S100A9

S100A9

A gene on chromosome 1q21 that encodes a member of the S100 family of proteins, which contain 2 EF-hand calcium-binding motifs and as a group regulate cell cycle progression and differentiation and other cellular processes. S100A9 has antimicrobial activity against bacteria and fungi and provides resistance to invasion by pathogenic bacteria, and it upregulates transcription of genes under the control of NF-kappa-B; it is linked to the endotoxic shock response to bacterial lipopolysaccharide. S100A9 promotes tubulin polymerisation and macrophage and granulocyte migration and infiltration into wound sites; it is a pro-inflammatory mediator and upregulates IL8 release and cell surface expression of ICAM1. Extracellular S100A9 (calprotectin) binds to target cells and promotes apoptosis.
 
Molecular pathology
Altered expression of S100A9 is linked to cystic fibrosis.
References in periodicals archive ?
Active involvement of alarmins S100A8 and S100A9 in the regulation of synovial activation and joint destruction during mouse and human osteoarthritis.
Moreover, S100A8 (calgranulin A) and S100A9 (calgranulin B) both relate to ROS production.
Serum protein S100A9, SOD3, and MMP9 as new diagnostic biomarkers for pulmonary tuberculosis by iTRAQ- coupled two-dimensional LC-MS/MS.
S100A8 and S100A9 induce cytokine expression and regulate the NLRP3 inflammasome via ROS-dependent activation of NF-[kappa][B.
Identification of human S100A9 as a novel target for treatment of autoimmune disease via binding to quinoline-3-carboxamides.
Calprotectin is a calcium and zinc binding protein complex formed by S100A8 and S100A9 proteins.
Other calcium ion binding proteins include calmodulin or S100A8 and S100A9, which complex to form calprotectin, which explains almost identical localization in Figure 5, a through e and f through j.
S100A8 and S100A9 calcium-binding proteins: localization within normal and cyclosporin A-induced overgrowth gingiva.
The students discovered that both groups of mice had similar levels of fibrosis and number of scar forming cells but the livers of S100A9 knockout mice had fewer neutrophils, suggesting that neutrophils are not important for promoting liver fibrosis (scarring).
Alterations of circulating endogenous secretory RAGE and S100A9 levels indicating dysfunction of the AGE-RAGE axis in autism.
Role of S100A8 and S100A9 in Neutrophil recruitment in response to monosodium urate monohydrate in the air-pouch model of acute gouty arthritis.
Other amniotic fluid biomarkers relevant for preterm birth are S100A9 and insulin-like growth factor-binding protein 1.