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Abstract:

The α9 and α10 nicotinic cholinergic subunits assemble to form the receptor believed to mediate synaptic transmission between efferent olivocochlear fibers and hair cells of the cochlea, one of the few examples of postsynaptic function for a non-muscle nicotinic acetylcholine receptor (nAChR). However, it has been suggested that the expression profile of α9 and α10 overlaps with that of α7 in the cochlea and in sites such as dorsal root ganglion neurons, peripheral blood lymphocytes, developing thymocytes, and skin. We now report the cloning, total synthesis, and characterization of a novel toxin α-conotoxin PeIA that discriminates between α9α10 and α7 nAChRs. This is the first toxin to be identified from Conus pergrandis, a species found in deep waters of the Western Pacific. α-Conotoxin PeIA displayed a 260-fold higher selectivity for α-bungarotoxin-sensitive α9α10 nAChRs compared with α-bungarotoxin-sensitive α7 receptors. The IC50 of the toxin was 6.9 ± 0.5 nM and 4.4 ± 0.5 nM for recombinant α9α10 and wild-type hair cell nAChRs, respectively. α-Conotoxin PeIA bears high resemblance to α-conotoxins MII and GIC isolated from Conus magus and Conus geographus, respectively. However, neither α-conotoxin MII nor α-conotoxin GIC at concentrations of 10 μM blocked acetylcholine responses elicited in Xenopus oocytes injected with the α9 and α10 subunits. Among neuronal non-α-bungarotoxin- sensitive receptors, α-conotoxin PeIA was also active at α3β2 receptors and chimeric α6/α3β2β3 receptors. α-Conotoxin PeIA represents a novel probe to differentiate responses mediated either through α9α10 or α7 nAChRs in those tissues where both receptors are expressed. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.

Registro:

Documento: Artículo
Título:A novel α-conotoxin, PeIA, cloned from Conus pergrandis, discriminates between Rat α9α10 and α7 nicotinic cholinergic receptors
Autor:McIntosh, J.M.; Plazas, P.V.; Watkins, M.; Gomez-Casati, M.E.; Olivera, B.M.; Elgoyhen, A.B.
Filiación:Department of Psychiatry, University of Utah, Salt Lake City, UT 84112, United States
Department of Biology, University of Utah, Salt Lake City, UT 84112, United States
Department of Pathology, University of Utah, Salt Lake City, UT 84112, United States
Instituto de Investigaciones en Ingeniería Genetica y Biología Molecular, Consejo Nacional de Investigaciones Cientificas y Técnicas, Universidad de Buenos Aires, Buenos Aires 1428, Argentina
Dept. Biology, University of Utah, 257 South 1400 East, Salt Lake City, UT 84112-0840, United States
Palabras clave:Biosynthesis; Blood; Cells; Characterization; Cloning; Molecular biology; Muscle; Skin; Cochlea; Hair cells; Thymocytes; Xenopus oocytes; Biochemistry; acetylcholine; alpha bungarotoxin; alpha conotoxin PeIA; bungarotoxin receptor; chimeric protein; conotoxin; nicotinic alpha9alpha10 receptor; nicotinic receptor; protein subunit; receptor subtype; recombinant protein; snail venom; unclassified drug; animal cell; article; binding affinity; cholinergic receptor blocking; cochlea; cochlear nerve; concentration response; controlled study; Conus pergrandis; DNA sequence; genetic variability; hair cell; IC 50; matrix assisted laser desorption ionization time of flight mass spectrometry; molecular cloning; molecular evolution; nonhuman; oocyte; priority journal; protein determination; protein expression; protein function; protein localization; rat; receptor binding; receptor sensitivity; sequence analysis; snail; synaptic transmission; toxin analysis; toxin synthesis; wild type; Xenopus; Acetylcholine; Amino Acid Sequence; Animals; Base Sequence; Bungarotoxins; Cell Differentiation; Cloning, Molecular; Conotoxins; Dose-Response Relationship, Drug; Electrophysiology; Ganglia, Spinal; Hair Cells, Inner; Inhibitory Concentration 50; Kinetics; Lymphocytes; Molecular Sequence Data; Mollusca; Neurons; Oocytes; Peptides; Protein Subunits; Rats; Rats, Sprague-Dawley; Receptors, Nicotinic; Recombinant Proteins; RNA; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Synaptic Transmission; Thymus Gland; Xenopus; Xenopus laevis; Conus geographus; Conus magus
Año:2005
Volumen:280
Número:34
Página de inicio:30107
Página de fin:30112
DOI: http://dx.doi.org/10.1074/jbc.M504102200
Título revista:Journal of Biological Chemistry
Título revista abreviado:J. Biol. Chem.
ISSN:00219258
CODEN:JBCHA
CAS:acetylcholine, 51-84-3, 60-31-1, 66-23-9; alpha bungarotoxin, 11032-79-4; Acetylcholine, 51-84-3; alpha-bungarotoxin receptor; alpha10 acetylcholine receptor, rat; Bungarotoxins; Chrna9 protein, rat; Conotoxins; Peptides; Protein Subunits; Receptors, Nicotinic; Recombinant Proteins; RNA, 63231-63-0
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v280_n34_p30107_McIntosh

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Citas:

---------- APA ----------
McIntosh, J.M., Plazas, P.V., Watkins, M., Gomez-Casati, M.E., Olivera, B.M. & Elgoyhen, A.B. (2005) . A novel α-conotoxin, PeIA, cloned from Conus pergrandis, discriminates between Rat α9α10 and α7 nicotinic cholinergic receptors. Journal of Biological Chemistry, 280(34), 30107-30112.
http://dx.doi.org/10.1074/jbc.M504102200
---------- CHICAGO ----------
McIntosh, J.M., Plazas, P.V., Watkins, M., Gomez-Casati, M.E., Olivera, B.M., Elgoyhen, A.B. "A novel α-conotoxin, PeIA, cloned from Conus pergrandis, discriminates between Rat α9α10 and α7 nicotinic cholinergic receptors" . Journal of Biological Chemistry 280, no. 34 (2005) : 30107-30112.
http://dx.doi.org/10.1074/jbc.M504102200
---------- MLA ----------
McIntosh, J.M., Plazas, P.V., Watkins, M., Gomez-Casati, M.E., Olivera, B.M., Elgoyhen, A.B. "A novel α-conotoxin, PeIA, cloned from Conus pergrandis, discriminates between Rat α9α10 and α7 nicotinic cholinergic receptors" . Journal of Biological Chemistry, vol. 280, no. 34, 2005, pp. 30107-30112.
http://dx.doi.org/10.1074/jbc.M504102200
---------- VANCOUVER ----------
McIntosh, J.M., Plazas, P.V., Watkins, M., Gomez-Casati, M.E., Olivera, B.M., Elgoyhen, A.B. A novel α-conotoxin, PeIA, cloned from Conus pergrandis, discriminates between Rat α9α10 and α7 nicotinic cholinergic receptors. J. Biol. Chem. 2005;280(34):30107-30112.
http://dx.doi.org/10.1074/jbc.M504102200