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Atherosclerosis is an arterial disease associated with dyslipidemia, abnormal arterial calcification and oxidative stress. It has been shown that a continued chronic inflammatory state of the arterial wall contributes to the development of atherosclerosis. The inflammatory stimulation, recruitment of inflammatory cells and production of pro-inflammatory cytokines enhances vascular inflammation. Some members of the S100 proteins family bind with their receptors, such as advanced glycation end products (RAGE), scavenger receptors (CD36) and toll-like receptor 4 (TLR-4), contributing to the cellular response in atherosclerotic progression. This review summarizes the roles of S100 proteins (S100A8, S100A9 and S100A12) in the vascular inflammation, vascular calcification and vascular oxidative stress. S100 proteins are released from monocytes, smooth muscle cells and endothelial cells in response to cellular stress stimuli, and then the binding of S100 proteins to RAGE activate downstream signaling such as transcription factor kappa B (NF-κB) translocation and reactive oxygen species (ROS) production, which act as a positive feedback loop for inducing pro-inflammatory phenotype in a wide variety of cell types including endothelial cells, vascular smooth muscle cells and leukocytes. Thus, it suggests that the inhibition of S100 proteins-mediated RAGE and TLR4 activation appears to be a promising approach to treat atherosclerosis. In addition, recent study showed that serum S100A12 can predict future cardiovascular events, highlighting that S100A12 is likely to be a potential biomarker of therapeutic efficacy and disease progression in coronary heart disease. Future studies of patients with coronary heart disease may provide more evidences supporting that S100 proteins is promising drug target in the prevention and therapy of atherosclerosis.
This article was published in the following journal.
Name: Clinica chimica acta; international journal of clinical chemistry
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An S100 protein characterized by four helix bundles that form N- and C-terminal EF HAND MOTIFS. It functions as a homodimer and interacts with both intracellular and extracellular signaling proteins. Aberrant S100A4 activity is associated with NEOPLASM METASTASIS; FIBROSIS; and RHEUMATOID ARTHRITIS.
A single-pass transmembrane CELL SURFACE RECEPTOR that binds ADVANCED GLYCOSYLATION END PRODUCTS to mediate cellular responses to both acute and chronic vascular inflammation in conditions such as ATHEROSCLEROSIS and DIABETES MELLITUS, TYPE 2 . It also binds AMYLOID BETA PEPTIDES and the alarmins S100A12 and S100 CALCIUM BINDING PROTEIN BETA SUBUNIT.
A single-pass transmembrane CELL SURFACE RECEPTOR that binds ADVANCED GLYCATION END PRODUCTS to mediate cellular responses to both acute and chronic vascular inflammation in conditions such as ATHEROSCLEROSIS and DIABETES MELLITUS, TYPE 2. It also binds AMYLOID BETA PEPTIDES and the ALARMINS - S100A12 and S100 CALCIUM BINDING PROTEIN BETA SUBUNIT.
A family of highly acidic calcium-binding proteins found in large concentration in the brain and believed to be glial in origin. They are also found in other organs in the body. They have in common the EF-hand motif (EF HAND MOTIFS) found on a number of calcium binding proteins. The name of this family derives from the property of being soluble in a 100% saturated ammonium sulfate solution.
An S100 calcium binding protein that contains two EF HAND MOTIFS and plays a role as a calcium sensor and modulator for many cellular processes such as CELL CYCLE progression; CELL MOTILITY and reorganization of the ACTIN CYTOSKELETON. Its expression is induced by growth factors and it is overexpressed in patients with ACUTE MYELOID LEUKEMIA.
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