Journal articles on the topic 'S100A12'
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1
Broome, Ann-Marie, David Ryan, and Richard L. Eckert. "S100 Protein Subcellular Localization During Epidermal Differentiation and Psoriasis." Journal of Histochemistry & Cytochemistry 51, no. 5 (May 2003): 675–85. http://dx.doi.org/10.1177/002215540305100513.
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S100 proteins are calcium-activated signaling proteins that interact with target proteins to modulate biological processes. Our present studies compare the level of expression, and cellular localization of S100A7, S100A8, S100A9, S100A10, and S100A11 in normal and psoriatic epidermis. S100A7 and S100A11 are present in the basal and spinous layers in normal epidermis. These proteins appear in the nucleus and cytoplasm in basal cells but are associated with the plasma membrane in spinous cells. S100A10 is present in basal and spinous cells, in the cytoplasm, and is associated with the plasma membrane. S100A8 and S100A9 are absent or are expressed at minimal levels in normal epidermis. In involved psoriatic tissue, S100A10 and S100A11 levels remain unchanged, whereas, S100A7, S100A8, and S100A9 are markedly overexpressed. The pattern of expression and subcellular localization of S100A7 is similar in normal and psoriatic tissue. S100A8 and S100A9 are strongly expressed in the basal and spinous layers in psoriasis-involved tissue. In addition, we demonstrate that S100A7, S100A10, and S100A11 are incorporated into detergent and reducing agent-resistant multimers, suggesting that they are in vivo trans-glutaminase substrates. S100A8 and S100A9 did not form these larger complexes. These results indicate that S100 proteins localize to the plasma membrane in differentiated keratinocytes, suggesting a role in regulating calcium-dependent, membrane-associated events. These studies also indicate, as reported previously, that S100A7, S100A8, and S100A9 expression is markedly altered in psoriasis, suggesting a role for these proteins in disease pathogenesis.
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McLachlan, Julia L., Alastair J. Sloan, Anthony J. Smith, Gabriel Landini, and Paul R. Cooper. "S100 and Cytokine Expression in Caries." Infection and Immunity 72, no. 7 (July 2004): 4102–8. http://dx.doi.org/10.1128/iai.72.7.4102-4108.2004.
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ABSTRACT The molecular immune response of the pulpal tissue during chronic carious infection is poorly characterized. Our objective was to examine the expression of potential molecular mediators of pulpal inflammation, correlate their levels with disease severity, and determine the cellular localization of key molecules. Results indicated that there was significantly increased transcriptional activity in carious compared to healthy pulp, and the increase correlated positively with disease severity. Semiquantitative reverse transcriptase PCR analysis in 10 carious and 10 healthy pulpal tissue samples of the S100 family members S100A8, S100A9, S100A10, S100A12, and S100A13; the cytokines tumor necrosis factor alpha (TNF-α), interleukin-1β (IL-1β), IL-8, IL-6, and epithelial cell-derived neutrophil attractant 78 (ENA-78); and the structural protein collagen-1α indicated that all genes tested, with the exception of S100A10, were more abundantly expressed in carious teeth. In addition, we found that the closer the carious lesion front was to the pulpal chamber the higher the expression was for all genes except S100A10. Multiple-regression analysis identified a significant positive correlation between the expression levels of S100A8 and IL-1β, ENA-78, and IL-6 and between collagen-1α and S100A8, TNF-α, IL-1β, IL-8, IL-6, and ENA-78. Immunohistochemical studies in carious pulpal tissue indicated that S100A8 and the S100A8/S100A9 complex were predominantly expressed by infiltrating neutrophils. Gene expression analyses in immune system cells supported these findings and indicated that bacterial activation of neutrophils caused upregulation of S100A8, S100A9, and S100A13. This study highlights the complex nature of the molecular immune response that occurs during carious infection.
