C-reactive protein fifty years on.
The discovery of C-reactive protein (CRP) half a century ago led to the description of the acute-phase reaction which is a fundamental response of the body to injury. Recent work on the structure and function of CRP has revealed the existence of a unique plasma protein family, including CRP and serum amyloid P component (SAP). These proteins have been conserved throughout vertebrate evolution. CRP binds specifically to a wide range of substances derived both from damaged autologous cells and from microorganisms. Complexed CRP can activate the complement system and, by virtue of its dramatically increased production in response to tissue injury, it probably acts primarily as a protective mechanism. However, in some circumstances CRP may also initiate or exacerbate inflammatory lesions. Clinical measurement of serum CRP is valuable as a screening test for organic disease and as a sensitive object index of disease activity and response to therapy in some inflammatory, infective, and ischaemic conditions. SAP closely resembles CRP in structure but not an acute-phase reactant in man. An apparently identical protein, amyloid P component (AP), is always found in amyloid deposits. AP is also found in normal tissues, as an integral constituent of vascular basement membranes and is located on the peripheral microfibrillar mantle of elastic fibres throughout the body.
D000208:Acute Disease; D002097:C-Reactive Protein / Q000032:analysis / Q000096:biosynthesis / Q000502:physiology*; D006801:Humans; D007239:Infections / Q000097:blood; D011485:Protein Binding; D000685:Serum Amyloid A Protein / Q000502:physiology
D000685:Serum Amyloid A Protein; D002097:C-Reactive Protein