the selection of exons 6b and 15 is preferentially coordinated in several human normal tissues: mature transcripts that predominantly include exon 6b tend to exclude exon 15. Unexpectedly, this coordination was not conserved in mouse tissues. This was mainly due to the fact that exon 15 was largely and predominantly excluded in the mouse, a fact that suggest a peculiar evolutionary conservation of AS in this gene. To explore if changes in splicing coordination of the two major AS events are associated to cancer development I evaluated normal mammalian tissue and corresponding breast tumors of the same cohort, obtained from surgical excision (n=18). The distribution of individual AS events did not change between normal and tumor tissues. However, the TMEM16A splicing coordination increased significantly in tumors. Indeed, the splicing coordination was present in 50% of normal mammalian breast tissues and in 84% in tumors. In conclusion this study identifies several cis-­‐acting elements and trans-­‐acting factors involved in the regulation of TMEM16A Alternative Splicing and provides evidence of its intragenic splicing coordination. The increase of TMEM16A splicing coordination observed in breast tumor, might represent a common event in genes with multiple AS events.
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Adomaviciene, Aiste. "TMEM16A channels : molecular physiology and pharmacological regulation." Thesis, University of Manchester, 2012. https://www.research.manchester.ac.uk/portal/en/theses/tmem16a-channels-molecular-physiology-and-pharmacological-regulation(681d1c72-3207-41f5-bd78-c6af0a6ccdf3).html.

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Calcium-activated chloride channels (CaCCs) are a class of the ligand-gated channels involved in numerous cellular functions. In vascular smooth muscle, these ion channels couple agonist-induced calcium-release from the sarcoplasmic reticulum to membrane depolarisation and vasoconstriction. For this reason, CaCCs have been suggested as a potential molecular target to treat a range of vascular disorders. These ion channels, however, have not been yet explored as a drug target because their molecular identity has been elusive and their pharmacology has been restricted to compounds with low potency and poor specificity. The general aims of this work of thesis are: i) to define the molecular identity of CaCCs in vascular smooth muscle, ii) to investigate how the structural features of the identified channel relate to its functional properties and iii) to examine how drug binding modulates CaCC activity. The main findings are the following:1) By using RNA interference technology and patch-clamp analysis, the Tmem16A gene was found to encode for CaCCs in pulmonary artery smooth muscle. Furthermore, Tmem16A appeared to be expressed in other vascular smooth muscles suggesting that this ion channel may represent CaCCs in various vascular beds.2) To understand the physiology and pharmacology of TMEM16A channels it is of a fundamental importance to elucidate the molecular mechanisms by which channel gating and conductance are achieved. TMEM16A comprises eight putative transmembrane domains (TMs) with TM5 and TM6 flanking a putative re-entrant loop, which resembles the pore of other ion channels. Using a chimeric approach the role of this region was investigated. The re-entrant loop of TMEM16A was found to mediate a range of functional roles: it controlled the response of the channel to intracellular calcium, the permeation of anions and the expression of channels on the plasma membrane. Specifically, a non-canonical trafficking motif was identified within in a 38 amino acid region within the re-entrant loop.3) Drugs that modulate the function of TMEM16A channels are currently limited. The generic chloride channel blocker anthracene-9-carboxylic acid (A9C) was found to produce a bimodal effect on TMEM16A currents: low concentrations of A9C activated the channels, while doses higher than ~300 µM produced current inhibition. These two effects were mediated via A9C binding to two separate sites. Binding of A9C into the pore resulted in channel inhibition, while A9C binding to an extracellular site increased the open probability of the channel. To conclude, this work of thesis has revealed the molecular identity of CaCCs in vascular smooth muscle and elucidated the functional roles of the re-entrant loop of the TMEM16A channel protein. The identification of the activating and inhibiting A9C binding sites may help the development of selective blockers and activators of TMEM16A channels.
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Meadows, Benjamin Roland Alexander. "Unravelling the cell adhesion defect in Meckel-Gruber syndrome." Thesis, University of Exeter, 2016. http://hdl.handle.net/10871/29380.

