Monoclonal antibody 5A binds apolipoprotein B-48 and inhibits the low density lipoprotein-receptor interaction
Articolo
Data di Pubblicazione:
1989
Citazione:
Monoclonal antibody 5A binds apolipoprotein B-48 and inhibits the low density lipoprotein-receptor interaction / A. Corsini, S. Fantappiè, S. Marcovina, A. Granata, R. Fumagalli, A.L. Catapano. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - 162:3(1989 Aug 15), pp. 908-915.
Abstract:
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.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
Antibodies, Monoclonal ; Endocytosis ; Antigen-Antibody Reactions ; Antibody Specificity ; Peptide Fragments ; Receptors, LDL ; Apolipoproteins B ; Humans ; Lipoproteins, LDL ; Apolipoprotein B-48 ; Epitopes ; Binding Sites
Elenco autori:
A. Corsini, S. Fantappiè, S. Marcovina, A. Granata, R. Fumagalli, A.L. Catapano
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