Contryphan-Vn: a modulator of Ca2+-dependent K+ channels
| Autor: | Paolo Ascenzi, Jordi Molgó, Maria Eugenia Schininà, Tommaso Eliseo, Julien Barbier, Maurizio Paci, Gabriella Raybaudi Massilia, Daniel O. Cicero, Françoise Grolleau, Bruno Lapied, Fabio Polticelli, Roland Bournaud |
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| Přispěvatelé: | Department of Biology, Universita di Roma, Department of Chemistry, Laboratoire Récepteurs et Canaux Ioniques Membranaires (RCIM), Université d'Angers (UA)-Institut National de la Recherche Agronomique (INRA), Laboratoire de neurobiologie cellulaire et moléculaire (NBCM), Centre National de la Recherche Scientifique (CNRS), Institut de Neurobiologie Alfred Fessard (INAF), Dipartimento di Scienze e Tecnologie Chimiche, Università degli Studi di Roma Tor Vergata [Roma], Scuola Internazionale Superiore di Studi Avanzati / International School for Advanced Studies (SISSA / ISAS), Department of Biochemical Sciences 'Rossi Fanelli', Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' [Rome], Récepteurs et Canaux Ioniques Membranaires (RCIM), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Massilia, Gr, Eliseo, T, Grolleau, F, Lapied, B, Barbier, J, Bournaud, R, Molgó, J, Cicero, Do, Paci, M, Schininà, Me, Ascenzi, Paolo, Polticelli, Fabio |
| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy Patch-Clamp Techniques Potassium Channels Time Factors Chromaffin Cells Ca2+ -dependent K+ channels Cockroach dorsal unpaired median neurons Contryphan-Vn Rat fetal chromaffin cells Solution structure Snails MESH: Neurons Venom Biochemistry 0302 clinical medicine MESH: Chromaffin Cells MESH: Animals MESH: Snails Cell Line Transformed Neurons 0303 health sciences ca2+ -dependent k+ channels ca2+-dependent k+ channels cockroach dorsal unpaired median neurons contryphan contryphan-vn cyclic peptides rat fetal chromaffin cells rat fetal chromaflin cells solution structure MESH: Electrophysiology biology Anatomy MESH: Potassium Channels Potassium channel Electrophysiology MESH: Calcium [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC] Ca2+-dependent K+ channels MESH: Models Molecular Periplaneta MESH: Rats Biophysics Mollusk Venoms Peptides Cyclic Cone snail Cell Line 03 medical and health sciences MESH: Patch-Clamp Techniques Animals Humans Channel blocker Patch clamp MESH: Cell Line Transformed Settore BIO/10 Molecular Biology MESH: Peptides Cyclic 030304 developmental biology Contryphan MESH: Humans MESH: Magnetic Resonance Spectroscopy MESH: Time Factors Cell Biology MESH: Mollusk Venoms biology.organism_classification Rats MESH: Cell Line Calcium 030217 neurology & neurosurgery |
| Zdroj: | Biochemical and Biophysical Research Communications Biochemical and Biophysical Research Communications, Elsevier, 2003, 303 (1), pp.238-46. ⟨10.1016/S0006-291X(03)00331-0⟩ |
| ISSN: | 0006-291X 1090-2104 |
| DOI: | 10.1016/S0006-291X(03)00331-0⟩ |
| Popis: | Contryphan-Vn is a D-tryptophan-containing disulfide-constrained nonapeptide isolated from the venom of Conus ventricosus, the single Mediterranean cone snail species. The structure of the synthetic Contryphan-Vn has been determined by NMR spectroscopy. Unique among Contryphans, Contryphan-Vn displays the peculiar presence of a Lys-Trp dyad, reminiscent of that observed in several voltage-gated K(+) channel blockers. Electrophysiological experiments carried out on dorsal unpaired median neurons isolated from the cockroach (Periplaneta americana) nerve cord on rat fetal chromaffin cells indicate that Contryphan-Vn affects both voltage-gated and Ca(2+)-dependent K(+) channel activities, with composite and diversified effects in invertebrate and vertebrate systems. Voltage-gated and Ca(2+)-dependent K(+) channels represent the first functional target identified for a conopeptide of the Contryphan family. Furthermore, Contryphan-Vn is the first conopeptide known to modulate the activity of Ca(2+)-dependent K(+) channels. |
| Databáze: | OpenAIRE |
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