Contryphan-Vn:: a modulator of Ca2+-dependent K+ channels

被引:43
|
作者
Massilia, GR
Eliseo, T
Grolleau, F
Lapied, B
Barbier, J
Bournaud, R
Molgó, J
Cicero, DO
Paci, M
Schininà, ME
Ascenzi, P
Polticelli, F
机构
[1] Univ Roma Tre, Dept Biol, I-00146 Rome, Italy
[2] Univ Roma La Sapienza, Dept Biochem Sci, I-00198 Rome, Italy
[3] Scuola Int Super Studi Avanzati, I-34014 Trieste, Italy
[4] Univ Roma Tor Vergata, Dept Chem Sci & Technol, I-00133 Rome, Italy
[5] Univ Roma Tor Vergata, INFM, I-00133 Rome, Italy
[6] CNRS, UPR 9040, Neurobiol Cellulaire & Mol Lab, F-91191 Gif Sur Yvette, France
[7] UFR Sci, UPRES EA 2647, Neurophysiol Lab, F-49045 Angers, France
[8] Univ Roma La Sapienza, Dept Chem, I-00185 Rome, Italy
关键词
contryphan-Vn; solution structure; cockroach dorsal unpaired median neurons; rat fetal chromaflin cells; Ca2+-dependent K+ channels;
D O I
10.1016/S0006-291X(03)00331-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 (Periplanela americana) nerve cord on rat fetal chromaffin cells indicate that Contryphan-Vn affects both voltage-gated and Ca2+-dependent K+ channel activities, with composite and diversified effects in invertebrate and vertebrate systems. Voltage-gated and Ca2+-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 Ca2+-dependent K+ channels. (C) 2003 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:238 / 246
页数:9
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