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Titolo:
Interactions between 3-(trifluoromethyl)-3-(m-[I-125]iodophenyl)diazirine and tetracaine, phencyclidine, or histrionicotoxin in the Torpedo species nicotinic acetylcholine receptor ion channel
Autore:
Gallagher, MJ; Chiara, DC; Cohen, JB;
Indirizzi:
Harvard Univ, Sch Med, Dept Neurobiol, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 ed, Dept Neurobiol, Boston, MA 02115 USA
Titolo Testata:
MOLECULAR PHARMACOLOGY
fascicolo: 6, volume: 59, anno: 2001,
pagine: 1514 - 1522
SICI:
0026-895X(200106)59:6<1514:IB3A>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
H-3 MEPROADIFEN MUSTARD; SODIUM DODECYL-SULFATE; AFFINITY BINDING-SITE; NONCOMPETITIVE ANTAGONIST; ALPHA-SUBUNIT; AMINO-ACIDS; GEL-ELECTROPHORESIS; CHLORPROMAZINE; BLOCKERS; REGIONS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Cohen, JB Harvard Univ, Sch Med, Dept Neurobiol, 220 Longwood Ave, Boston,MA 02115 USA Harvard Univ 220 Longwood Ave Boston MA USA 02115 , MA 02115 USA
Citazione:
M.J. Gallagher et al., "Interactions between 3-(trifluoromethyl)-3-(m-[I-125]iodophenyl)diazirine and tetracaine, phencyclidine, or histrionicotoxin in the Torpedo species nicotinic acetylcholine receptor ion channel", MOLEC PHARM, 59(6), 2001, pp. 1514-1522

Abstract

3-(Trifluoromethyl)-3-(m-[I-125]iodophenyl)diazirine ([I-125]TID) and [H-3]tetracaine, an aromatic amine, are noncompetitive antagonists (NCAs) of the Torpedo species nicotinic acetylcholine receptor (nAChR), which have beenshown by photoaffinity labeling to bind to a common site in the ion channel in the closed state, Although tetracaine and TID bind to the same site, the amine NCAs phencyclidine (PCP) and histrionicotoxin (HTX), which are also believed to bind within the ion channel, interact competitively with tetracaine but allosterically with TID. To better characterize drug interactions within the nAChR ion channel in the closed state, we identified the aminoacids photoaffinity labeled by [I-125]TID in the presence of tetracaine, PCP, or HTX. In the absence of other drugs, [I-125]TID reacts with alpha Leu-251 (alpha M2-9) and alpha Val-255 (alpha M2-13) and the homologous residues in each of the other subunits. None of the NCAs shifted the sites of [I-125]TID labeling to other residues within the ion channel. Tetracaine inhibited [I-125]TID labeling of M2-9 and M2-13 without changing the relative(125)I incorporation at these positions, whereas PCP and HTX each altered the pattern of [I-125]TID incorporation at M2-9 and M2-13. These results indicate that tetracaine and TID bind in a mutually exclusive manner to a common site in the closed channel that is spatially separated from the binding sites for PCP and HTX.

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Documento generato il 26/09/20 alle ore 12:11:04