Methfessel C

General

Full name : Methfessel Christoph

First name : Christoph

Mail : BAYER AG ZF-FP Biophysik GEB E41, D-51368 Leverkusen

Zip Code :

City :

Country : Germany

Email : christoph.methfessel.cm@bayer-ag.de

Phone : 49 21 4307876

Fax : 49 21 43 050698

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References (15)

Title : The novel alpha7 nicotinic acetylcholine receptor agonist N-[(3R)-1-azabicyclo[2.2.2]oct-3-yl]-7-[2-(methoxy)phenyl]-1-benzofuran-2-carboxa mide improves working and recognition memory in rodents - Boess_2007_J.Pharmacol.Exp.Ther_321_716
Author(s) : Boess FG , De Vry J , Erb C , Flessner T , Hendrix M , Luithle J , Methfessel C , Riedl B , Schnizler K , van der Staay FJ , Van Kampen M , Wiese WB , Koenig G
Ref : Journal of Pharmacology & Experimental Therapeutics , 321 :716 , 2007
Abstract : The relative contribution of alpha4beta2, alpha7 and other nicotinic acetylcholine receptor (nAChR) subtypes to the memory enhancing versus the addictive effects of nicotine is the subject of ongoing debate. In the present study, we characterized the pharmacological and behavioral properties of the alpha7 nAChR agonist N-[(3R)-1-azabicyclo[2.2.2]oct-3-yl]-7-[2-(methoxy)phenyl]-1-benzofuran-2-carboxa mide (ABBF). ABBF bound to alpha7 nAChR in rat brain membranes (Ki=62 nM) and to recombinant human 5-hydroxytryptamine (5-HT)3 receptors (Ki=60 nM). ABBF was a potent agonist at the recombinant rat and human alpha7 nAChR expressed in Xenopus oocytes, but it did not show agonist activity at other nAChR subtypes. ABBF acted as an antagonist of the 5-HT3 receptor and alpha3beta4, alpha4beta2, and muscle nAChRs (at higher concentrations). ABBF improved social recognition memory in rats (0.3-1 mg/kg p.o.). This improvement was blocked by intracerebroventricular administration of the alpha7 nAChR antagonist methyllycaconitine at 10 microg, indicating that it is mediated by alpha7 nAChR agonism. In addition, ABBF improved working memory of aged rats in a water maze repeated acquisition paradigm (1 mg/kg p.o.) and object recognition memory in mice (0.3-1 mg/kg p.o.). Rats trained to discriminate nicotine (0.4 mg/kg s.c.) from vehicle did not generalize to ABBF (0.3-30 mg/kg p.o.), suggesting that the nicotine cue is not mediated by the alpha7 nAChR and that selective alpha7 nAChR agonists may not share the abuse liability of nicotine. Our results support the hypothesis that alpha7 nAChR agonists may provide a novel therapeutic strategy for the treatment of cognitive deficits with low abuse potential.
ESTHER : Boess_2007_J.Pharmacol.Exp.Ther_321_716
PubMedSearch : Boess_2007_J.Pharmacol.Exp.Ther_321_716
PubMedID: 17308038

Title : A novel chloride channel in Drosophila melanogaster is inhibited by protons - Schnizler_2005_J.Biol.Chem_280_16254
Author(s) : Schnizler K , Saeger B , Pfeffer C , Gerbaulet A , Ebbinghaus-Kintscher U , Methfessel C , Franken EM , Raming K , Wetzel CH , Saras A , Pusch H , Hatt H , Gisselmann G
Ref : Journal of Biological Chemistry , 280 :16254 , 2005
Abstract : A systematic analysis of the Drosophila genome data reveals the existence of pHCl, a novel member of ligand-gated ion channel subunits. pHCl shows nearly identical similarity to glutamate-, glycine-, and histamine-gated ion channels, does however not belong to any of these ion channel types. We identified three different sites, where splicing generates multiple transcripts of the pHCl mRNA. The pHCl is expressed in Drosophila embryo, larvae, pupae, and the adult fly. In embryos, in situ hybridization detected pHCl in the neural cord and the hindgut. Functional expression of the three different splice variants of pHCl in oocytes of Xenopus laevis and Sf9 cells induces a chloride current with a linear current-voltage relationship that is inhibited by extracellular protons and activated by avermectins in a pH-dependent manner. Further, currents through pHCl channels were induced by a raise in temperature. Our data give genetic and electrophysiological evidence that pHCl is a member of a new branch of ligand-gated ion channels in invertebrates with, however, a hitherto unique combination of pharmacological and biophysical properties.
ESTHER : Schnizler_2005_J.Biol.Chem_280_16254
PubMedSearch : Schnizler_2005_J.Biol.Chem_280_16254
PubMedID: 15713676

