These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Bioenergetic actions of beta-bungarotoxin, dendrotoxin and bee-venom phospholipase A2 on guinea-pig synaptosomes. Author: Nicholls D, Snelling R, Dolly O. Journal: Biochem J; 1985 Aug 01; 229(3):653-62. PubMed ID: 4052016. Abstract: Low concentrations of beta-bungarotoxin or bee-venom phospholipase A2 cause a progressive Ca2+-dependent increase in the proton permeability of the mitochondria within the synaptosomal cytosol, manifested as an increase in oligomycin-insensitive respiration and a partial depolarization of the mitochondrial membrane potential. This uncoupling appears to be a consequence of fatty acids liberated by phospholipase A2 activity at the plasma membrane, since it can be mimicked by the addition of oleate-albumin complexes, in which case there is no requirement for external Ca2+. Dendrotoxin does not affect the mitochondrial proton permeability in situ, but protects partially against the uncoupling action of beta-bungarotoxin. In contrast, this effect of bee-venom phospholipase A2 is unaffected by dendrotoxin. beta-Bungarotoxin, but not bee-venom phospholipase A2, induces a slow progressive depolarization of the plasma membrane. The action of beta-bungarotoxin at the plasma membrane appears not to be related to fatty acid production, since it is augmented rather than inhibited by raising albumin concentrations in the medium. It is concluded that beta-bungarotoxin has at least two actions on intact synaptosomes, both of which may involve interaction at the plasma membrane with a site common to dendrotoxin: first, a mitochondrial uncoupling mediated by fatty acids and, secondly, a depolarization at the plasma membrane.[Abstract] [Full Text] [Related] [New Search]