Interaction of malondialdehyde-modified bovine serum albumin and mouse peritoneal macrophages.

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Abstract
Reaction of bovine serum albumin (BSA) with malondialdehyde (MDA), a product of lipid oxidation, resulted in the modification of amino residues of the protein to produce three kinds of adducts in the protein molecules, aminopropenal (1), N,N''-disubstituted 1-amino-3-iminopropene (2) and 4-methyl-1,4-dihydropyridine-3,5-dicarbaldehyde (3). Modified BSA, in which 39 out of the total of 60 amino residues were modified, showed effective binding to thioglycollate-induced mouse peritoneal macrophages. MDA-modified BSA inhibited the binding of formaldehyde-modified BSA to the macrophages, indicating that MDA-modified BSA binds to the scavenger receptor for formaldehyde-modified BSA. However, the converse was not the case, suggesting that MDA-modified BSA binds to additional receptors to which formaldehyde-modified BSA does not. Reduction of the double bonds of 1 and 2, and the aldehyde functions of 1 and 3 in MDA-modified BSA did not affect the binding of the protein. However, modification of the aldehyde function of 1 with glycine resulted in loss of the ligand activity of the protein. These results suggest that adducts 1, 2, and 3 in the BSA molecule are not directly involved in the binding to the scavenger receptor of the macrophages, though adduct 1 may be located near the binding site or may play a role in maintaining the active conformation of the binding site.

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