Interaction of gangliosides with low-density proteins from human blood
Timofeeva, N.G.; Martynova, M.A.; Pokrovskiĭ, S.N.; Adamova, I.I.; Prokazova, N.V.
Biokhimiia 52(4): 650-654
1987
ISSN/ISBN: 0320-9725 PMID: 3593794 Document Number: 301398
Gangliosides have been shown to modulate the receptor-mediated endocytosis of low density lipoproteins (LDL). The direct interaction of LDL with various gangliosides has been studied. Binding of gangliosides to LDL immobilized on CNBr-Sepharose (LDL-Sepharose) and the influence of gangliosides on the fluorescence of LDL containing anthrylvinyl-labeled sphingomyelin were investigated. The binding of 3H-gangliosides to LDL-Sepharose, as well as fluorescence polarization of LDL were found to depend on the structure and concentration of the gangliosides in a specific saturable manner. The data obtained indicate that gangliosides interact with apolipoprotein B via specific binding sites.