There are 13 families and about 1,400 described species/subspecies of scorpions. Scorpion venom/toxins are proteins that bind to Na or K channels. For
Na channel, the toxin inhibits the inactivation of activated channels and blocking neuronal transmission. There are short- and long-chain peptide
toxins. Short chain scorpion toxins constitute the largest group of K channel blockers. One of the role of a K channel, known as KV1.3, is to help
maintain large electrical gradients for the sustained transport of ions such as Ca2+ that controls T lymphocyte proliferation. Thus
KV1.3 blockers could be potential immunosuppressants for the treatment of autoimmune disorders (such as rheumatoid arthritis, inflammatory bowel
disease and multiple sclerosis). Toxins being investigated include: * Chlorotoxin is a 36-amino acid peptide found in the venom of the
deathstalker scorpion (Leiurus quinquestriatus) which blocks small-conductance chloride channels. The fact that chlorotoxin binds preferentially to
glioma cells has allowed the development of new methods, that still are under investigation, for the treatment and diagnosis of several types of
cancer. * Maurotoxin from the venom of the Tunisian Scorpio maurus palmatus
edit on 14-5-2011 by RRokkyy because: (no reason given)
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