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

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Researchers partially purified a 94- to 97-kDa macrophage receptor that specifically binds oxidized low-density lipoprotein and recognizes oxidatively damaged cells, distinguishing it from the acetyl LDL receptor and other known binding proteins.

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This study characterizes a 94- to 97-kDa plasma membrane protein from mouse peritoneal macrophages that specifically binds oxidized low density lipoprotein with higher affinity than acetylated low density lipoprotein. The researchers demonstrate that this receptor is distinct from the acetyl LDL receptor, as well as from Fc gamma RII and CD36, indicating it represents a separate pathway for oxidatively modified lipid uptake. They propose that this protein facilitates the recognition and phagocytosis of oxidatively damaged cells by macrophages. The paper does not explicitly discuss endometriosis or adenomyosis; it was included in the corpus via a keyword match in the upstream search index.

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Abstract

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 distinct receptor that recognizes OxLDL with a higher affinity than it recognizes acetyl LDL. We describe the partial purification and characterization of a 94- to 97-kDa plasma membrane protein from mouse peritoneal macrophages that specifically binds OxLDL. This receptor is shown to be distinct from the acetyl LDL receptor as well as from two other macrophage proteins that also bind OxLDL--the Fc gamma RII receptor and CD36. We suggest that this OxLDL-binding membrane protein participates in uptake of OxLDL by murine macrophages and also represents a receptor responsible for macrophage binding and phagocytosis of oxidatively damaged cells.
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Abstract 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 distinct receptor that recognizes OxLDL with a higher affinity than it recognizes acetyl LDL. We describe the partial purification and characterization of a 94- to 97-kDa plasma membrane protein from mouse peritoneal macrophages that specifically binds OxLDL. This receptor is shown to be distinct from the acetyl LDL receptor as well as from two other macrophage proteins that also bind OxLDL--the Fc gamma RII receptor and CD36. We suggest that this OxLDL-binding membrane protein participates in uptake of OxLDL by murine macrophages and also represents a receptor responsible for macrophage binding and phagocytosis of oxidatively damaged cells. 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MeSH descriptors

Cell Adhesion Molecules Lipoproteins, LDL Macrophages Receptors, Cell Surface Receptors, LDL Animals Antigens, CD Antigens, CD CD36 Antigens Female Humans In Vitro Techniques Lipoproteins, LDL Lipoproteins, LDL Macrophages Macrophages Membrane Proteins Membrane Proteins Membrane Proteins Mice

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