Melittin Stimulates Incorporation and Degradation of Sphingomyelin in Synaptosomal Plasma Membranes |
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| Authors: | R. Pellkofer D. Marsh P. Hoffmann-Bleihauer K. Sandhoff |
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| Affiliation: | Institut für Organische Chemie und Biochemie der Universität Bonn, F.R.G.;Max-Plunck-Institut fur hiophysikalische Chemie, Güttingen, F.R.G. |
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| 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. |
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| Keywords: | Membrane-bound neutral sphingomyelinase Synaptosomal plasma membranes Melittin Fluorescence depolarization Electron spin resonance Sphingomyelin spin label |
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