| Literature DB >> 17083939 |
Paola Caccin1, Michela Rigoni, Alessandra Bisceglie, Ornella Rossetto, Cesare Montecucco.
Abstract
Lysophosphatidylcholine rapidly paralyses the neuromuscular junction (NMJ), similarly to snake phospholipase A2 neurotoxins, implicating a lipid hemifusion-pore transition in neuroexocytosis. The mode and kinetics of NMJ paralysis of different lysophospholipids (lysoPLs) in high or low [Mg2+] was investigated. The following order of potency was found: lysophosphatidylcholine>lysophosphatidylethanolamine>lysophosphatidic acid>lysophosphatidylserine>lysophosphatidylglycerol. The latter two lysoPLs closely mimic the profile of paralysis caused by the toxins in high [Mg2+]. This paralysis is fully reversed by albumin washing. These findings provide novel insights on the mode of action of snake neurotoxins and qualify lysoPLs as novel agents to study neuroexocytosis.Entities:
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Year: 2006 PMID: 17083939 DOI: 10.1016/j.febslet.2006.10.039
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124