Abstract

Publisher Summary The polyamine toxins, obtained from the venom of a variety of orb-weaver spiders are rapidly emerging as unique tools for understanding excitatory amino acid (EM) transmission and related pharmacology or physiology. In this chapter, the chemistry and pharmacology of Araneidae polyamine spider venom toxins is reviewed and a brief discussion of the venom from the funnel-web spider is also included. The chemistry involved in the preparation of many of the naturally occurring polyamines has been discussed in the chapter. Polyamine spider venoms have highly polar hydroxyaryl and amino acid residues. Interest in the polyamine spider toxins is a result of the observation that these molecules affect those synapses, at which an excitatory amino acid (EAA) is the neurotransmitter. Compounds that affect EAA function, particularly those that antagonize the action of such transmitters, are therefore of considerable agricultural (insect control) and therapeutic interest. Blockade of neuromuscular transmission in invertebrates by polyamin spider toxins reveals their glutamate antagonist activity. Polyamine spider venoms also act on glutaminergic synapses in vertebrate systems. Partially purified JSTX blocks the responses of CA1 pyramidal neurons in rat hippocampus both to stimulation of the appropriate afferent neurons and to direct the application of glutamate. A variety of venoms have been screened for their ability to block synaptic transmission at glutaminergic synapses in the chick cochlear nucleus. A number of toxins from the funnel-web spider Agelenopsis aperta paralyze insects. These toxins contain low molecular weight acylpolyamine constituents, at least six amino acid residue peptides, and several larger polypeptides. Two classes of toxins from Agelenopsis aperta venom that block the transmission in the chick cochlear nucleus assay have also been discussed in the chapter. The results of these studies suggest that considerable structural and functional diversity exists within the polyamine toxin class and that these compounds differ significantly from previously-known classes of EAA and calcium antagonists.

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