What does CRP do?
CRP was first discovered as a major binding protein to the cell wall protein of pneumococci. CRP is a member of the pentraxin protein family, which is so named because it is made of 5 identical peptide subunits. It is synthesized by the hepatocytes. CRP, which is elaborated dramatically during acute Inflammation, augments the immune response to certain antigens, activates complement, and Increases the monocytic production of tissue factors. Complement, which is activated, creates the membrane attack complex. Bacterial toxins elicit a response from NF kappa B and IL-6 . Interestingly, CRP also appears to bind low-density lipoprotein cholesterol (LDLC) in vitro, which suggests a direct interaction with the atherogenic lipid. Actually binding of CRP to enzymatically remodeled LDL (E-LDL) activates complement via CRP dependent pathways. Initially, CRP is a protective protein, which binds to E-LDL sparing the terminal sequence.