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Leach, Steven T., Hazel M. Mitchell, Carolyn L. Geczy, Philip M. Sherman, and Andrew S. Day. "S100 Calgranulin Proteins S100A8, S100A9 and S100A12 are Expressed in the Inflamed Gastric Mucosa ofHelicobacter Pylori-Infected Children." Canadian Journal of Gastroenterology 22, no. 5 (2008): 461–64. http://dx.doi.org/10.1155/2008/308942.
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The expression of the inflammatory S100 calgranulin proteins (S100A8, S100A9 and S100A12) in normal andHelicobacter pylori-infected gastric mucosa of children were examined. S100A8, S100A9 and S100A12, which were virtually absent in normal gastric mucosa, were highly expressed inH pylori-infected mucosa. This expression correlated with the severity of gastritis (r=0.9422, P<0.05). S100 calgranulins may be involved in bacterial-induced gastritis and may limit bacterial growth.
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Tardif, Mélanie R., Julie Andrea Chapeton-Montes, Alma Posvandzic, Nathalie Pagé, Caroline Gilbert, and Philippe A. Tessier. "Secretion of S100A8, S100A9, and S100A12 by Neutrophils Involves Reactive Oxygen Species and Potassium Efflux." Journal of Immunology Research 2015 (2015): 1–16. http://dx.doi.org/10.1155/2015/296149.
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S100A8/A9 (calprotectin) and S100A12 proinflammatory mediators are found at inflammatory sites and in the serum of patients with inflammatory or autoimmune diseases. These cytoplasmic proteins are secreted by neutrophils at sites of inflammation via alternative secretion pathways of which little is known. This study examined the nature of the stimuli leading to S100A8/A9 and S100A12 secretion as well as the mechanism involved in this alternative secretion pathway. Chemotactic agents, cytokines, and particulate molecules were used to stimulate human neutrophils. MSU crystals, PMA, and H2O2induced the release of S100A8, S100A9, and S100A12 homodimers, as well as S100A8/A9 heterodimer. High concentrations of S100A8/A9 and S100A12 were secreted in response to nanoparticles like MSU, silica, TiO2, fullerene, and single-wall carbon nanotubes as well as in response to microbe-derived molecules, such as zymosan or HKCA. However, neutrophils exposed to the chemotactic factors fMLP failed to secrete S100A8/A9 or S100A12. Secretion of S100A8/A9 was dependent on the production of reactive oxygen species and required K+exchanges through the ATP-sensitive K+channel. Altogether, these findings suggest that S100A12 and S100A8/A9 are secreted independently either via distinct mechanisms of secretion or following the activation of different signal transduction pathways.
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SHISHIBORI, Tsuyoshi, Yuhta OYAMA, Osamu MATSUSHITA, Kayoko YAMASHITA, Hiromi FURUICHI, Akinobu OKABE, Hajime MAETA, Yuiro HATA, and Ryoji KOBAYASHI. "Three distinct anti-allergic drugs, amlexanox, cromolyn and tranilast, bind to S100A12 and S100A13 of the S100 protein family." Biochemical Journal 338, no. 3 (March 8, 1999): 583–89. http://dx.doi.org/10.1042/bj3380583.
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To investigate the roles of calcium-binding proteins in degranulation, we used three anti-allergic drugs, amlexanox, cromolyn and tranilast, which inhibit IgE-mediated degranulation of mast cells, as molecular probes in affinity chromatography. All of these drugs, which have different structures but similar function, scarcely bound to calmodulin in bovine lung extract, but bound to the same kinds of calcium-binding proteins, such as the 10-kDa proteins isolated in this study, calcyphosine and annexins I–V. The 10-kDa proteins obtained on three drug-coupled resins and on phenyl-Sepharose were analysed by reversed-phase HPLC. It was found that two characteristic 10-kDa proteins, one polar and one less polar, were bound with all three drugs, although S100A2 (S100L), of the S100 family, was bound with phenyl-Sepharose. The cDNA and deduced amino acid sequence proved our major polar protein to be identical with the calcium-binding protein in bovine amniotic fluid (CAAF1, S100A12). The cDNA and deduced amino acid sequence of the less-polar protein shared 95% homology with human and mouse S100A13. In addition, it was demonstrated that the native S100A12 and recombinant S100A12 and S100A13 bind to immobilized amlexanox. On the basis of these findings, we speculate that the three anti-allergic drugs might inhibit degranulation by binding with S100A12 and S100A13.
