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It is known that macrophages recognize and take up oxidized low density lipoprotein (LDL) and this macrophage recognition has been suggested to be due to modification of the lysine (Lys) residues of apoprotein B (apo B). In order to determine whether such modification is involved in recognition, delipidated apo B was modified with lipid peroxidation products and the macrophage recognition of the modified apo B was examined. When delipidated apo B was treated with linoleic acid 13-mono-hydroperoxide (LOOH) and trans-2-octenal (octenal), apo B became fluorescent and its Lys and histidine (His) residues were decreased. When delipidated apo B, partially methylated at the epsilon-amino groups of Lys residues, was treated with LOOH and octenal, fluorescence was not produced and the free Lys residues were not decreased. LOOH- and octenal-modified delipidated apo B were recognized by mouse peritoneal macrophages. The macrophage recognition of the modified apo B was prevented by maleyl bovine serum albumin, indicating that the scavenger receptor was involved in recognition. Neither methyl apo B nor methyl apo B, modified with LOOH or octenal, was recognized by macrophages. Neutralization of positively charged Lys residues of apo B by modification with LOOH and octenal may be requisite for recognition. Bovine serum albumin modified with LOOH and octenal prevented the recognition of the modified apo B, indicating that none of the intrinsic structure of apo B is required for recognition.

Modification of Delipidated Apoprotein B of Low Density Lipoprotein by Lipid Oxidation Products in Relation to Macrophage Scavenger Receptor Binding.