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In its role as a highly expressed mediator of sterile inflammation in Kawasaki disease, S100A12 appears to activate human coronary artery endothelial cells in an IL-1beta-dependent manner. These data provide new mechanistic insights into the contributions of S100A12 and IL-1beta to disease pathogenesis.
High S100A12 expression due to DNA hypermethylation is associated with inflammation in cystic fibrosis.
In the active phase, S100A12 levels were significantly higher in patients with systemic juvenile idiopathic arthritis and familial Mediterranean fever compared with those with Blau syndrome.
the direct effects of S100A12 on human osteoclasts in vitro, were examined.
serum S100A12 levels were higher in juvenile idiopathic arthritis patients
S100A12 is differentially expressed in chronic rhinosinusitis subtypes and is significantly elevated in patients with chronic rhinosinusitis with nasal polyps and associated with chronic rhinosinusitis-specific disease severity
Used fluorescence and NMR spectroscopy to analyze the interaction of S100A9 with S100A12. Binary complex models of S100A9-S100A12 were developed using data obtained from 1H-15N HSQC NMR titrations and the HADDOCK program; overlaid the complex models of S100A9-S100A12 with the same orientation of S100A9 and the RAGE V-domain. Complex showed that S100A12 protein blocks the interaction between S100A9 and the RAGE V-domain.
S100A12 activates NLPR3 inflammasomes to induce MUC5AC production in airway epithelial cells. ATP induces MUC5AC production in a mechanistically similar mode to S100A12.
The results suggest that S100A12 does not participate in the induction of inflammation in dental pulp. However, RAGE can participate in the inflammation in the pulp of males.
S100A12 was a significant predictor of lung alveolar infiltration (OR 2.60, 95%CI 1.35-5.00, p = 0.004). These results suggest that S100A12 has the potential to assess the extent of alveolar infiltration in Pulmonary tuberculosis.
Results indicated that S100A12 could increase the expression of MMP-2, MMP-9, and vascular cell adhesion molecule 1 (VCAM-1) in HASMCs via activation of ERK1/2 signal pathway, which leads to injury of HASMCs.
S100A12 binds to CD36 in the low nanomolar range at the CD36 thrombospondin-1 binding site.
data on the antimicrobial activity of S100A12 have been reported. Proinflammatory role of S100A12 is supported by another newly found receptor, Toll-like receptor 4 (TLR4).
Report role of fecal S100A12 assay in the diagnosis and management of inflammatory bowel disease.
The aim of this mini-review was to outline the pleiotropic actions of S100A12 and to highlight the potential clinical importance of this protein in kidney and cardiovascular diseases. [review]
serum levels had significant, positive correlations with intensive care unit length of stay, 28-day mortality, and in-hospital mortality after major abdominal surgery
Elevated S100A8 and S100A9 gene expression in SP-infected HMEECs and in the middle ear mucosa of OM, minor co-localized with neutrophil markers suggests that middle ear epithelial cell secretion of S100A8 and S100A9 may play a role in the pathogenesis of recurrent and chronic OM
Expression of S100A8, S100A9 and S100A12 is modulated by eicosapentaenoic acid and docosahexaenoic acid during Inflammation in adipose tissue and mononuclear cells.
The binding interface between S100A12 and the V domain of RAGE has been identified and mapped.
S100A12 functions as a proinflammatory cytokine and activates dermal fibroblasts, causing dermal fibrosis
show that pS100A12 is expressed preferentially in immune organs/tissues, e.g., bone marrow, spleen, and inguinal lymph nodes.
the S100A12 level in milk may serve as a diagnostic tool for subclinical mastitis in cows without obvious clinical signs.
The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein is proposed to be involved in specific calcium-dependent signal transduction pathways and its regulatory effect on cytoskeletal components may modulate various neutrophil activities.
, S100 calcium-binding protein A12 (calgranulin C)
, calcium-binding protein in amniotic fluid 1
, calgranulin C
, extracellular newly identified RAGE-binding protein
, migration inhibitory factor-related protein 6
, neutrophil S100 protein
, protein S100-A12
, S100 calcium-binding protein A12
, RAGE-binding protein
, cornea-associated antigen