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BASIKA, TATIANA, NATALIA MUÑOZ, CECILIA CASARAVILLA, FLORENCIA IRIGOÍN, CARLOS BATTHYÁNY, MARIANA BONILLA, GUSTAVO SALINAS, et al. "Phagocyte-specific S100 proteins in the local response to theEchinococcus granulosuslarva." Parasitology 139, no. 2 (January 5, 2012): 271–83. http://dx.doi.org/10.1017/s003118201100179x.
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SUMMARYInfection by larvalEchinococcus granulosusis usually characterized by tight inflammatory control. However, various degrees of chronic granulomatous inflammation are also observed, reaching a high point in infection of cattle by the most prevalent parasite strain worldwide, which is not well adapted to this host species. In this context, epithelioid and multinucleated giant macrophages surround the parasite, and the secreted products of these cells often associate with the larval wall. The phagocyte-specific S100 proteins, S100A8, S100A9 and S100A12, are important non-conventionally secreted amplifiers of inflammatory responses. We have analysed by proteomics and immunohistochemistry the presence of these proteins at theE. granulosuslarva-host interface. We found that, in the context of inflammatory control as observed in human infections, the S100 proteins are not abundant, but S100A9 and S100A8 can be expressed by eosinophils distal to the parasite. In the granulomatous inflammation context as observed in cattle infections, we found that S100A12 is one of the most abundant host-derived, parasite-associated proteins, while S100A9 and S100A8 are not present at similarly high levels. As expected, S100A12 derives mostly from the epithelioid and multinucleated giant cells. S100A12, as well as cathepsin K and matrix metalloproteinase-9, also expressed byE. granulosus-elicited epithelioid cells, are connected to the Th17 arm of immunity, which may therefore be involved in this granulomatous response.
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Zeng, Meng-Lu, Xian-Jin Zhu, Jin Liu, Peng-Chong Shi, Yan-Li Kang, Zhen Lin, and Ying-Ping Cao. "An Integrated Bioinformatic Analysis of the S100 Gene Family for the Prognosis of Colorectal Cancer." BioMed Research International 2020 (November 26, 2020): 1–15. http://dx.doi.org/10.1155/2020/4746929.
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Background. S100 family genes exclusively encode at least 20 calcium-binding proteins, which possess a wide spectrum of intracellular and extracellular functions in vertebrates. Multiple lines of evidences suggest that dysregulated S100 proteins are associated with human malignancies including colorectal cancer (CRC). However, the diverse expression patterns and prognostic roles of distinct S100 genes in CRC have not been fully elucidated. Methods. In the current study, we analyzed the mRNA expression levels of S100 family genes and proteins and their associations with the survival of CRC patients using the Oncomine analysis and GEPIA databases. Expressions and mutations of S100 family genes were analyzed using the cBioPortal, and protein-protein interaction (PPI) networks of S100 proteins and their mutation-related coexpressed genes were analyzed using STRING and Cytoscape. Results. We observed that the mRNA expression levels of S100A2, S100A3, S100A9, S100A11, and S100P were higher and the level of S100B was lower in CRC tissues than those in normal colon mucosa. A high S100A10 levels was associated with advanced-stage CRC. Results from GEPIA database showed that highly expressed S100A1 was correlated with worse overall survival (OS) and disease-free survival (DFS) and that overexpressions of S100A2 and S100A11 were associated with poor DFS of CRC, indicating that S100A1, S100A2, and S100A11 are potential prognostic markers. Unexpectedly, most of S100 family genes showed no significant prognostic values in CRC. Conclusions. Our findings, though still need to be ascertained, offer novel insights into the prognostic implications of the S100 family in CRC and will inspire more clinical trials to explore potential S100-targeted inhibitors for the treatment of CRC.
