High-sensitivity C-reactive Protein
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High-sensitivity C-reactive Protein
C-reactive protein (CRP) is an annular (ring-shaped) pentameric protein found in blood plasma, whose circulating concentrations rise in response to inflammation. It is an acute-phase protein 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 C1q. 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. It 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. History Discovered by Tillett and Francis in 1930, it was initially thought that CRP might be a pathogenic secretion since it was elevated in a variety of illnesses, including cancer. The later ...
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Pentameric Protein
A pentameric protein is a quaternary protein structure that consists of five protein subunits. Examples Ligand-gated ion channels Five sub-units come together to form a channel. Each channel consist of two alpha chain, one beta, one gamma and one delta chain. These five chains assemble together (along with certain receptors like protons or acetylcholine) forming the structure of the channel. A ligand-gated ion channel on the post-synaptic junction of the muscle-end plate is an example of such a channel. They are acetylcholine-operated ion channels, which means that acetylcholine brings about a conformational change. The channel allows the free movement of the cations like Na and K when acetylcholine binds to its receptors. Viral capsids Many viral capsids are formed by hexameric and pentameric proteins. Such capsids are assigned a triangulation number (T-number) which describe relation between the number of pentagons and hexagons. Carboxysomes Protein enclosing bacterial organe ...
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