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Melittin Stimulates Incorporation and Degradation of Sphingomyelin in Synaptosomal Plasma Membranes
Authors:R Pellkofer  D Marsh  P Hoffmann-Bleihauer  K Sandhoff
Institution:Institut für Organische Chemie und Biochemie der Universität Bonn, F.R.G.;Max-Plunck-Institut fur hiophysikalische Chemie, Güttingen, F.R.G.
Abstract:Abstract: Melittin enhanced sphingomyelin (SPM) degradation by the neutral membrane-bound sphingomyelinase from calf brain synaptosomal plasma membranes (SYM) up to 20-fold. Melittin in concentrations as high as 100 μM did not significantly alter membrane fluidity of SYM as measured by fluorescence depolarization and electron spin resonance (ESR) using diphenylhexatriene and a doxy1 derivative of SPM, respectively. In the concentration range 100-1000 μM. melittin was observed to rigidify SYM. The incorporation of SPM.erivatives into the lipid bilayer of SYM.as demonstrated by ESR measurements. Melittin enhanced the uptake of SPM-derivatives into SYM.
Keywords:Membrane-bound neutral sphingomyelinase  Synaptosomal plasma membranes  Melittin  Fluorescence depolarization  Electron spin resonance  Sphingomyelin spin label
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