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Thames, Brittany E., James W. Barr, Jan S. Suchodolski, Jörg M. Steiner, and Romy M. Heilmann. "Prospective evaluation of S100A12 and S100A8/A9 (calprotectin) in dogs with sepsis or the systemic inflammatory response syndrome." Journal of Veterinary Diagnostic Investigation 31, no. 4 (June 6, 2019): 645–51. http://dx.doi.org/10.1177/1040638719856655.
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Pattern recognition receptors (e.g., S100A12 or S100A8/A9) hold promise as inflammatory biomarkers. We prospectively determined and compared serum S100A12 and S100A8/A9 concentrations in dogs with sepsis ( n = 11) or systemic inflammatory response syndrome (SIRS; n = 8) over a 3-d period with each other, healthy controls ( n = 50), and other clinical and clinicopathologic variables. Serum S100A12 and S100A8/A9 concentrations were significantly higher in dogs with sepsis or SIRS (all p < 0.05) at the time of hospital admission (day 1) compared to healthy controls, with no differences between patient groups. However, septic dogs had significantly lower serum S100A12 concentrations on day 2 and day 3 (both p < 0.05) compared to dogs with SIRS. Likewise, dogs with sepsis had significantly lower S100A8/A9 concentrations on day 2 ( p < 0.05). Neither serum S100A12 nor S100A8/A9 concentrations were associated with survival to discharge. Our results suggest a differential expression of the S100/calgranulins between dogs with sepsis and those with SIRS. Serum S100A12 or S100A8/A9 concentration at the time of hospital admission did not differentiate dogs with sepsis from those with SIRS, but the trend of S100/calgranulin concentrations during the following 24–48 h may be a useful surrogate marker for differentiating sepsis from SIRS.
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Peterova, Eva, Jan Bures, Paula Moravkova, and Darina Kohoutova. "Tissue mRNA for S100A4, S100A6, S100A8, S100A9, S100A11 and S100P Proteins in Colorectal Neoplasia: A Pilot Study." Molecules 26, no. 2 (January 14, 2021): 402. http://dx.doi.org/10.3390/molecules26020402.
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S100 proteins are involved in the pathogenesis of sporadic colorectal carcinoma through different mechanisms. The aim of our study was to assess tissue mRNA encoding S100 proteins in patients with non-advanced and advanced colorectal adenoma. Mucosal biopsies were taken from the caecum, transverse colon and rectum during diagnostic and/or therapeutic colonoscopy. Another biopsy was obtained from adenomatous tissue in the advanced adenoma group. The tissue mRNA for each S100 protein (S100A4, S100A6, S100A8, S100A9, S100A11 and S100P) was investigated. Eighteen biopsies were obtained from the healthy mucosa in controls and the non-advanced adenoma group (six individuals in each group) and thirty biopsies in the advanced adenoma group (ten patients). Nine biopsies were obtained from advanced adenoma tissue (9/10 patients). Significant differences in mRNA investigated in the healthy mucosa were identified between (1) controls and the advanced adenoma group for S100A6 (p = 0.012), (2) controls and the non-advanced adenoma group for S100A8 (p = 0.033) and (3) controls and the advanced adenoma group for S100A11 (p = 0.005). In the advanced adenoma group, differences between the healthy mucosa and adenomatous tissue were found in S100A6 (p = 0.002), S100A8 (p = 0.002), S100A9 (p = 0.021) and S100A11 (p = 0.029). Abnormal mRNA expression for different S100 proteins was identified in the pathological adenomatous tissue as well as in the morphologically normal large intestinal mucosa.
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Åberg, Anna-Maja, Sofia Halin Bergström, Elin Thysell, Lee-Ann Tjon-Kon-Fat, Jonas A. Nilsson, Anders Widmark, Camilla Thellenberg-Karlsson, Anders Bergh, Pernilla Wikström, and Marie Lundholm. "High Monocyte Count and Expression of S100A9 and S100A12 in Peripheral Blood Mononuclear Cells Are Associated with Poor Outcome in Patients with Metastatic Prostate Cancer." Cancers 13, no. 10 (May 17, 2021): 2424. http://dx.doi.org/10.3390/cancers13102424.
