Venom from Anemesia species of spider modulates high voltage-activated Ca(2+) currents from rat cultured sensory neurones and excitatory post synaptic currents from rat hippocampal slices.

Abstract:

:The actions of crude venom from Anemesia species of spider were investigated in cultured dorsal root ganglion neurones from neonatal rats and hippocampal slices. Using mass spectrometry (MALDI-TOF MS), 10-12 distinct peptides with masses between about 3 and 10kDa were identified in the crude spider venom. At a concentration of 5 microg/ml crude Anemesia venom transiently enhanced the mean peak whole cell voltage-activated Ca(2+) current in a voltage-dependent manner and potentiated transient increases in intracellular Ca(2+) triggered by 30mM KCI as measured using Fura-2 fluorescence imaging. Additionally, 5-8 microg/ml Anemesia venom increased the amplitude of glutamatergic excitatory postsynaptic currents evoked in hippocampal slices. Omega-Conotoxin GVIA (1 microM) prevented the increase in voltage-activated Ca(2+) currents produced by Anemesia venom. This attenuation occurred when the cone shell toxin was applied before or after the spider venom. Anemesia venom (5 microg/ml) created no significant change in evoked action potentials but produced modest but significant inhibition of voltage-activated K(+) currents. At a concentration of 50 microg/ml Anemesia venom only produced reversible inhibitory effects, decreasing voltage-activated Ca(2+) currents. However, no significant effects on Ca(2+) currents were observed with a concentration of 0.5 microg/ml. The toxin(s) in the venom that enhanced Ca(2+) influx into sensory neurones was heat-sensitive and was made inactive by boiling or repetitive freeze-thawing. Boiled venom (5 microg/ml) produced significant inhibition of voltage-activated Ca(2+) currents and freeze-thawed venom inhibited Ca(2+) transients measured using Fura-2 fluorescence. Our data suggest that crude Anemesia venom contains components, which increased neuronal excitability and neurotransmission, at least in part this was mediated by enhancing Ca(2+) influx through N-type voltage-activated Ca(2+) channels.

journal_name

Cell Calcium

journal_title

Cell calcium

authors

Kalikulov D,Ayar A,Nuritova F,Frenguelli BG,McClelland D,Martin DJ,Davidson I,Scott RH

doi

10.1054/ceca.2001.0228

keywords:

subject

Has Abstract

pub_date

2001-09-01 00:00:00

pages

212-21

issue

3

eissn

0143-4160

issn

1532-1991

pii

S0143-4160(01)90228-3

journal_volume

30

pub_type

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