Title : Refolding of the Escherichia coli expressed extracellular domain of alpha 7 nicotinic acetylcholine receptor - Tsetlin_2002_Eur.J.Biochem_269_2801
Author(s) : Tsetlin VI , Dergousova NI , Azeeva EA , Kryukova EV , Kudelina IA , Shibanova ED , Kasheverov IE , Methfessel C
Ref : European Journal of Biochemistry , 269 :2801 , 2002
Abstract : Heterologous expression of the extracellular domains (ECDs) of the nicotinic acetylcholine receptor (AChR) subunits may give large amounts of proteins for studying the functional and spatial characteristics of their ligand-binding sites. The ECD of the alpha 7 subunit of the homo-oligomeric alpha 7 neuronal AChR appears to be a more suitable object than the ECDs of other heteromeric neuronal or muscle-type AChRs. The rat alpha 7 ECDs (amino-acid residues approximately 1-210) were recently expressed in Escherichia coli as fusion proteins with maltose-binding protein [Fischer, M., Corringer, P., Schott, K., Bacher, A. & Changeux, J. (2001) Proc. Natl Acad. Sci. USA 98, 3567-3570] and glutathione S-transferase (GST) [Utkin, Y., Kukhtina, V., Kryukova, E., Chiodini, F., Bertrand, D., Methfessel, C. & Tsetlin, V. (2001) J. Biol. Chem. 276, 15810-15815]. However, these proteins exist in solution mostly as high-molecular mass aggregates rather than monomers or oligomers. In the present work it is found that refolding of GST-alpha 7-(1-208) protein in the presence of 0.1% SDS considerably decreases the formation of high-molecular mass aggregates. The C116S mutation in the alpha 7 moiety was found to further decrease the aggregation and to increase the stability of protein solutions. This mutation slightly increased the affinity of the protein for alpha-bungarotoxin (from Kd approximately 300 to 150 nm). Gel-permeation HPLC was used to isolate the monomeric form of the GST-alpha 7-(1-208) protein and its mutant almost devoid of SDS. CD spectra revealed that the C116S mutation considerably increased the content of beta structure and made it more stable under different conditions. The monomeric C116S mutant appears promising both for further structural studies and as a starting material for preparing the alpha 7 ECD in an oligomeric form.
ESTHER : Tsetlin_2002_Eur.J.Biochem_269_2801
PubMedSearch : Tsetlin_2002_Eur.J.Biochem_269_2801
PubMedID: 12047391

Title : Neuronal nicotinic receptors in the locust Locusta migratoria. Cloning and expression - Hermsen_1998_J.Biol.Chem_273_18394
Author(s) : Hermsen B , Stetzer E , Thees R , Heiermann R , Schrattenholz A , Ebbinghaus U , Kretschmer A , Methfessel C , Reinhardt S , Maelicke A
Ref : Journal of Biological Chemistry , 273 :18394 , 1998
Abstract : We have identified five cDNA clones that encode nicotinic acetylcholine receptor (nAChR) subunits expressed in the nervous system of the locust Locusta migratoria. Four of the subunits are ligand-binding alpha subunits, and the other is a structural beta subunit. The existence of at least one more nAChR gene, probably encoding a beta subunit, is indicated. Based on Northern analysis and in situ hybridization, the five subunit genes are expressed. localpha1, localpha3, and locbeta1 are the most abundant subunits and are expressed in similar areas of the head ganglia and retina of the adult locust. Because Loc<alpha3 binds alpha-bungarotoxin with high affinity, it may form a homomeric nAChR subtype such as the mammalian alpha7 nAChR. Localpha1 and Locbeta1 may then form the predominant heteromeric nAChR in the locust brain. localpha4 is mainly expressed in optic lobe ganglionic cells and localpha2 in peripherally located somata of mushroom body neurons. localpha3 mRNA was additionally detected in cells interspersed in the somatogastric epithelium of the locust embryo, suggesting that this isoform may also be involved in functions other than neuronal excitability. Transcription of all nAChR subunit genes begins approximately 3 days before hatching and continues throughout adult life. Electrophysiological recordings from head ganglionic neurons also indicate the existence of more than one functionally distinct nAChR subtype. Our results suggest the existence of several nAChR subtypes, at least some of them heteromeric, in this insect species.
ESTHER : Hermsen_1998_J.Biol.Chem_273_18394
PubMedSearch : Hermsen_1998_J.Biol.Chem_273_18394
PubMedID: 9660807