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Increasing evidence indicates calcium-binding S100 protein involvement in inflammation and tumor progression. In this prospective study, we evaluated the mRNA levels of two members of this family, S100A9 and S100A12, in peripheral blood mononuclear cells (PBMCs) in a cohort of 121 prostate cancer patients using RT-PCR. Furthermore, monocyte count was determined by flow cytometry. By stratifying patients into different risk groups, according to TNM stage, Gleason score and PSA concentration at diagnosis, expression of S100A9 and S100A12 was found to be significantly higher in patients with metastases compared to patients without clinically detectable metastases. In line with this, we observed that the protein levels of S100A9 and S100A12 in plasma were higher in patients with advanced disease. Importantly, in patients with metastases at diagnosis, high monocyte count and high levels of S100A9 and S100A12 were significantly associated with short progression free survival (PFS) after androgen deprivation therapy (ADT). High monocyte count and S100A9 levels were also associated with short cancer-specific survival, with monocyte count providing independent prognostic information. These findings indicate that circulating levels of monocytes, as well as S100A9 and S100A12, could be biomarkers for metastatic prostate cancer associated with particularly poor prognosis.
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de Seny, Dominique, Marianne Fillet, Clio Ribbens, Raphaël Marée, Marie-Alice Meuwis, Laurence Lutteri, Jean-Paul Chapelle, et al. "Monomeric Calgranulins Measured by SELDI-TOF Mass Spectrometry and Calprotectin Measured by ELISA as Biomarkers in Arthritis." Clinical Chemistry 54, no. 6 (June 1, 2008): 1066–75. http://dx.doi.org/10.1373/clinchem.2007.099549.
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AbstractBackground: SELDI-TOF mass spectrometry (MS) is a high-throughput proteomic approach with potential for identifying novel forms of serum biomarkers of arthritis.Methods: We used SELDI-TOF MS to analyze serum samples from patients with various forms of inflammatory arthritis. Several protein profiles were collected on different Bio-Rad Laboratories ProteinChip arrays (CM10 and IMAC-Cu2+) and were evaluated statistically to select potential biomarkers.Results: SELDI-TOF MS analyses identified several calgranulin proteins [S100A8 (calgranulin A), S100A9 (calgranulin B), S100A9*, and S100A12 (calgranulin C)], serum amyloid A (SAA), SAA des-Arg (SAA-R), and SAA des-Arg/des-Ser (SAA-RS) as biomarkers and confirmed the results with other techniques, such as western blotting, immunoprecipitation, and nano-LC-MS/MS. The S100 proteins were all able to significantly differentiate samples from patients with rheumatoid arthritis (RA), psoriatic arthritis (PsA), and ankylosing spondylitis (AS) from those of patients with inflammatory bowel diseases used as an inflammatory control (IC) group, whereas the SAA, SAA-R, and SAA-RS proteins were not, with the exception of AS. The 4 S100 proteins were coproduced in all of the pathologies and were significantly correlated with the plasma calprotectin concentration; however, these S100 proteins were correlated with the SAA peak intensities only in the RA and IC patient groups. In RA, these S100 proteins (except for S100A12) were significantly correlated with the serum concentrations of C-reactive protein, matrix metalloproteinase 3, and anti–cyclic citrullinated peptide and with the Disease Activity Score (DAS28).Conclusions: The SELDI-TOF MS technology is a powerful approach for analyzing the status of monomeric, truncated, or posttranslationally modified forms of arthritis biomarkers, such as the S100A8, S100A9, S100A12, and SAA proteins. The fact that the SELDI-TOF MS data were correlated with results obtained with the classic calprotectin ELISA test supports the reliability of this new proteomic technique.