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Meckel-Gruber syndrome (MKS) is a universally lethal heritable human disease characterised by CNS malformations, cystic kidney, polydactyly, and liver fibrosis. MKS is classed as one of the ciliopathies due to its association with dysfunctional primary cilia, signalling organelles found on most cells in the human body. Some of the symptoms of MKS can be explained as a consequence of disrupted developmental signalling through the primary cilium, other defects are harder to explain, and evidence now exists for non-ciliary influences on ciliopathies. The nature of these influences, and the implications they may have for our understanding of ciliary function and the aetiology of MKS, remain unclear. In this thesis, defects in cell-extracellular matrix (ECM) interaction in MKS are investigated to determine whether MKS proteins have a role in this process, and if so, whether this role may be involved in MKS pathology. A combination of transcriptomic, proteomic, and cell imaging approaches are used to demonstrate that MKS patient cells produce a defective extracellular matrix, and that the MKS protein TMEM67 is present at the cell surface at sites of cell-ECM interaction. It is shown that the full-length TMEM67 protein is required for correct ECM morphology, and it is further shown that the abnormal extracellular matrix morphology in MKS cells underlies other defects, including failure to build cilia and alterations to the actin cytoskeleton. This represents the first set of causal relationships identified between the cellular defects in this complex disease. It is further shown that treatment with developmental signalling pathway antagonists can rescue these defects, potentially revealing a new avenue of therapeutic intervention for MKS. Finally, possible upstream defects are investigated that might underlie the ECM defect, including alterations to cell spreading behaviour and cell deformation resistance.
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Brookfield, Rebecca. "The pharmacology and cardiovascular function of TMEM16A channels." Thesis, University of Manchester, 2015. https://www.research.manchester.ac.uk/portal/en/theses/the-pharmacology-and-cardiovascular-function-of-tmem16a-channels(bdc16466-cecd-4343-9d40-b20bc647d70f).html.

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Calcium-activated chloride channels (CaCCs) are ubiquitously expressed in a plethora of cell types and, consequently, are involved in numerous cellular processes as diverse as epithelial secretion, regulation of cardiac excitability and smooth muscle contraction. Current pharmacology of CaCCs is limited to compounds with low potency and poor selectivity. The lack of knowledge surrounding the molecular identity of the CaCC has greatly hindered the development of more specific drugs and has impaired our understanding of the channel physiology and biophysics. The recent discovery that the TMEM16A gene codes for CaCCs has offered hope for new developments in these areas. CaCCs have been suggested as possible targets to treat a variety of conditions including asthma as well as pulmonary and systemic hypertension. Due to the ubiquitous expression of CaCCs and the ability of the channel to interact with a number of pharmacological compounds with diverse chemical structures however, it was hypothesised that TMEM16A could be a possible source for off-target drug effects and may represent a concern for safety pharmacology. The principal aim of this thesis was to assess the functional significance of TMEM16A in the cardiovascular system, as this is one of the major systems of concern for safety pharmacology and accounts for the largest number of post-market drug withdrawals. The main findings of this study can be summarised as follows: 1) RT-PCR analysis revealed a ubiquitous expression of TMEM16A in tissues of the rat and human cardiovascular systems, including systemic and pulmonary arteries as well as cardiac tissue. Analysis also revealed the presence of multiple TMEM16A splice variants in all rat tissues examined, in addition to a number of other TMEM16x family members. 2) Myography experiments using the “classical” CaCC blocker niflumic acid and newly identified TMEM16A blockers confirmed a functional role for TMEM16A in phenylephrine-induced vascular smooth muscle contraction. 3) The suitability of currently available Cl- channel blockers for use as pharmacological tools for TMEM16A research was assessed using conventional whole-cell patch clamp and high-throughput electrophysiology techniques to respectively compare their potencies and selectivity over other cardiovascular ion channels. Of the compounds tested, DIDS and T16Ainh-A01 appeared the most suitable blockers; however all compounds had a degree of non-selectivity, raising concerns for their use in functional studies. In conclusion, these findings provide evidence for the ubiquitous expression and functional significance of TMEM16A within the cardiovascular system and support the hypothesis that TMEM16A is a concern for safety pharmacology and should be included into future pre-clinical safety assays. The inadequacy of current inhibitors however highlights the urgency for the development of novel potent and selective channel modulators for future TMEM16A research.
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SCUDIERI, PAOLO. "Intermolecular Interactions in the TMEM16A Dimer Controlling Channel Activity." Doctoral thesis, Università degli studi di Genova, 2018. http://hdl.handle.net/11567/929402.

