A MACROPHAGE RECEPTOR FOR OXIDIZED LOW-DENSITY-LIPOPROTEIN DISTINCT FROM THE RECEPTOR FOR ACETYL LOW-DENSITY-LIPOPROTEIN - PARTIAL-PURIFICATION AND ROLE IN RECOGNITION OF OXIDATIVELY DAMAGED CELLS
E. Ottnad et al., A MACROPHAGE RECEPTOR FOR OXIDIZED LOW-DENSITY-LIPOPROTEIN DISTINCT FROM THE RECEPTOR FOR ACETYL LOW-DENSITY-LIPOPROTEIN - PARTIAL-PURIFICATION AND ROLE IN RECOGNITION OF OXIDATIVELY DAMAGED CELLS, Proceedings of the National Academy of Sciences of the United Statesof America, 92(5), 1995, pp. 1391-1395
The binding and uptake of oxidatively modified low density lipoprotein
(OxLDL) by mouse peritoneal macrophages occurs, in part, via the well
characterized acetyl LDL receptor, However, several lines of evidence
indicate that as much as 30-70% of the uptake can occur via a distinc
t receptor that recognizes OxLDL with a higher affinity than it recogn
izes acetyl LDL, We describe the partial purification and characteriza
tion of a 94- to 97-kDa plasma membrane protein from mouse peritoneal
macrophages that specifically binds OxLDL. This receptor is shown to b
e distinct from the acetyl LDL receptor as well as from two other macr
ophage proteins that also bind OxLDG - the Fc gamma RII receptor and C
D36, We suggest that this OHLDL-binding membrane protein participates
in uptake of OxLDL by murine macrophages and also represents a recepto
r responsible for macrophage binding and phagocytosis of oxidatively d
amaged cells.