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Haley, Kathryn P., Alberto G. Delgado, M. Blanca Piazuelo, Brittany L. Mortensen, Pelayo Correa, Steven M. Damo, Walter J. Chazin, Eric P. Skaar, and Jennifer A. Gaddy. "The Human Antimicrobial Protein Calgranulin C Participates in Control of Helicobacter pylori Growth and Regulation of Virulence." Infection and Immunity 83, no. 7 (May 11, 2015): 2944–56. http://dx.doi.org/10.1128/iai.00544-15.
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During infectious processes, antimicrobial proteins are produced by both epithelial cells and innate immune cells. Some of these antimicrobial molecules function by targeting transition metals and sequestering these metals in a process referred to as “nutritional immunity.” This chelation strategy ultimately starves invading pathogens, limiting their growth within the vertebrate host. Recent evidence suggests that these metal-binding antimicrobial molecules have the capacity to affect bacterial virulence, including toxin secretion systems. Our previous work showed that the S100A8/S100A9 heterodimer (calprotectin, or calgranulin A/B) binds zinc and represses the elaboration of theH. pyloricagtype IV secretion system (T4SS). However, there are several other S100 proteins that are produced in response to infection. We hypothesized that the zinc-binding protein S100A12 (calgranulin C) is induced in response toH. pyloriinfection and also plays a role in controllingH. pylorigrowth and virulence. To test this, we analyzed gastric biopsy specimens fromH. pylori-positive and -negative patients for S100A12 expression. These assays showed that S100A12 is induced in response toH. pyloriinfection and inhibits bacterial growth and viabilityin vitroby binding nutrient zinc. Furthermore, the data establish that the zinc-binding activity of the S100A12 protein represses the activity of thecagT4SS, as evidenced by the gastric cell “hummingbird” phenotype, interleukin 8 (IL-8) secretion, and CagA translocation assays. In addition, high-resolution field emission gun scanning electron microscopy (FEG-SEM) was used to demonstrate that S100A12 represses biogenesis of thecagT4SS. Together with our previous work, these data reveal that multiple S100 proteins can repress the elaboration of an oncogenic bacterial surface organelle.
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Tydén, H., C. Lood, B. Gullstrand, A. Jönsen, F. Ivars, T. Leanderson, and A. A. Bengtsson. "Pro-inflammatory S100 proteins are associated with glomerulonephritis and anti-dsDNA antibodies in systemic lupus erythematosus." Lupus 26, no. 2 (July 19, 2016): 139–49. http://dx.doi.org/10.1177/0961203316655208.
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Objectives Systemic lupus erythematosus (SLE) is associated with elevated levels of S100A8/A9, pro-inflammatory proteins mainly secreted by activated polymorphonuclear neutrophils (PMNs). The underlying mechanisms for increased S100A8/A9 levels and their relation to the clinical phenotype have not been carefully investigated. We assessed S100A8/A9 and S100A12 levels in SLE patient sera in relation to disease activity, clinical phenotype, presence of anti-dsDNA antibodies and ability to promote phagocytosis of necrotic cells (NCs) by PMNs. Methods Serum levels of S100A8/A9 and S100A12 were measured by ELISA in paired samples of 100 SLE patients at time points of higher and lower disease activity. Serum-mediated phagocytosis of NCs by PMNs was analysed by flow cytometry. Clinical data were recorded at time points of blood sampling. Results Serum levels of S100A8/A9 and S100A12 were increased in SLE patients with high disease activity compared to paired samples at low disease activity ( p = 0.01 and p = 0.008, respectively). Elevated levels of S100A8/A9 were particularly seen in patients with anti-dsDNA antibodies ( p = 0.01) and glomerulonephritis before treatment ( p = 0.02). Immunosuppressive therapy was associated with a reduction of S100A8/A9 serum levels ( p = 0.002). The ability of serum to support phagocytosis of NCs by PMNs was related to increased S100A8/A9 levels ( p = 0.01). Conclusions Elevated serum levels of S100A8/A9 may be used to monitor disease activity and response to treatment in SLE patients, especially in patients with glomerulonephritis. S100A12 may be a marker of disease activity in SLE. Increased S100A8/A9 levels may reflect immune-pathological processes involving phagocytosis of immune complexes by PMNs.