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TMEM16A e TMEM16B sono proteine di membrana con funzione di canali del cloruro attivati da calcio. Attraverso la generazione di canali chimerici, e in particolare, sostituendo la regione carbossi-terminale di TMEM16A con la regione equivalente di TMEM16B, sono stati ottenuti dei canali dotati di una maggiore attività. Il progressivo accorciamento della regione chimerica ha permesso di restringere il “dominio attivante” a una corta sequenza di 14 aminoacidi localizzata vicino all’ultimo dominio transmembrana e ha generato proteine-canale TMEM16A dotate di un’attività molto alta anche a concentrazioni basse di calcio intracellulare. Per chiarire il meccanismo molecolare alla base di questo effetto, sono stati eseguiti esperimenti basati sulla generazione di doppie chimere, Forster resonance Energy transfer e cross-linking intermolecolare. Inoltre, è stato generato un modello tridimensionale teorico di TMEM16A basato sulla struttura di una proteina TMEM16 del fungo Nectria haematococca. I risultati ottenuti indicano che l’aumentata attività nei canali chimerici è causata da un’alterazione dell’interazione tra il carbossi-terminale e la prima ansa intracellulare di TMEM16A. L’identificazione di piccole molecole farmacologiche in grado di mimare questa perturbazione potrebbe rappresentare la base di un approccio farmacologico volto a stimolare il trasporto ionico TMEM16A-dipendente. L’attivazione farmacologica di TMEM16A potrebbe essere utile per stimolare la secrezione epiteliale nelle vie aeree, un effetto potenzialmente benefico in patologie quali la fibrosi cistica e altre malattie ostruttive croniche dell’apparato respiratorio
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Gyobu, Sayuri. "A role of TMEM16E carrying a scrambling domain in sperm motility." Kyoto University, 2016. http://hdl.handle.net/2433/215460.

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論文1ページ目の下部に著作権を表示すること。（© 2016, American Society for Microbiology. ）
Kyoto University (京都大学)
0048
新制・課程博士
博士(医科学)
甲第19634号
医科博第72号
新制||医科||5(附属図書館)
32670
京都大学大学院医学研究科医科学専攻
(主査)教授 近藤 玄, 教授 篠原 隆司, 教授 秋山 芳展
学位規則第4条第1項該当
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Schwenk, Benjamin. "The FTLD risk factor TMEM106B controls lysosomal trafficking and dendrite outgrowth." Diss., Ludwig-Maximilians-Universität München, 2015. http://nbn-resolving.de/urn:nbn:de:bvb:19-181956.

