Kourie, J. I., and A. A. Shorthouse. Properties of cytotoxic peptideformed ion channels. Am J Physiol Cell Physiol 278: C1063–C1087, 2000.—Cytotoxic peptides are relatively small cationic molecules such as those found 1) in venoms, e.g., melittin in bee, scorpion toxins in scorpion, pilosulin 1 in jumper ant, and lycotoxin I and II in wolf spider; 2) in skin secretions (e.g., magainin I and II ...

Sodium currents mediated by voltage-sensitive sodium channels in normal and scorpion toxin-resistant neuroblastoma cells were measured using a giga-ohm seal recording method in the whole cell patch configuration. The voltage and time dependence of sodium currents were similar in normal and mutant cell lines. Half-maximal activation occurred for test depolarizations in the range of -7 to -11 mV....

Scorpion stings are very frequent in Tunisia; yet a method for evaluating envenoming severity and consequently victim treatment, has never been adequately established nor has its efficiency been properly evaluated. Indeed, a management of envenomed patients requires the optimization of envenoming antivenom immunotherapy. This task requires either, an accurate evaluation of toxicokinetic paramet...

Voltage sensing by voltage-gated sodium channels determines the electrical excitability of cells, but the molecular mechanism is unknown. ß-scorpion toxins bind specifically to neurotoxin receptor site 4 and induce a negative shift in the voltage dependence of activation through a voltagesensor trapping mechanism. Kinetic analysis showed that β-scorpion toxin binds to the resting state and subs...

he present study aimed to develop a method to record circadian patterns of electroretinogram (ERG) and electromyogram (EMG) simultaneously in unrestrained Egyptian yellow fat-tailed scorpion Androctonus australis under different light regimes. A specially designed aluminum "jacket" was properly fixed on the scorpion allowing its free movement during recording. The lightjacket extends along the ...

Scorpion venoms are complex polypeptide mixtures, the ion channel blockers and antimicrobial peptides being the best studied components. The coagulopathic properties of scorpion venoms are poorly studied and the data about substances exhibiting these properties are very limited. During research on the Heterometrus laoticus scorpion venom, we have isolated low-molecular compounds with anticoagul...

Predators feeding on toxic prey may evolve physiological resistance to the preys' toxins. Grasshopper mice (Onychomys spp.) are voracious predators of scorpions in North American deserts. Two species of grasshopper mice (Onychomys torridus and Onychomys arenicola) are broadly sympatric with two species of potentially lethal bark scorpion (Centruroides exilicauda and Centruroides vittatus) in th...

Excitation-contraction coupling was characterized in scorpion striated muscle fibers using standard microelectrode techniques as employed in studies on vertebrate skeletal muscle. The action potential of scorpion muscle consists of two phases of regenerative activity. A relatively fast, overshooting initial spike is followed by a prolonged after-discharge of smaller, repetitive spikes. This aft...

Scorpions and their venoms have been employed in medication since thousands of years in Asia. The scorpion venom is an extremely advanced mixture of salts, nucleotides, biogenic amines, enzymes, mucoproteins, peptides and proteins (e.g. Neurotoxins). Scorpion venoms contain peptides that block or modify ion-channel function and present some doable applications to regulate cell excitability. Spe...

Kurtoxin is a 63-amino acid polypeptide isolated from the venom of the South African scorpion Parabuthus transvaalicus. It is the first and only peptide ligand known to interact with Cav3 (T-type) voltage-gated Ca(2+) channels with high affinity and to modify the voltage-dependent gating of these channels. Here we describe the nuclear magnetic resonance (NMR) solution structure of kurtoxin dete...