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McMorran, Brendan J., Severine A. Ouvry Patat, John B. Carlin, Keith Grimwood, Alun Jones, David S. Armstrong, John C. Galati, et al. "Novel Neutrophil-Derived Proteins in Bronchoalveolar Lavage Fluid Indicate an Exaggerated Inflammatory Response in Pediatric Cystic Fibrosis Patients." Clinical Chemistry 53, no. 10 (October 1, 2007): 1782–91. http://dx.doi.org/10.1373/clinchem.2007.087650.
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Abstract Background: Airway inflammation in cystic fibrosis (CF) is exaggerated and characterized by neutrophil-mediated tissue destruction, but its genesis and mechanisms remain poorly understood. To further define the pulmonary inflammatory response, we conducted a proteome-based screen of bronchoalveolar lavage fluid (BALF) collected from young children with and without CF experiencing endobronchial infection. Methods: We collected BALF samples from 45 children younger than 5 years and grouped them according to the presence of respiratory pathogens: ≥1 × 105 colony-forming units (CFU)/mL BALF (18 and 12 samples with and without CF, respectively) and <1 × 105 CFU/mL (23 and 15 samples). BALF proteins were analyzed with SELDI-TOF mass spectrometry (MS) and H4 ProteinChips®. Proteins were identified and characterized using trypsin digestion, tandem MS, Fourier transform ion cyclotron resonance MS, immunoblotting, and ELISA. Results: The SELDI-TOF MS BALF profiles contained 53 unique, reliably detected proteins. Peak intensities of 24 proteins differed significantly between the CF and non-CF samples. They included the neutrophil proteins, α-defensin 1 and 2, S100A8, S100A9, and S100A12, as well as novel forms of S100A8 and S100A12 with equivalent C-terminal deletions. Peak intensities of these neutrophil proteins and immunoreactive concentrations of selected examples were significantly higher in CF than non-CF samples. Conclusions: Small neutrophil-derived BALF proteins, including novel C-terminal truncated forms of S100A proteins, are easily detected with SELDI-TOF MS. Concentrations of these molecules are abnormally high in early CF lung disease. The data provide new insights into CF lung disease and identify novel proteins strongly associated with CF airway inflammation.
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Reinhardt, Katharina, Dirk Föll, Thomas Vogl, Falko Fend, Christian Gille, Tobias Feuchtinger, Peter Lang, Rupert Handgretinger, Wolfgang A. Bethge, and Ursula Holzer. "Involvement Of S100 Proteins and Hsp90 In The Pathogenesis Of Graft-Versus-Host Disease After Allogeneic Hematopoetic Cell Transplantation." Blood 122, no. 21 (November 15, 2013): 2058. http://dx.doi.org/10.1182/blood.v122.21.2058.2058.