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Frontotemporal dementia is the second most common neurodegenerative disease in people younger than 65 years. Patients suffer from behavioral changes, language deficits and speech impairment. Unfortunately, there is no effective treatment available at the moment. Cytoplasmic inclusions of the DNA/RNA-binding protein TDP-43 are the pathological hallmark in the majority of FTLD cases, which are accordingly classified as FTLD-TDP. Mutations in GRN, the gene coding for the trophic factor progranulin, are responsible for the majority of familiar FTLD-TDP cases. The first genome-wide association study performed for FTLD-TDP led to the identification of risk variants in the so far uncharacterized gene TMEM106B. Initial cell culture studies revealed intracellular localization of TMEM106B protein in lysosomes but its neuronal function remained elusive. Based on these initial findings, I investigated the physiological function of TMEM106B in primary rat neurons during this thesis. I demonstrated that endogenous TMEM106B is localized to late endosomes and lysosomes in primary neurons, too. Notably, knockdown of the protein does neither impair general neuronal viability nor the protein level of FTLD associated proteins, such as GRN or TDP-43. However, shRNA-mediated knockdown of TMEM106B led to a pronounced withering of the dendritic arbor in developing and mature neurons. Moreover, the strong impairment of dendrite outgrowth and maintenance was accompanied by morphological changes and loss of dendritic spines. To gain mechanistic insight into the loss-of-function phenotypes, I searched for coimmunoprecipitating proteins by LC-MS/MS. I specifically identified the microtubule-binding protein MAP6 as interaction partner and was able to validate binding. Strikingly, overexpression of MAP6 in primary neurons phenocopied the TMEM106B knockdown effect on dendrites and loss of MAP6 restored dendritic branching in TMEM106B knockdown neurons, indicating functional interaction of the two proteins. The link between a lysosomal and a microtubule-binding protein made me study the microtubule dependent transport of dendritic lysosomes. Remarkably, live cell imaging studies revealed enhanced movement of dendritic lysosomes towards the soma in neurons devoid of TMEM106B. Again, MAP6 overexpression phenocopied and MAP6 knockdown rescued this effect, strengthening the functional link. The MAP6-independent rescue of dendrite outgrowth by enhancing anterograde lysosomal movement provided additional evidence that dendritic arborization is directly controlled by lysosomal trafficking. From these findings I suggest the following model: TMEM106B and MAP6 together act as a molecular brake for the retrograde transport of dendritic lysosomes. Knockdown of TMEM106B and (the presumably dominant negative) overexpression of MAP6 release this brake and enhance the retrograde movement of lysosomes. Subsequently, the higher protein turnover and the net loss of membranes in distal dendrites may cause the defect in dendrite outgrowth. The findings of this study suggest that lysosomal misrouting in TMEM106B risk allele carrier might further aggravate lysosomal dysfunction seen in patients harboring GRN mutations and thereby contribute to disease progression. Taken together, I discovered the first neuronal function for the FTLD-TDP risk factor TMEM106B: This lysosomal protein acts together with its novel, microtubule-associated binding partner MAP6 as molecular brake for the dendritic transport of lysosomes and thereby controls dendrite growth and maintenance.
Frontotemporale Demenz ist die zweithäufigste Form neurodegenerativer Erkrankungen bei Menschen unter 65 Jahren. Patienten leiden an Verhaltensauffälligkeiten und Sprach- sowie Artikulationsstörungen. Leider steht zurzeit keine wirksame medikamentöse Therapie zur Verfügung. Das pathologische Hauptmerkmal der meisten FTLD-Fälle sind zytoplasmatische Einschlüsse des DNA/RNA-bindenden Proteins TDP-43. Diese Fälle werden entsprechend als FTLD-TDP klassifiziert. Für einen Großteil der familiären FTLD-TDP Fälle sind Mutationen in GRN, dem für den Wachstumsfaktor Progranulin kodierenden Gen, verantwortlich. Die erste für FTLD-TDP durchgeführte genomweite Assoziationsstudie führte zur Entdeckung von genetischen Varianten im bis dato uncharakterisierten Gen TMEM106B. Diese Varianten sind mit einem erhöten Risiko an FTLD zu erkranken assoziiert. Initiale Studien in Zellkultur zeigten eine Lokalisierung des TMEM106B Proteins in Lysosomen, die Frage nach der neuronale Funktion des Proteins blieb allerdings bisher unbeantwortet. Auf diesen ersten Ergebnissen aufbauend untersuchte ich während meiner Dissertation die physiologische Funktion von TMEM106B in primären Ratten-neuronen. Ich konnte zeigen, dass endogenes TMEM106B auch in primären Neuronen in späten Endsosomen und Lysosomen lokalisiert ist. Beachtenswerterweise verminderte die Herunterregulierung (shRNA-vermittelter Gen-Knockdown) des Proteins weder das generelle Überleben der Neuronen noch die Level von anderen FTLD-assoziierten Proteinen, wie GRN oder TDP-43. Die Herunterregulierung von TMEM106B führte jedoch zu einem ausgeprägten Verlust von Dendriten in sich entwickelnden und ausgereiften Neuronen. Des Weiteren war die starke Beeinträchtigung dendritischen Wachstums und Aufrechterhaltung von einer morphologischen Veränderung und dem Verlust der Dornfortsätze begleitet. Um den Mechanismus dieser Phänotypen zu erklären, suchte ich nach TMEM106B coimmunopräzipitierenden Proteinen mittels Massenspektrometrie. Ich konnte das Mikrotubuli bindende Protein MAP6 als spezifischen Bindungspartner identifizieren und die Interaktion beider Proteine validieren. Hervorzuheben ist, dass die Überexpression von MAP6 in primären Neuronen den Effekt der Herunterregulation von TMEM106B auf die Dendriten kopierte und die Herunterregulation von MAP6 die dendritischen Verästelungen in TMEM106B depletierten Neuronen sogar wiederherstellen konnte. Diese Ergebnisse legen eine funktionelle Interaktion beider Proteine nahe. Die Verbindung zwischen einem lysosomalen und einem an die Mikrotubuli bindenden Protein brachte mich dazu, den Mikrotubuli abhängigen Transport von dendritischen Lysosomen zu untersuchen. Bemerkenswerterweise zeigten mittels Lebendzellmikroskopie erzeugte Aufnahmen eine erhöhte Bewegung dendritischer Lysosomen Richtung Zellsoma in TMEM106B depletierten Neuronen. Auch in diesem Kontext konnte die Überexpression von MAP6 den Effekt kopieren und die Herunterregulation von MAP6 den Effekt aufheben und somit die These einer funktionellen Interaktion festigen. Die MAP6 unabhängige Wiederherstellung des dendritischen Wachstums durch die Erhöhung des lysosomalen Transports in anterograder Richtung lieferte einen zusätzlichen Beweis dafür, dass das dendritische Wachstum direkt von lysosomalem Transport abhängt. Ausgehend von diesen Ergebnissen schlage ich folgendes Modell vor: TMEM106B und MAP6 wirken zusammen als molekulare Bremse für den retrograden Transport dendritischer Lysosomen. Die Herunterregulation von TMEM106B und die (wahrscheinlich dominant negative wirkende) Überexpression von MAP6 lösen diese Bremse und verstärken die retrograde Bewegung von Lysosomen. Daraufhin könnten der gestiegene Proteinumsatz und der Verlust von Plasmamembranbestandteilen zu einem Fehler im dendritischen Wachstum führen. Die Ergebnisse dieser Arbeit legen nahe, dass fehlerhafter, lysosomaler Transport in TMEM106B Risikoallelträgern zu einer Verstärkung der lysosomalen Fehlfunktion in Patienten mit GRN Mutation führt und dabei zur Krankheitsentwicklung beiträgt. Zusammengefasst habe ich die erste neuronale Funktion für den FTLD-TDP Risikofaktor TMEM106B entdeckt: Dieses lysosomale Protein wirkt zusammen mit seinem neuentdeckten, Mikrotubuli assoziierten Bindungspartner MAP6 als molekulare Bremse für den dendritischen Transport von Lysosomen und kontrolliert dadurch Wachstum und Aufrechterhaltung von Dendriten.
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Book chapters on the topic "TMEM16B"

