The fully air-conditioned Wistari conference room offers a view l

The fully air-conditioned Wistari conference room offers a view like no other – the reef is right outside. After

‘work’ you can fish, swim, dive, reef walk, take a snorkel boat or semi-submersible trip, or enjoy a p38 MAPK signaling sunset cruise or island spa. Attendance is limited to 100 participants. Further Organisers: Paul Alewood, Richard Lewis and Glenn King. Enquiries to Thea:[email protected]
“Potassium channels are multiprotein complexes formed of conducting α-subunits which can be associated with regulatory β-subunits. The α subunit can assemble into homo or hetero-tetramers forming the K+ selective pore, which is structurally conserved between the different families of K+ channels (MacKinnon et al., 1998). The potassium voltage-gated channel family (KV channels) is activated by depolarization allowing an outward movement of potassium ions through

the pore of this multiprotein. This influx of ions repolarizes the membrane potential (Catterall, 1995). KV channels play a major role in a wide variety of physiological process such as regulation of heart rate, neuronal excitability, BEZ235 manufacturer muscle contraction, hormonal secretion, neurotransmitter release, insulin secretion, cell volume regulation and cell proliferation (Coetzee et al., 1999 and Abbas et al., 2008). This family of channels is remarkable because of their diversity, which include 40 different channels, classified into 12 distinct subfamilies based on their amino acid sequence homology (KV1 to KV 12) (Gutman et al., 2005). To access the specific function of each KV channel in the cell some selective blockers and modulators need to be identified and characterized. Because of their importance in many aspects of cellular regulation, the KV channels are molecular targets for a wide range of biological compounds such as animal toxins (Catterall et al., 2007). Scorpions are one of the most ancient groups of animals on earth, with more than 400 million years of evolution without big

changes in their morphology (Briggs, 1987). Their venoms contain a cocktail of components such as enzymes, peptides, nucleotides, lipids, mucoproteins, Paclitaxel biogenic amines and other unknown molecules (Possani et al., 1981). The venom of the Brazilian yellow scorpion Tityus serrulatus (Tsv) has been extensively investigated and many of its toxins have been isolated and characterized (for review see Cologna et al., 2009). The best studied components of Tsv are the long chain toxins containing 60–70 amino acidic residues cross-linked by four disulfide brigdes and mainly active on NaV channels. Short chain toxins, composed of 30–42 amino acidic residues and cross-linked by three or four disulfide bridges, establish a second family of toxins from Tsv, most of them active on KV channels.

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