CIRCULATING HUMAN C-REACTIVE PROTEIN BINDS VERY LOW-DENSITY LIPOPROTEINS

  • 1 January 1984
    • journal article
    • research article
    • Vol. 58  (1) , 237-244
Abstract
Native human CRP [C-reactive protein] in solution formed complexes with the abnormal lipoprotein .beta.-VLDL [very low density lipoprotein] in serum of patients with type III hyperlipoproteinemia. CRP also formed complexes in sera from individuals with type IV and type V hyperlipoproteinemia. The binding was Ca-dependent and inhibitable by free phosphorylcholine. No complexes were demonstrable in sera containing high LDL [low density lipoprotein] levels from cases of type IIa hyperlipoproteinemia. Addition of isolated .beta.-VLDL, but not of isolated LDL, to acute phase normolipoproteinemic serum caused the appearance of soluble CRP-lipoprotein complexes. In contrast, addition of an excess of isolated normal VLDL to acute phase serum or to isolated CRP was followed by agglutination (creaming) of the lipoprotein particles. Rabbit CRP formed soluble complexes both with normal human apoB [apolipoprotein B] containing lipoproteins and with the abnormal .beta.-VLDL. Human CRP complexed with rabbit .beta.-VLDL but not with normal rabbit serum lipoproteins. These interactions may be important for the role of CRP in health and disease. [CRP is the classical acute phase reactant.].