C-Reactive Protein : A Liver Boon

The acute-phase protein known as C-reactive protein (CRP) has a homopentameric structure with phosphocholine (PCh) as its particular phospholipid for Ca binding. Interleukin-6 is the major inducer of the gene during the acute phase, which regulates CRP expression mostly at the transcriptional level. The architecture and chemical makeup of CRP's ligand-binding site as well as its crystal structure have been identified. CRP can identify a variety of pathogenic targets as well as membranes of injured and necrotic host cells thanks to PCh's widespread dispersion in pathogen polysaccharides and cellular membranes.

When CRP is attached to a multivalent ligand, it can effectively start the assembly of a C3 convertase by the conventional pathway, opsonizing complement fragments on the surface of the ligand. The CRP-initiated complement activation, however, does not trigger acute inflammatory responses and membrane damage because the protein does not favour the creation of a C5 convertase. CRP also functions as an opsonin by interacting with the Fc receptors on phagocytic cells. Neutrophil Fc receptor interactions with other CRP-initiated signals result in an overall anti-inflammatory impact. Therefore, host defence against bacterial infections and cell elimination seem to be the primary biological functions of CRP.

In vivo testing using transgenic mice has demonstrated protection against deadly bacterial infection, complement-induced alveolitis, and endotoxemia. The involvement in atherogenesis and the pathophysiology of myocardial damage during myocardial infarction are two additional roles that have been described. CRP, like other acute-phase proteins, is a part of the first line of innate host defence, according to the overwhelming body of evidence.

References:

1. https://stock.adobe.com/ca/images/c-reactive-protein-crp-human-inflammation-biomarker-3d-render/450402565

2. https://pubmed.ncbi.nlm.nih.gov/11532280/