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J. Biol. Chem., Vol. 259, Issue 18, 11305-11311, 09, 1984
ME Haberland, CL Olch and AM Folgelman
The ability of the scavenger receptor of human monocyte macrophages to
recognize human low density lipoproteins (LDL) progressively modified by
three lysine-specific reagents, malondialdehyde, acetic anhydride, or
succinic anhydride, has been investigated. Regardless of the reagent
utilized, receptor-mediated uptake was dependent upon modification of
greater than 16% of the peptidyl lysines rather than upon the net negative
charge of derivatized LDL. Rates of lysosomal hydrolysis of acetyl-LDL and
succinyl-LDL increased as a function of progressive modification and
reflected the amount of derivatized LDL binding to the receptor.
Succinylation or acetylation of greater than 60% of the lysines was
necessary to attain maximal ligand binding, internalization, and
degradation. In contrast, modification of only 16% of the peptidyl lysines
by malondialdehyde resulted in maximal levels of binding, uptake, and
hydrolysis. The expression of receptor recognition site(s) appears to
depend upon the charge modification of critical lysine residues of the LDL
protein rather than the net negative charge of the lipoprotein complex.
Malondialdehyde, a bifunctional reactant, may modify surface and
sequestered lysines concomitantly and thus promote efficient formation of
the recognition site(s).
Role of lysines in mediating interaction of modified low density lipoproteins with the scavenger receptor of human monocyte macrophages
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