]> BibSonomy publications for /author/Fantappi%C3%A8 http://www.bibsonomy.org/burst/author/Fantappi%C3%A8 BibSonomy BuRST Feed for /author/Fantappi%C3%A8 2008-07-20T23:43:06+02:00 Monoclonal antibodies to human low density lipoprotein identify distinct areas on apolipoprotein B-100 relevant to the low density lipoprotein-receptor interaction. http://www.bibsonomy.org/bibtex/28470a55ffd3031830371a1e0072d15bf/biblio24 biblio24 2006-07-07T01:10:50+02:00 apob epitope mapping
Monoclonal antibodies to human low density lipoprotein identify distinct areas on apolipoprotein B-100 relevant to the low density lipoprotein-receptor interaction.
S. Fantappiè and A. Corsini and A. Sidoli and P. Uboldi and A. Granata and T. Zanelli and P. Rossi and S. Marcovina and R. Fumagalli and A. L. Catapano Journal of Lipid Research 33 1111--1121 (1992)
to apob epitope mapping by biblio24 on 2006-07-07 01:10:50 ]]> Institute of Pharmacological Sciences, University of Milano, Italy.Journal of Lipid ResearchAugust81111--1121Monoclonal antibodies to human low density lipoprotein identify distinct areas on apolipoprotein B-100 relevant to the low density lipoprotein-receptor interaction.331992apob epitope mapping 2006-07-07 01:10:50.0We have characterized the epitopes for ten murine monoclonal antibodies (Mabs) to human low density lipoprotein (LDL) and studied their ability to interfere with the LDL-receptor interaction. The epitopes for the antibodies were defined by using the following approaches: 1) interaction with apoB-48; 2) interaction with apoB-100 thrombolytic fragments; and 3) interaction with beta-galactosidase-apoB fusion proteins spanning different areas of the apoB-100 sequence. The results obtained are consistent with the following map of epitopes: Mab 6E, amino acids (aa) 1-1297, Mabs 5A and 6B, aa 1480-1693, Mabs 2A, 7A, 3B, and 4B, aa 2152-2377, Mabs 8A and 9A, aa 2657-3248 and 3H, aa 4082-4306. Four Mabs (2A, 5A, 7A, and 9A) whose epitopes are located in three different areas of apoB, dramatically reduced (up to 95%) the LDL-receptor interaction on cultured human fibroblasts; Fab fragments were as effective as the whole antibodies. Mab 3H, on the other hand, increased LDL binding up to threefold. These findings are consistent with the hypothesis that several areas of apoB-100 are involved independently or in concert in modulating the apoprotein B conformation required for interaction with the LDL receptor. Monoclonal antibody 5A binds apolipoprotein B-48 and inhibits the low density lipoprotein-receptor interaction. http://www.bibsonomy.org/bibtex/28a5794e6f329c353fcea2f5897cbd46b/biblio24 biblio24 2006-07-07T01:10:50+02:00 apob epitope mapping
Monoclonal antibody 5A binds apolipoprotein B-48 and inhibits the low density lipoprotein-receptor interaction.
A. Corsini and S. Fantappiè and S. Marcovina and A. Granata and R. Fumagalli and A. L. Catapano Biochem Biophys Res Commun 162 908--915 (1989)
to apob epitope mapping by biblio24 on 2006-07-07 01:10:50 ]]> Institute of Pharmacological Sciences, University of Milan, Italy.Biochem Biophys Res CommunAugust3908--915Monoclonal antibody 5A binds apolipoprotein B-48 and inhibits the low density lipoprotein-receptor interaction.1621989apob epitope mapping 2006-07-07 01:10:50.0In 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.