Article Abstract:
Research findings on transmembrane receptors that are activated by extracellular adenosine and ATP were presented at the 5th Annual Neuropharmacology Conference held in Oct 1997. A proposed topology for P2X receptors of two transmembrane regions consisted of a large extracellular loop and intracellular N and C termini. The loop was found to be the site for the glycosylation of the P2X receptor. Data suggest that the P2Y receptor UDP is a species homologue of the P2Y6 receptor. The conference also highlighted the neurotransmitter functions of ATP.
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Article Abstract:
The pharmacological and electrophysiological properties of adenosine triphosphate-channels were studied and results show that these channels are ligand-gated and are present in muscle and neural cells. The receptor on the ATP-activated ion channel is of the P2 type with reactive blue 2 dye as a potent competitive antagonist. However, data on potential channel blockers are limited. It is suggested that these channels have a nicotinic acetylcholine-like receptive subunit.
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Article Abstract:
ATP-binding cassette (ABC) proteins belong to a family of structurally related membrane proteins with a common intracellular motif that binds and hydrolyzes ATP. Recent findings show that sulphonylurea drugs, traditionally used in the treatment of non-insulin dependent diabetes mellitus, bind to an ABC protein to modulate insulin secretion. This discovery suggests that other ABC proteins could be pharmacological targets for future drug discovery.
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