Interaction of low-density lipoproteins with gangliosides.
The ganglioside uptake capacity of human serum low-density lipoproteins (LDL), the mode of ganglioside-LDL binding, and the influence of gangliosides on the floatation properties, size distribution, stability and fluorescence of LDL were investigated. The data obtained suggest that both hydrophobic and electrostatic forces are involved in formation of ganglioside-LDL complexes, but the former appear to be more important. Although association of gangliosides with LDL is predominantly unspecific, nonsaturable, and weak, a small saturable component due to specific ganglioside-apolipoprotein binding, also appears to be involved. In the presence of gangliosides the lipoprotein particles aggregate, the intrinsic fluorescence of LDL and their interaction with antibodies against apo-B change indicating that the state of apo-B [corrected] is modified by gangliosides.
Mikhailenko
I A
IA
Institute of Experimental Cardiology, U.S.S.R. Academy of Medical Sciences, Moscow.
Dubrovskaya
S A
SA
Korepanova
O B
OB
Timofeeva
N G
NG
Morozkin
A D
AD
Prokazova
N V
NV
Bergelson
L D
LD
D000937:Antigen-Antibody Reactions; D001055:Apolipoproteins B / Q000276:immunology; D002846:Chromatography, Affinity; D005679:G(M3) Ganglioside / Q000097:blood; D005732:Gangliosides / Q000097:blood*; D006801:Humans; D008077:Lipoproteins, LDL / Q000097:blood*; D046911:Macromolecular Substances; D013050:Spectrometry, Fluorescence
D001055:Apolipoproteins B; D005679:G(M3) Ganglioside; D005732:Gangliosides; D008077:Lipoproteins, LDL; D046911:Macromolecular Substances; C021298:ganglioside, GD1a