Title : Pharmacology of the nicotinic acetylcholine receptor from fetal rat muscle expressed in Xenopus oocytes - Cooper_1996_Eur.J.Pharmacol_309_287
Author(s) : Cooper JC , Gutbrod O , Witzemann V , Methfessel C
Ref : European Journal of Pharmacology , 309 :287 , 1996
Abstract : The fetal rat muscle nicotinic acetylcholine receptor was expressed in Xenopus oocytes. Using the voltage-clamp technique, the response to a range of agonists was measured, listed in order of (decreasing) activity efficacy: anatoxin > or = epibatidine > acetylcholine > DMPP (1,1-dimethyl-4-phenylpiperazinium) > > cytisine > pyrantel > nicotine > coniine > tubocurare > lobeline. The agonist responses were compared with the steric and electrostatic properties of the molecules, using molecular modelling. Single-channel current were measured in outside-out patches for acetylcholine, nicotine, cytisine, anatoxin and epibatidine. The conductance of the single channels was independent of the type of agonist. The mean open times were characteristic of the agonist applied. Tubocurare, better known for its antagonist properties, was also a partial agonist. Single-channel currents were also observed for tubocurare, and for methyllycaconitine in patches with a very high density of the muscle nicotinic acetylcholine receptor, and these were blocked by alpha-bungarotoxin. The agonist properties of physostigmine, galanthamine and their methyl derivatives were also investigated. The conductance of the channels observed in outside-out patches was similar to that obtained for the classical agonists. The single-channel currents observed for physostigmine, galanthamine and their methyl derivatives were blocked by alpha-bungarotoxin, methyllycaconitine and mecamylamine, in contrast to previously reported studies on neuronal and adult muscle nicotinic acetylcholine receptors.
ESTHER : Cooper_1996_Eur.J.Pharmacol_309_287
PubMedSearch : Cooper_1996_Eur.J.Pharmacol_309_287
PubMedID: 8874153

Title : Stable expression in HEK-293 cells of the rat alpha3\/beta4 subtype of neuronal nicotinic acetylcholine receptor - Stetzer_1996_FEBS.Lett_397_39
Author(s) : Stetzer E , Ebbinghaus U , Storch A , Poteur L , Schrattenholz A , Kramer G , Methfessel C , Maelicke A
Ref : FEBS Letters , 397 :39 , 1996
Abstract : The alpha3/beta4 subtype of neuronal nicotinic acetylcholine receptor (nAChR) was stably expressed in human embryonic kidney (HEK) 293 cells that co-expressed a voltage-gated Ca2+ channel. alpha3/beta4-nAChR-expressing clones were identified using the fura-2 Ca2+ imaging technique, and were further characterised by single-cell and whole-cell patch-clamp studies. Acetylcholine (ACh) induced fast activating currents which showed desensitisation and inward rectification. The conductance of the ACh-activated channel was 29 pS. The order of potency of the nicotinic agonists tested was cytisine approximately = nicotine > acetylcholine. The EC50 value for ACh was 145 microM; the Hill coefficient was close to 2. The currents elicited by ACh were effectively blocked by nicotinic antagonists, but not by the muscarinic antagonist atropine. These properties are comparable to the pharmacological and physiological profile of ganglionic nicotinic receptors and type III currents of cultured hippocampal neurons.
ESTHER : Stetzer_1996_FEBS.Lett_397_39
PubMedSearch : Stetzer_1996_FEBS.Lett_397_39
PubMedID: 8941710

