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Melittin Stimulates Incorporation and Degradation of Sphingomyelin in Synaptosomal Plasma Membranes
Author(s) -
Pellkofer R.,
Marsh D.,
HoffmannBleihauer P.,
Sandhoff K.
Publication year - 1982
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1982.tb07895.x
Subject(s) - melittin , sphingomyelin , degradation (telecommunications) , membrane , chemistry , synaptosome , biochemistry , biophysics , biology , computer science , telecommunications
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.