Monoclonal antibody 5A binds apolipoprotein B-48 and inhibits the low density lipoprotein-receptor interaction.
In a panel of 10 monoclonal antibodies raised against human LDL we detected three antibodies (named 5A, 6B, and 6E) which recognize both apolipoprotein B-100 and B-48. Antibody 5A inhibited, in a dose dependent manner, the interaction of 125I-LDL with their receptor on human skin fibroblasts. Using thrombolytic fragments, the epitope of antibody 5A was mapped to the carboxy terminal region of apo B-48. MAB 5A was equipotent with MAB Mb 47, an inhibitory antibody whose epitope lies near a putative receptor binding domain of apo B in thrombolytic fragment T2. These findings suggest that areas other than the carboxy terminal portion of apo B-100 may participate in the LDL-receptor interaction, either directly or by determining the exposition of high affinity sites of apo B-100.
Corsini
A
A
Institute of Pharmacological Sciences, University of Milan, Italy.
Fantappiè
S
S
Marcovina
S
S
Granata
A
A
Fumagalli
R
R
Catapano
A L
AL
D000911:Antibodies, Monoclonal / Q000276:immunology*; D000918:Antibody Specificity; D000937:Antigen-Antibody Reactions; D053283:Apolipoprotein B-48; D001055:Apolipoproteins B / Q000276:immunology* / Q000378:metabolism; D001665:Binding Sites; D004705:Endocytosis; D000939:Epitopes; D006801:Humans; D066298:In Vitro Techniques; D008077:Lipoproteins, LDL / Q000276:immunology / Q000378:metabolism*; D010446:Peptide Fragments / Q000276:immunology; D011973:Receptors, LDL / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D053283:Apolipoprotein B-48; D001055:Apolipoproteins B; D000939:Epitopes; D008077:Lipoproteins, LDL; D010446:Peptide Fragments; D011973:Receptors, LDL