Title : Noncompetitive agonism at nicotinic acetylcholine receptors\; functional significance for CNS signal transduction - Maelicke_1995_J.Recept.Signal.Transduct.Res_15_333
Author(s) : Maelicke A , Schrattenholz A , Storch A , Schroder B , Gutbrod O , Methfessel C , Weber KH , Pereira EE , Alkondon M , Albuquerque EX
Ref : J Recept Signal Transduct Res , 15 :333 , 1995
Abstract : The alkaloids (-)physostigmine (Phy), galanthamine (Gal) and codeine (Cod), and several derivatives and homologous compounds, can act as noncompetitive agonists (NCA) of nicotinic acetylcholine receptors (nAChR) from Torpedo electrocytes, frog and mammalian muscle cells, clonal rat pheochromocytoma cells, cultured hippocampal neurons and several ectopic expression systems, by interacting with a binding site on the alpha-subunits of these nAChRs that is insensitive to the natural transmitter, acetylcholine (ACh), and ACh-competitive agonists and antagonists. Several endogenous ligands, including opioid-type compounds, can also act via this site, albeit at higher concentrations than is typical for the interaction with their cognate receptors. The NCA-evoked responses can be observed at the single-channel level but they do not summate to significant macroscopic currents, suggesting that the major role of NCAs is to act as "co-agonists", thereby potentiating nAChR channel activation by the natural transmitter. In more general terms, noncompetitive agonists may constitute part of a "chemical network", by which intercellular messengers, in addition to serving their cognate receptors, could modulate the sensitivity of other neuroreceptors to their archetypic ligands. Such a mode of action would make centrally acting NCAs interesting candidate drugs in the treatment of neuro-degenerative diseases.
ESTHER : Maelicke_1995_J.Recept.Signal.Transduct.Res_15_333
PubMedSearch : Maelicke_1995_J.Recept.Signal.Transduct.Res_15_333
PubMedID: 8903949

Title : Physostigmine, galanthamine and codeine act as 'noncompetitive nicotinic receptor agonists' on clonal rat pheochromocytoma cells - Storch_1995_Eur.J.Pharmacol_290_207
Author(s) : Storch A , Schrattenholz A , Cooper JC , Abdel Ghani EM , Gutbrod O , Weber KH , Reinhardt S , Lobron C , Hermsen B , Soskic V , Pereira EF , Albuquerque EX , Methfessel C , Maelicke A
Ref : European Journal of Pharmacology , 290 :207 , 1995
Abstract : The acetylcholine esterase inhibitor (-)-physostigmine has been shown to act as agonist on nicotinic acetylcholine receptors from muscle and brain, by binding to sites on the alpha-polypeptide that are distinct from those for the natural transmitter acetylcholine (Schrder et al., 1994). In the present report we show that (-)-physostigmine, galanthamine, and the morphine derivative codeine activate single-channel currents in outside-out patches excised from clonal rat pheochromocytoma (PC12) cells. Although several lines of evidence demonstrate that the three alkaloids act on the same channels as acetylcholine, the competitive nicotinic antagonist methyllycaconitine only inhibited channel activation by acetylcholine but not by (-)-physostigmine, galanthamine or codeine. In contrast, the monoclonal antibody FK1, which competitively inhibits (-)-physostigmine binding to nicotinic acetylcholine receptors, did not affect channel activation by acetylcholine but inhibited activation by (-)-physostigmine, galanthamine and codeine. The three alkaloids therefore act via binding sites distinct from those for acetylcholine, in a 'noncompetitive' fashion. The potency of (-)-physostigmine and related compounds to act as a noncompetitive agonist is unrelated to the level of acetylcholine esterase inhibition induced by these drugs. (-)-Physostigmine, galanthamine and codeine do not evoke sizable whole-cell currents, which is due to the combined effects of low open-channel probability, slow onset and slow inactivation of response. In contrast, they sensitize PC12 cell nicotinic receptors in their submaximal response to acetylcholine. While the abundance of nicotinic acetylcholine receptor isoforms expressed in PC12 cells excludes identification of specific nicotinic acetylcholine receptor subtypes that interact with noncompetitive agonists, the identical patterns of single-channel current amplitudes observed with acetylcholine and with noncompetitive agonists suggested that all PC12 cell nicotinic acetylcholine receptor subtypes that respond to acetylcholine also respond to noncompetitive agonist. The action of noncompetitive agonists therefore seems to be highly conserved between nicotinic acetylcholine receptor subtypes, in agreement with the high level of structural conservation in the sequence region harboring major elements of this site.
ESTHER : Storch_1995_Eur.J.Pharmacol_290_207
PubMedSearch : Storch_1995_Eur.J.Pharmacol_290_207
PubMedID: 7589215

