The reference OMIM entry for this protein is 123260

C-reactive protein, pentraxin-related; crp
Pentraxin 1, short; ptx1

CLONING

Oliveira et al. (1979) reported that the CRP protein contains 187 amino acids, but Lei et al. (1985) and Woo et al. (1985) determined that CRP contains an 18-amino acid signal sequence and a mature protein of 206 amino acids. CRP and serum amyloid P protein (APCS; 104770) are members of the family of proteins known as pentraxins (see 600750). CRP is a ubiquitous protein found in both vertebrates and invertebrates phylogenetically spanning 400 million years of evolution. Originally CRP was defined as a substance, observed in the plasma of patients with acute infections, that reacted with the C polysaccharide of the pneumococcus. It was discovered by Tillett and Francis (1930) and studied by Abernethy and Avery (1941). It is one of the plasma proteins that are called acute phase reactants because of a pronounced rise in concentration after tissue injury or inflammation; in the case of CRP, the rise may be 1000-fold or more. CRP is composed of 5 identical, 21,500-molecular weight subunits. It is detectable on the surface of about 4% of normal peripheral blood lymphocytes. Acute phase reactant CRP is produced in the liver; CRP detectable on lymphocytes is produced by those cells (Kuta and Baum, 1986). Kilpatrick and Volanakis (1991) reviewed the molecular genetics, structure, and function of CRP.

GENE FUNCTION

On the basis of in vitro and in vivo experiments, it has been proposed that the function of CRP relates to its ability to recognize specifically foreign pathogens and damaged cells of the host and to initiate their elimination by interacting with humoral and cellular effector systems in the blood. Thus, the CRP molecule has both a recognition and an effector function (Kilpatrick and Volanakis, 1991). Robey et al. (1984) demonstrated that CRP binds with high affinity to chromatin. It has been proposed that one of its major physiologic functions is to act as a scavenger for chromatin released by dead cells during the acute inflammatory process. Interleukin-6 (IL6; 147620) and tumor necrosis factor alpha (TNFA; 191160) are inflammatory cytokines and the main inducers of the secretion of C-reactive protein in the liver. CRP is a marker of low-grade inflammation that may have a role in the pathogenesis of atherosclerotic lesions in humans (Blake and Ridker, 2002). The effects of TNF-alpha are mediated by 2 receptors: type 1 (TNFR1; 191190) and type 2 (TNFR2; 191191). The Nurses' Health Study (NHS) and the Health Professionals Follow-up Study (HPFS) are prospective cohort investigations involving a large number of U.S. female registered nurses and U.S. male health professionals, respectively. Pai et al. (2004) examined plasma levels of soluble TNFR1, soluble TNFR2, interleukin-6, and C-reactive protein as markers of risk for coronary heart disease among women and men participating, respectively, in these 2 studies. Among participants who provided a blood sample and who were free of cardiovascular disease at baseline, 239 women and 265 men had a nonfatal myocardial infarction or fatal coronary heart disease (see 607339) during 8 years and 6 years of follow-up, respectively. Pai et al. (2004) found elevated levels of inflammatory markers, particularly C-reactive protein, indicating an increased risk of coronary heart disease. Although plasma lipid levels were more strongly associated with an increased risk than were inflammatory markers, the level of C-reactive protein was a significant contributor to the predict ... More on the omim web site

Subscribe to this protein entry history

June 30, 2020: Protein entry updated
Automatic update: OMIM entry 123260 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).