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Biochemistry of C-reactive protein (CRP)
- Molecular mass: 23 000 D
- Synthesis: Liver
- Normal range: < 3mg/l
Biochemistry of C-reactive protein (CRP)
C-reactive protein (CRP) is an annular (ring-shaped), pentameric acute phase protein found in blood plasma, whose levels rise in response to inflammation. It consists of 5 identical subunits and shows high similarity to the serum amyloidal p protein (SAP). CRP is also known as high-sensitivity C-reactive protein (hs-CRP) and ultra-sensitive C-reactive protein (us-CRP).
CRP is of hepatic origin that increases following interleukin-6 secretion by macrophages and T cells. Its physiological role is to bind to lysophosphatidylcholine expressed on the surface of dead or dying cells (and some types of bacteria) in order to activate the complement system via the C1Q complex.
CRP is synthesized by the liver in response to factors released by macrophages and fat cells (adipocytes). It is a member of the pentraxin family of proteins. CRP is not related to C-peptide (insulin) or protein C (blood coagulation). C-reactive protein was the first pattern recognition receptor (PRR) to be identified.
Clinical significance of C-reactive protein
In inflammatory processes, infections and tissue damage serum concentrations of the acute phase proteins, as that of the CRP, can increase 10,000-fold. Recent studies further demonstrate a correlation between the CRP concentration and coronary disease. Slightly increased CRP levels can serve as a predictor for cardiovascular disease, even if the concentrations are within the normal range. Highly sensitive determinations of this parameter allow an early recognition of the risk in stable and unstable angina pectoris.
Clinical or Research use of CRP
Prognostic marker for cardiovascular diseases
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