Title : Physostigmine and neuromuscular transmission - Maelicke_1993_Ann.N.Y.Acad.Sci_681_140
Author(s) : Maelicke A , Coban T , Schrattenholz A , Schroder B , Reinhardt-Maelicke S , Storch A , Godovac-Zimmermann J , Methfessel C , Pereira EF , Albuquerque EX
Ref : Annals of the New York Academy of Sciences , 681 :140 , 1993
Abstract : Single channel studies carried out in cultured rat myoballs and cultured hippocampal neurons, and ion flux studies performed on Torpedo electrocyte membrane vesicles, showed that physostigmine (Phy), a well-established acetylcholinesterase inhibitor, interacts directly with nicotinic acetylcholine receptors (nAChR). Low concentrations (0.1 microM) of Phy activate the receptor integral channel, whereas higher concentrations blocked the channel in its opened state. In contrast to channel activation by acetylcholine (ACh) and classical cholinergic agonists, however, Phy was capable of activating the nAChR channel even when the ACh binding sites were blocked by competitive antagonists, such as alpha-neurotoxins and d-tubocurarine, or when the nAChR was desensitized by preincubation with high concentrations of ACh. The binding site at which Phy binds and activates the nAChR was mapped. It was located within the N-terminal extracellular region of the alpha-polypeptide, in close proximity to the binding site of the natural transmitter. These data identify a novel binding site at nAChRs from many species and tissues that may be involved in receptor regulatory processes.
ESTHER : Maelicke_1993_Ann.N.Y.Acad.Sci_681_140
PubMedSearch : Maelicke_1993_Ann.N.Y.Acad.Sci_681_140
PubMedID: 8395146

Title : Molecular cloning of the antagonist-binding subunit of the glycine receptor - Grenningloh_1988_J.Recept.Res_8_183
Author(s) : Grenningloh G , Rienitz A , Schmitt B , Methfessel C , Zensen M , Beyreuther K , Gundelfinger ED , Betz H
Ref : J Recept Res , 8 :183 , 1988
Abstract : The postsynaptic receptor for the inhibitory neurotransmitter glycine is a heterooligomeric membrane protein which, after affinity purification on an antagonist column, contains three polypeptides of 48K, 58K and 93K. Sequencing of cDNA clones of the antagonist-binding 48K subunit revealed a structural organization similar to and significant amino acid homology with nicotinic acetylcholine receptor proteins. Our data suggest the existence of a set of related genes encoding transmembrane channel-forming neurotransmitter receptor polypeptides of excitable membranes.
ESTHER : Grenningloh_1988_J.Recept.Res_8_183
PubMedSearch : Grenningloh_1988_J.Recept.Res_8_183
PubMedID: 2838615

Title : The strychnine-binding subunit of the glycine receptor shows homology with nicotinic acetylcholine receptors - Grenningloh_1987_Nature_328_215
Author(s) : Grenningloh G , Rienitz A , Schmitt B , Methfessel C , Zensen M , Beyreuther K , Gundelfinger ED , Betz H
Ref : Nature , 328 :215 , 1987
Abstract : We have cloned and sequenced cDNAs of the strychnine-binding subunit of the rat glycine receptor, a neurotransmitter-gated chloride channel protein of the CNS. The deduced polypeptide shows significant structural and amino-acid sequence homology with nicotinic acetylcholine receptor proteins, indicating that there is a family of genes encoding neurotransmitter-gated ion channels.
ESTHER : Grenningloh_1987_Nature_328_215
PubMedSearch : Grenningloh_1987_Nature_328_215
PubMedID: 3037383

Title : Location of a delta-subunit region determining ion transport through the acetylcholine receptor channel - Imoto_1986_Nature_324_670
Author(s) : Imoto K , Methfessel C , Sakmann B , Mishina M , Mori Y , Konno T , Fukuda K , Kurasaki M , Bujo H , Fujita Y , Numa S
Ref : Nature , 324 :670 , 1986
Abstract : The combination of complementary DNA expression and single-channel current analysis provides a powerful tool for studying the structure-function relationship of the nicotinic acetylcholine receptor (AChR) (refs 1-5). We have previously shown that AChR channels consisting of subunits from different species, expressed in the surface membrane of Xenopus oocytes, can be used to relate functional properties to individual subunits. Here we report that, in extracellular solution of low divalent cation concentration, the bovine AChR channel has a smaller conductance than the Torpedo AChR channel. Replacement of the delta-subunit of the Torpedo AChR by the bovine delta-subunit makes the channel conductance similar to that of the bovine AChR channel. To locate the region in the delta-subunit responsible for this difference, we have constructed chimaeric delta-subunit cDNAs with different combinations of the Torpedo and bovine counterparts. The conductances of AChR channels containing chimaeric delta-subunits suggest that a region comprising the putative transmembrane segment M2 and the adjacent bend portion between segments M2 and M3 is involved in determining the rate of ion transport through the open channel.
ESTHER : Imoto_1986_Nature_324_670
PubMedSearch : Imoto_1986_Nature_324_670
PubMedID: 2432430

