Correction to “Characterization of human α4β2-nicotinic acetylcholine receptors stably and heterologously expressed in native nicotinic receptor-null SH-EP1 human epithelial cells”: TABLE 3

2004 ◽  
Vol 66 (1) ◽  
pp. 197-197
Keyword(s):  
Epithelial Cells ◽  
Nicotinic Acetylcholine Receptors ◽  
Nicotinic Receptor ◽  
Acetylcholine Receptors ◽  
Nicotinic Acetylcholine ◽  
Human Epithelial Cells

scholarly journals Phosphocholine-Modified Lipooligosaccharides of Haemophilus influenzae Inhibit ATP-Induced IL-1β Release by Pulmonary Epithelial Cells

Molecules ◽  
2018 ◽  
Vol 23 (8) ◽  
pp. 1979 ◽  
Author(s):  
Katrin Richter ◽  
Christian Koch ◽  
Alexander Perniss ◽  
Philipp Wolf ◽  
Elke Schweda ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Haemophilus Influenzae ◽  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Opportunistic Pathogen ◽  
Mammalian Host ◽  
Nicotinic Acetylcholine ◽  
Pulmonary Epithelial Cells ◽  
Airway Infections ◽  
Human Lung Carcinoma

Phosphocholine-modified bacterial cell wall components are virulence factors enabling immune evasion and permanent colonization of the mammalian host, by mechanisms that are poorly understood. Recently, we demonstrated that free phosphocholine (PC) and PC-modified lipooligosaccharides (PC-LOS) from Haemophilus influenzae, an opportunistic pathogen of the upper and lower airways, function as unconventional nicotinic agonists and efficiently inhibit the ATP-induced release of monocytic IL-1β. We hypothesize that H. influenzae PC-LOS exert similar effects on pulmonary epithelial cells and on the complex lung tissue. The human lung carcinoma-derived epithelial cell lines A549 and Calu-3 were primed with lipopolysaccharide from Escherichia coli followed by stimulation with ATP in the presence or absence of PC or PC-LOS or LOS devoid of PC. The involvement of nicotinic acetylcholine receptors was tested using specific antagonists. We demonstrate that PC and PC-LOS efficiently inhibit ATP-mediated IL-1β release by A549 and Calu-3 cells via nicotinic acetylcholine receptors containing subunits α7, α9, and/or α10. Primed precision-cut lung slices behaved similarly. We conclude that H. influenzae hijacked an endogenous anti-inflammatory cholinergic control mechanism of the lung to evade innate immune responses of the host. These findings may pave the way towards a host-centered antibiotic treatment of chronic airway infections with H. influenzae.

Biophysical and pharmacological characterization of α6-containing nicotinic acetylcholine receptors expressed in HEK293 cells

2014 ◽  
Vol 1542 ◽  
pp. 1-11 ◽  
Author(s):  
Andreas H. Rasmussen ◽  
Dorte Strøbæk ◽  
Tino Dyhring ◽  
Marianne L. Jensen ◽  
Dan Peters ◽  
...  
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Hek293 Cells ◽  
Pharmacological Characterization ◽  
Nicotinic Acetylcholine

Molecular characterization of the specificity of interactions of various neurotoxins on two distinct nicotinic acetylcholine receptors

2000 ◽  
Vol 393 (1-3) ◽  
pp. 197-204 ◽  
Author(s):  
Denis Servent ◽  
Stéphanie Antil-Delbeke ◽  
Carole Gaillard ◽  
Pierre-Jean Corringer ◽  
Jean Pierre Changeux ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Nicotinic Acetylcholine

scholarly journals αM-Conotoxin MIIIJ Blocks Nicotinic Acetylcholine Receptors at Neuromuscular Junctions of Frog and Fish

Toxins ◽  
2020 ◽  
Vol 12 (3) ◽  
pp. 197
Author(s):  
Matthew J. Rybin ◽  
Henrik O’Brien ◽  
Iris Bea L. Ramiro ◽  
Layla Azam ◽  
J. Michael McIntosh ◽  
...  
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Neuromuscular Junctions ◽  
Functional Characterization ◽  
Cone Snail ◽  
Nicotinic Acetylcholine ◽  
New Class ◽  
Goldfish Carassius Auratus ◽  
Snake Neurotoxin

