Arterioscler Thromb 1994,
PMID: 8305421
Mookerjea, S; Francis, J; Hunt, D; Yang, C Y; Nagpurkar, A
We have previously shown the binding of low-density lipoprotein (LDL) to immobilized rat C-reactive protein (CRP) and the formation of a fluid-phase complex between these two proteins. In this report we used immunoelectrophoresis and agarose gel electrophoresis to show increased anodic migration of the LDL particle as a result of the modification of LDL by rat CRP. The degradation of the modified 125I-LDL by rat peritoneal macrophages was increased more than twofold in the presence of rat CRP. The increase in rat CRP-mediated 125I-LDL degradation by macrophages was dependent on the concentrations of 125I-LDL and rat CRP. This increased 125I-LDL degradation was inhibited by phosphorylcholine. In contrast, the degradation of 125I-acetyl-LDL by macrophages was not affected by rat CRP, although acetylated LDL inhibited the rat CRP-stimulated degradation of 125I-LDL. Increasing concentrations of LDL did not affect the degradation of rat 125I-CRP by the macrophages, which suggested that the rat CRP and the modified LDL did not enter the cell as a complex. Our results suggested that the increased degradation of 125I-LDL was caused by the charge modification of 125I-LDL by rat CRP, due to a fluid-phase complex formation between 125I-LDL and rat CRP, and that the degradation involved the scavenger receptor present on the macrophages.
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Text Mining Data
LDL → C-reactive protein: "
Rat
C-reactive protein causes a charge modification of
LDL and stimulates its degradation by macrophages
"
125I-LDL → CRP: "
The degradation of the modified 125I-LDL by rat peritoneal macrophages was increased more than twofold in the presence of rat CRP
"
125I-LDL → CRP: "
In contrast, the degradation of 125I-acetyl-LDL by macrophages was not affected by rat CRP, although acetylated LDL inhibited the rat CRP stimulated degradation of 125I-LDL
"
125I-acetyl-LDL — CRP: "
In contrast, the degradation of 125I-acetyl-LDL by macrophages was not affected by rat CRP , although acetylated LDL inhibited the rat CRP stimulated degradation of 125I-LDL
"
125I-LDL → CRP: "
Our results suggested that the increased degradation of 125I-LDL was caused by the charge modification of 125I-LDL by rat CRP , due to a fluid-phase complex formation between 125I-LDL and rat CRP, and that the degradation involved the scavenger receptor present on the macrophages
"
Manually curated Databases
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