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Scudieri, Paolo, and Luis J. V. Galietta. "TMEM16 Proteins (Anoctamins) in Epithelia." In Ion Channels and Transporters of Epithelia in Health and Disease, 553–67. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-3366-2_17.

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Scudieri, Paolo, and Luis J. V. Galietta. "TMEM16 Proteins (Anoctamins) in Epithelia." In Studies of Epithelial Transporters and Ion Channels, 671–96. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-55454-5_17.

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Schulte Althoff, S., M. Grüneberg, J. Reunert, J. H. Park, S. Rust, C. Mühlhausen, Y. Wada, R. Santer, and T. Marquardt. "TMEM165 Deficiency: Postnatal Changes in Glycosylation." In JIMD Reports, 21–29. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/8904_2015_455.

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Le, Son C., and Huanghe Yang. "Structure–Function of TMEM16 Ion Channels and Lipid Scramblases." In Ion Channels in Biophysics and Physiology, 87–109. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-4254-8_6.

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Brunner, Janine Denise, and Stephan Schenck. "Preparation of Proteoliposomes with Purified TMEM16 Protein for Accurate Measures of Lipid Scramblase Activity." In Methods in Molecular Biology, 181–99. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9136-5_14.

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Mizuta, Ken, Masahide Sakabe, Satoshi Somekawa, Yoshihiko Saito, and Osamu Nakagawa. "TMEM100: A Novel Intracellular Transmembrane Protein Essential for Vascular Development and Cardiac Morphogenesis." In Etiology and Morphogenesis of Congenital Heart Disease, 169–70. Tokyo: Springer Japan, 2016. http://dx.doi.org/10.1007/978-4-431-54628-3_21.

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Zeevaert, R., F. de Zegher, L. Sturiale, D. Garozzo, M. Smet, M. Moens, G. Matthijs, and J. Jaeken. "Bone Dysplasia as a Key Feature in Three Patients with a Novel Congenital Disorder of Glycosylation (CDG) Type II Due to a Deep Intronic Splice Mutation in TMEM165." In JIMD Reports, 145–52. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/8904_2012_172.

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Yang, H., and L. Y. Jan. "TMEM16 Membrane Proteins in Health and Disease." In Ion Channels in Health and Disease, 165–97. Elsevier, 2016. http://dx.doi.org/10.1016/b978-0-12-802002-9.00007-8.

