1992 Volume 21 Issue 4 Pages 231-244
The aim of this study is to define the role of human C-reactive protein (CRP) in lipid metabolism, especially in relation to the binding capacity of CRP with serum lipoproteins (LP) by using gel filtration. The uptake of the CRP-LP complex through macrophage was observed by means of a light microscope.
Column chromatography of hyperlipidemic human serum with or without the addition of CRP revealed that a complex was formed between CRP and LP, when the serum contained more than 180mg/dl of total cholesterol and also with more than 110mg/dl of triglyceride. CRP binds sufficiently with LP if the column is passed through with serum in which the titer of total cholesterol is around 250-299mg/dl. Very low density lipoproteins (VLDL) were found to bind with CRP in the hyperlipidemic serum. Binding of CRP with LP was calcium ion-dependent and was inhibited by ligands such as phosphorylcholine or 6-amino-n-caproic acid. The CRP-LP complex was ingested by macrophage.