Title : Patch clamp measurements on Xenopus laevis oocytes: currents through endogenous channels and implanted acetylcholine receptor and sodium channels - Methfessel_1986_Pflugers.Arch_407_577
Author(s) : Methfessel C , Witzemann V , Takahashi T , Mishina M , Numa S , Sakmann B
Ref : Pflugers Arch , 407 :577 , 1986
Abstract : Functional acetylcholine receptor (AChR) and sodium channels were expressed in the membrane of Xenopus laevis oocytes following injection with poly(A)+-mRNA extracted from denervated rat leg muscle. Whole-cell currents, activated by acetylcholine or by depolarizing voltage steps had properties comparable to those observed in rat muscle. Oocytes injected with specific mRNA, transcribed from cDNA templates and coding for the AChR of Torpedo electric organ, expressed functional AChR channels at a much higher density. Single-channel currents were recorded from the oocyte plasma membrane following removal of the follicle cell layer and the vitelline membrane from the oocyte. The follicle cell layer was removed enzymatically with collagenase. The vitelline membrane was removed either mechanically after briefly exposing the oocyte to a hypertonic solution, or by enzyme treatment with pronase. Stretch activated (s.a.) currents were observed in most recordings from cell-attached patches obtained with standard patch pipettes. S.a.-currents were evoked by negative or positive pressure (greater than or equal to 5 mbar) applied to the inside of the pipette, and were observed in both normal and mRNA injected oocytes indicating that they are endogenous to the oocyte membrane. The s.a.-channels are cation selective and their conductance is 28 pS in normal frog Ringer's solution (20 +/- 1 degree C). Their gating is voltage dependent, and their open probability increases toward more positive membrane potentials. The density of s.a.-channels is estimated to be 0.5-2 channels per micron 2 of oocyte plasma membrane. In cell-attached patches s.a.-currents are observed much less frequently when current measurement is restricted to smaller patches of 3-5 micron 2 area using thick-walled pipettes with narrow tips. In outside-out patches s.a.-currents occur much less frequently than in cell-attached or inside-out patches. AChR-channel and sodium channel currents were observed only in a minority of patches from oocytes injected with poly(A)+-mRNA from rat muscle. AChR-channel currents were seen in all patches of oocytes injected with specific mRNA coding for Torpedo AChR. In normal frog Ringer's solution (20 +/- 2 degrees C) the conductance of implanted rat muscle AChR-channels was 38 pS and that of sodium channels 20 pS. The conductance of implanted Torpedo AChR channels was 40 pS. The conductance of implanted channels was similar in cell-attached and in cell-free patches.
ESTHER : Methfessel_1986_Pflugers.Arch_407_577
PubMedSearch : Methfessel_1986_Pflugers.Arch_407_577
PubMedID: 2432468

Title : Molecular distinction between fetal and adult forms of muscle acetylcholine receptor - Mishina_1986_Nature_321_406
Author(s) : Mishina M , Takai T , Imoto K , Noda M , Takahashi T , Numa S , Methfessel C , Sakmann B
Ref : Nature , 321 :406 , 1986
Abstract : Distinct classes of acetylcholine receptor channels are formed when Xenopus oocytes are injected with combinations of the bovine alpha-, beta-, gamma- and delta- or the alpha-, beta-, gamma- and epsilon-subunit-specific messenger RNAs. The conductance and gating properties of the two classes of channels, in conjunction with the developmental changes in the muscular contents of the mRNAs, suggest that replacement of the gamma-subunit by the epsilon-subunit is responsible for the functional alteration of the receptor during muscle development.
ESTHER : Mishina_1986_Nature_321_406
PubMedSearch : Mishina_1986_Nature_321_406
PubMedID: 2423878

Title : Role of acetylcholine receptor subunits in gating of the channel - Sakmann_1985_Nature_318_538
Author(s) : Sakmann B , Methfessel C , Mishina M , Takahashi T , Takai T , Kurasaki M , Fukuda K , Numa S
Ref : Nature , 318 :538 , 1985
Abstract : The Torpedo and calf acetylcholine receptors and hybrids composed of subunits from the two species have been produced in Xenopus oocytes by the use of the cloned complementary DNAs. Single-channel current measurements indicate that these receptors form channels of similar conductance but with different gating behaviour.
ESTHER : Sakmann_1985_Nature_318_538
PubMedSearch : Sakmann_1985_Nature_318_538
PubMedID: 2415826