Immobilization Onto A Microtiter Plate Induces C-reactive Protein(CRP) To Form A Biologically Active Isoform Expressing Both PCRP And MCRP Antigenicity

It has been shown that there are at least two distinct isoforms of C-reactive protein (CRP), the native pentameric CRP (pCRP) and the modified CRP (mCRP), both of which play an important role in inflammation and the cardiovascular disease. Recently researchers have focused on the connection of previously obtained data to the new understanding of the existence of different CRP isoforms with very distinct characteristics. It is believed that the various effection of CRP is regulated by its conformational change. We immobilized pCRP onto the microtiter plate, showing that the strong-hydrophobic interface can induce pCRP to form a biologically active isoform of CRP expressing the antigenicity of both pCRP and mCRP. The new isoform is shown to be able to bind pCRP with high affinity in a Ca-dependent way, depending on the C-terminal octapeptide, PC-binding site and 8D8-recognition epitopes. It is also shown to be able to activate classical complement pathway, and exert a different effection on monocyte-macrophage from pCRP and mCRP. The functional characteristics of the isoform provide a possible way by which the apoptotic or injured cells interact with pCRP, regulating the process of inflammation.