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Pusch, Michael, and Giovanni Zifarelli. "Thermal Sensitivity of CLC and TMEM16 Chloride Channels and Transporters." In Current Topics in Membranes, 213–31. Elsevier, 2014. http://dx.doi.org/10.1016/b978-0-12-800181-3.00008-7.

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Nguyen, Dung Manh, and Tsung-Yu Chen. "Structure and Function of Calcium-Activated Chloride Channels and Phospholipid Scramblases in the TMEM16 Family." In Handbook of Experimental Pharmacology. Berlin, Heidelberg: Springer Berlin Heidelberg, 2022. http://dx.doi.org/10.1007/164_2022_595.

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Conference papers on the topic "TMEM16B"

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Brett, T., M. Sala-Rabanal, K. Berry, D. F. Steinberg, and C. G. Nichols. "Modulation of TMEM16B Channel Activity by the Calcium-Activated Chloride Channel Regulator 4 Suggests a Common Function for CLCA Proteins in Modifying TMEM16 Channels." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a2127.

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Koyama, Yoshinobu, Soichiro Fuke, Yoshiharu Sato, Akemi Senoh, and Toshie Higuchi. "AB0208 UP-REGULATION OF TMEM176A AND TMEM176B IN PERIPHERAL BLOOD CELLS, A POSSIBLE BIOMARKER FOR THE DEVELOPMENT OF EARLY PULMONARY VASCULAR DISEASE IN SYSTEMIC SCLEROSIS." In Annual European Congress of Rheumatology, EULAR 2019, Madrid, 12–15 June 2019. BMJ Publishing Group Ltd and European League Against Rheumatism, 2019. http://dx.doi.org/10.1136/annrheumdis-2019-eular.6628.

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Kondo, M., K. Hara, M. Tsuji, A. Kurokawa, K. Takeyama, and E. Tagaya. "TMEM16A Inhibitors Decrease TMEM16A Expression and Goblet Cell Metaplasia in IL-13-Treated Guinea Pig Trachea In Vivo." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a2186.

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Cao, G., B. Deeney, E. Chung, J. Jude, P. Saad, N. Hartwick, and R. A. Panettieri. "TMEM16A Modulates TGFβ1-Induced MLC2 Phosphorylation in Human Airway Smooth Muscle." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a1255.

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Warner, Amanda N., Samrat T. Kundu, Rakhee Bajaj, Bertha Leticia Rodriguez, and Don Gibbons. "Lysosomal transmembrane protein TMEM106B alters TFEB signaling and the tumor immune microenvironment." In Leading Edge of Cancer Research Symposium. The University of Texas at MD Anderson Cancer Center, 2022. http://dx.doi.org/10.52519/00093.

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Danielsson, J., A. Kuforiji, Y. Zhang, and C. W. Emala. "TMEM16A Agonism Contracts Airway Smooth Muscle in In Vivo and Ex Vivo Models." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a2839.

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Danielsson, J., G. T. Yocum, D. B. Xu, and C. W. Emala. "TMEM16A siRNA Knockdown Increases Expression of PPARG Coactivator 1 Alpha in Airway Smooth Muscle." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a1250.

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Wu, A. "TMEM16A Antagonism Prevents β-Adrenoceptor Desensitization in Ex-Vivo Human Airway Smooth Muscle Tissue." In American Thoracic Society 2022 International Conference, May 13-18, 2022 - San Francisco, CA. American Thoracic Society, 2022. http://dx.doi.org/10.1164/ajrccm-conference.2022.205.1_meetingabstracts.a3462.

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Bassiouni, M., K. Stölzel, H. Olze, and A. Szczepek. "Expression des Mikrogliamarkers TMEM119 in der postnatalen und adulten Cochlea." In Abstract- und Posterband – 90. Jahresversammlung der Deutschen Gesellschaft für HNO-Heilkunde, Kopf- und Hals-Chirurgie e.V., Bonn – Digitalisierung in der HNO-Heilkunde. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1686116.

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Wu, A., A. Kuforiji, C. W. Emala, and J. Danielsson. "The TMEM16A Antagonist Benzbromarone Decreases β2-Adrenergic Receptor Desensitization in Human Airway Smooth Muscle In Vitro." In American Thoracic Society 2021 International Conference, May 14-19, 2021 - San Diego, CA. American Thoracic Society, 2021. http://dx.doi.org/10.1164/ajrccm-conference.2021.203.1_meetingabstracts.a4502.

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