We report the discovery and functional characterization of αM-Conotoxin MIIIJ, a peptide from the venom of the fish-hunting cone snail Conus magus. Injections of αM-MIIIJ induced paralysis in goldfish (Carassius auratus) but not mice. Intracellular recording from skeletal muscles of fish (C. auratus) and frog (Xenopus laevis) revealed that αM-MIIIJ inhibited postsynaptic nicotinic acetylcholine receptors (nAChRs) with an IC50 of ~0.1 μM. With comparable potency, αM-MIIIJ reversibly blocked ACh-gated currents (IACh) of voltage-clamped X. laevis oocytes exogenously expressing nAChRs cloned from zebrafish (Danio rerio) muscle. αM-MIIIJ also protected against slowly-reversible block of IACh by α-bungarotoxin (α-BgTX, a snake neurotoxin) and α-conotoxin EI (α-EI, from Conus ermineus another fish hunter) that competitively block nAChRs at the ACh binding site. Furthermore, assessment by fluorescence microscopy showed that αM-MIIIJ inhibited the binding of fluorescently-tagged α-BgTX at neuromuscular junctions of X. laevis, C. auratus, and D. rerio. (Note, we observed that αM-MIIIJ can block adult mouse and human muscle nAChRs exogenously expressed in X. laevis oocytes, but with IC50s ~100-times higher than those of zebrafish nAChRs.) Taken together, these results indicate that αM-MIIIJ inhibits muscle nAChRs and furthermore apparently does so by interfering with the binding of ACh to its receptor. Comparative alignments with homologous sequences identified in other fish hunters revealed that αM-MIIIJ defines a new class of muscle nAChR inhibitors from cone snails.

Human and Rodent Bronchial Epithelial Cells Express Functional Nicotinic Acetylcholine Receptors

1998 ◽  
Vol 54 (5) ◽  
pp. 779-788 ◽  
Author(s):  
Arno D. J. Maus ◽  
Edna F. R. Pereira ◽  
Peter I. Karachunski ◽  
Robert M. Horton ◽  
Duraiswamy Navaneetham ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Bronchial Epithelial Cells ◽  
Nicotinic Acetylcholine ◽  
Bronchial Epithelial

Characterization of AN317, a novel selective agonist of α6β2-containing nicotinic acetylcholine receptors

2020 ◽  
Vol 174 ◽  
pp. 113786 ◽  
Author(s):  
Karin Sandager-Nielsen ◽  
Philip K. Ahring ◽  
Jessica Klein ◽  
Marloes van Hout ◽  
Siganya Thaneshwaran ◽  
...  
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Nicotinic Acetylcholine ◽  
Selective Agonist

Molecular cloning and characterization of a novel human variant of RIC-3, a putative chaperone of nicotinic acetylcholine receptors

2008 ◽  
Vol 28 (6) ◽  
pp. 299-306 ◽  
Author(s):  
Tamara Seredenina ◽  
Teresa Ferraro ◽  
Georg C. Terstappen ◽  
Andrea Caricasole ◽  
Renza Roncarati
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Coiled Coil ◽  
Surface Expression ◽  
Protein Product ◽  
Nicotinic Acetylcholine ◽  
Α7 Nachr ◽  
New Variant ◽  
Novel Variant

Recent reports demonstrate that the RIC-3 (resistant to inhibitors of cholinesterase-3) protein is important for the maturation of nAChRs (nicotinic acetylcholine receptors). In the present study RIC-3e, a novel variant of RIC-3, is described. This variant contains a deletion of exons 4 and 5 of RIC-3, resulting in a protein product lacking a conserved coiled-coil domain. Like RIC-3, the new variant is predominantly, but not exclusively, expressed in the brain. The analysis of expression of variant RIC-3 mRNA and of α7-nAChR mRNA in a set of human tissues shows a similar profile. The RIC-3e protein is functionally active and enables surface expression of mature α7-nAChRs in cell lines not otherwise permissive for the expression of this receptor.

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