257
Original Paper
Cell Physiol Biochem 2006;17:257-268 Accepted: April 05, 2006 Cellular Physiology Cellular Physiology Cellular Physiology Cellular Physiology Cellular Physiology
and Biochemistr and Biochemistr and Biochemistr and Biochemistr and Biochemistry
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The Sodium Channel of Human Excitable Cells is
a Target for Gambierol
M. Carmen Louzao
1
, Eva Cagide
1
, Mercedes R. Vieytes
2
, Makoto
Sasaki
3
, Haruhiko Fuwa
3
, Takeshi Yasumoto
4
and Luis M. Botana
1
1
Departamento de Farmacologia,
2
Departamento de Fisiologia Animal. Facultad de Veterinaria,
Universidad de Santiago de Compostela, Lugo,
3
Graduate School of Life Sciences, Tohoku University,
4
Japan Food Research Laboratories, Tama Laboratory, Tokyo
Luis M. Botana
Departamento de Farmacologia, Facultad de Veterinaria
Universidad de Santiago de Compostela
27002 Lugo (Spain)
Tel & Fax -+34 982 252 242, E-Mail ffbotana@lugo.usc.es
Key Words
Sodium channel Gambierol Neuroblastoma
Abstract
Background: Gambierol is a polycyclic ether toxin with
the same biogenetic origin as ciguatoxins. Gambierol
has been associated with neurological symptoms in
humans even though its mechanism of action has not
been fully characterized. Methods: We studied the
effect of gambierol in human neuroblastoma cells by
using bis-oxonol to measure membrane potential and
FURA-2 to monitor intracellular calcium. Results: We
found that this toxin: i) produced a membrane
depolarization, ii) potentiated the effect of veratridine
on membrane potential iii) decreased ciguatoxin-
induced depolarization and iv) increased cytosolic
calcium in neuroblastoma cells. Conclusion: These
results indicate that gambierol modulate ion fluxes
by acting as a partial agonist of sodium channels.
Introduction
In the last years there has been an explosion of
interest in biologically active natural products of marine
origin [1-4]. Polycyclic ethers class of marine natural
products (exemplified by brevetoxins (PbTXs), ciguatoxins
(CTXs), maitotoxin and recently gambierol) are
particularly attractive for chemists, due to their structural
novelty and toxicity [3, 5]. The target receptor has only
been identified for PbTXs and CTXs, mainly because of
the extremely limited availability of those toxins from
natural sources [6]. PbTXs and CTXs exert their
neurotoxicity by association with a specific binding site
on the voltage-gated sodium channels of excitable
membranes, designed as site 5 [7-12]. Toxin binding alters
the channel’s function in two ways: (1) the activation
voltage for channel opening shifts to a more negative value
and (2) the inactivation of opened channels is inhibited,
resulting in persistent activation [11, 13].
Despite the common polycyclic structure, all those
toxins show diverse biological activities with extreme
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