Scavenger receptor-mediated recognition of maleylated albumin and its relation to subsequent endocytic degradation.

Rat sinusoidal liver cells take up maleylated bovine serum albumin (maleyl-BSA) and its demaleylated form (demaleyl-BSA) by scavenger receptor-mediated endocytosis. Cellular binding of maleyl-BSA and demaleyl-BSA and its quantitative relation to subsequent intracellular degradation were investigated. The binding affinities of these ligands were almost equal whereas the number of binding sites for maleyl-BSA was more than twice as large than that for demaleyl-BSA. However, no difference was observed in their endocytic degradation. The amounts of maleyl-BSA degraded were proportional to those bound to the cell surface up to a certain level. However, a further increase in cell-bound ligands did not affect the degradation of maleyl-BSA. Several polyanions such as fucoidin and dextran sulfate of Mr = 5000 inhibited the binding of maleyl-BSA but did not affect its degradation. In contrast, acetylated or oxidized low density lipoprotein had virtually no effect on cellular binding of maleyl-BSA but exhibited profound effects on its intracellular degradation. Similar results were obtained with rat peritoneal macrophages. Based on these data, we would propose that two binding sites are involved in the receptor-mediated ligand recognition; one is coupled to subsequent endocytic degradation, and the other serves as a binding site for polyanionic compounds.