TY - JOUR
T1 - Immunoreactivity of apo B towards monoclonal antibodies that inhibit the LDL-receptor interaction
T2 - effects of LDL oxidation
AU - Negri, Simonetta
AU - Roma, Paola
AU - Fogliatto, Roberta
AU - Uboldi, Patrizia
AU - Marcovina, Santica
AU - Catapano, Alberico L.
PY - 1993
Y1 - 1993
N2 - We studied the immunochemical stability of the epitopes for six monoclonal antibodies to human apolipoprotein B-100 upon Cu 2+-mediated (20 μM) oxidation of LDL. The antibodies used in this study, some of which are known to interfere with the interaction of LDL with their cellular receptors, recognize epitopes in the amino terminal region (Mb 19), in the middle part (6B, 2A, 7A, and 9A) and near as 3500 (Mb 47) of native apo B. All antibodies except one (7A) recognized native and oxidized LDL (OxLDL) equally well; the immunoreactivity of the epitope for Ab 7A was markedly reduced upon LDL oxidation. Since antibodies 2A, 7A, 9A, and Mb 47 inhibit the LDL-receptor interaction and OxLDL poorly interact in vitro with the LDL receptor we conclude that: (1) various epitopes for monoclonal antibodies against native apo B are spared upon LDL oxidation; and (2) the epitopes for antibodies 2A, 9A, and Mb 47 do not define a unique domain of apo B directly involved in the binding of LDL to their receptor.
AB - We studied the immunochemical stability of the epitopes for six monoclonal antibodies to human apolipoprotein B-100 upon Cu 2+-mediated (20 μM) oxidation of LDL. The antibodies used in this study, some of which are known to interfere with the interaction of LDL with their cellular receptors, recognize epitopes in the amino terminal region (Mb 19), in the middle part (6B, 2A, 7A, and 9A) and near as 3500 (Mb 47) of native apo B. All antibodies except one (7A) recognized native and oxidized LDL (OxLDL) equally well; the immunoreactivity of the epitope for Ab 7A was markedly reduced upon LDL oxidation. Since antibodies 2A, 7A, 9A, and Mb 47 inhibit the LDL-receptor interaction and OxLDL poorly interact in vitro with the LDL receptor we conclude that: (1) various epitopes for monoclonal antibodies against native apo B are spared upon LDL oxidation; and (2) the epitopes for antibodies 2A, 9A, and Mb 47 do not define a unique domain of apo B directly involved in the binding of LDL to their receptor.
KW - LDL receptor
KW - Monoclonal antibodies
KW - Oxidized LDL
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U2 - 10.1016/0021-9150(93)90099-G
DO - 10.1016/0021-9150(93)90099-G
M3 - Article
C2 - 7692863
AN - SCOPUS:0027308077
VL - 101
SP - 37
EP - 41
JO - Atherosclerosis
JF - Atherosclerosis
SN - 0021-9150
IS - 1
ER -