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Pentameric CRP can be irreversibly dissociated, with the resultant free subunits termed monomeric (or modified) CRP (mCRP). The dissociation of nCRP into free subunits has been observed at either high concentrations of urea (34) or high temperatures in the absence of calcium (35). The mCRP molecules are distinguished from nCRP by their different antigenic, biological, and electrophoretic activities (36) and by the fact that they express different neoepitopes (37). The two isoforms of CRP have been shown to have distinct biological functions in the inflammatory process. For example, Khreiss et al. (37) provided evidence that nCRP suppresses the adherence of platelets to neutrophils, whereas mCRP enhances these interactions. This difference in function can be explained by the two isoforms binding to differing types of Fcgamma (Fcγ)-receptor involved in the signaling process. The mCRP isoform utilizes the low-affinity immune complex binding immunoglobulin G (IgG) receptor called FcγRIIIb (CD16b) on neutrophils and FcγRIIIa (CD16a) on monocytes, while nCRP binds to the low-affinity IgG receptor FcγRIIa (CD32) (38).
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