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Abstract Graft-versus-host disease (GvHD) is one of the major live threatening complications of allogeneic hematopoietic cell transplantation (HCT). The pathophysiology of GvHD is complex and not fully understood yet. However, it has been shown that Th17 cells play an important role in the pathogenesis of acute and chronic GvHD. Therefore, the development of Th17 cells in patients with GvHD was further investigated in the present study. The influence of monocytes and their activation with proinflammatory S100 proteins and 90 kDa heat shock protein (Hsp90) on the induction of Th17 cells was examined. Furthermore, the suitability of S100 proteins as diagnostic markers for intestinal GvHD was analyzed. In the present study, it could be demonstrated that monocytes from patients with acute and chronic skin or intestinal GvHD grade I-IV (n=13) induced significant higher percentages of Th17 cells compared to monocytes from healthy donors (n=32) or patients without GvHD at several timepoints after HCT (n=21) (p<0.001). It is known that faecal S100A12 is a potential non-invasive marker for inflammatory bowel disease. Therefore, the concentration of S100A12 in the stool of patients with and without intestinal GvHD was determined. The obtained results showed that the concentration of S100A12 was significantly increased in the stool of patients with intestinal GvHD (n=7) compared to patients without GvHD (n=16) (p<0.05). Furthermore, S100A9 and S100A12 could be detected immunohistochemically in intestinal tissue from patients with intestinal GvHD indicating that S100 proteins of the calgranulin subfamily could be potential diagnostic markers for intestinal GvHD. Additionally, the effect of S100A8, S100A9 and the heterodimer S100A8/9 on the induction of Th17 cells was investigated. Monocytes from healthy donors stimulated with these S100 proteins induced significant higher percentages of Th17 cells compared to unstimulated monocytes (n=7) (p<0.05). Furthermore, the influence of the 90 kDa heat shock protein (Hsp90) in monocytes on the induction of Th17 cells was examined. Therefore, Hsp90 was inhibited by the geldanamycin analog 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG) in monocytes from patients with GvHD and the effect on the induction of Th17 cells was analyzed. It could be shown that inhibition of Hsp90 resulted in a significant decrease in the percentage of induced Th17 cells (n=3) (p<0.001). Further results indicated that stimulation of monocytes with S100A8, S100A9 and S100A8/9 induces an elevation in Hsp90 expression levels. In conclusion, our findings suggest that monocytes may play a major role in the pathogenesis of GvHD by triggering the induction of Th17 cells. Monocyte-induced Th17 cell development could further be enhanced by stimulation of monocytes with purified S100 proteins. The chaperone Hsp90 could be an important regulator in monocyte-induced development of Th17 cells and therefore be a therapeutic target for GvHD. Furthermore, S100 proteins might be novel diagnostic markers in intestinal tissue and potential non-invasive markers in the stool for intestinal GvHD. Disclosures: No relevant conflicts of interest to declare.
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Xu, Su-Ling, Qiong-Yan Zhou, Wei Lin, Xiao-Xia Zhu, Meng-Xia Ying, Lei Shi, and Bing-Jiang Lin. "Increased plasma levels of S100A8, S100A9, and S100A12 in chronic spontaneous urticaria." Indian Journal of Dermatology 64, no. 6 (2019): 441. http://dx.doi.org/10.4103/ijd.ijd_375_18.
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Hong, Wenzhou, Pawjai Khampang, Tina L. Samuels, Joseph E. Kerschner, Ke Yan, and Pippa Simpson. "Expression of calcium-binding proteins S100A8, S100A9 and S100A12 in otitis media." International Journal of Pediatric Otorhinolaryngology 101 (October 2017): 30–36. http://dx.doi.org/10.1016/j.ijporl.2017.07.025.
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Ruperto, N., G. Schulert, A. Sproles, S. Thornton, G. Vega Cornejo, J. Anton, R. Cuttica, et al. "POS0076 S100A8/A9 AND S100A12 AS POTENTIAL PREDICTIVE BIOMARKERS OF ABATACEPT RESPONSE IN POLYARTICULAR JUVENILE IDIOPATHIC ARTHRITIS." Annals of the Rheumatic Diseases 80, Suppl 1 (May 19, 2021): 245–46. http://dx.doi.org/10.1136/annrheumdis-2021-eular.1081.
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Background:The calcium-binding proteins S100A8/A9 (calprotectin) and S100A12 (extracellular newly identified receptor for advanced glycation end-products binding protein [EN-RAGE]) are involved in multiple signalling pathways to mediate inflammation, can be secreted by activated monocytes/macrophages and exhibit cytokine-like extracellular functions. Circulating levels of these proteins have been associated with disease and clinical responses in systemic juvenile idiopathic arthritis (sJIA), including treatment response.1 Studies suggest that serum S100A8/A9 and S100A12, which are released at inflammation sites, are more specific biomarkers of local inflammation (e.g. in the synovium) than systemic biomarkers such as CRP and ESR.2,3Objectives:To investigate if baseline S100A8/A9 and S100A12 predict clinical response to abatacept treatment in polyarticular JIA (pJIA), and to assess whether changes from baseline in S100A8/A9 or S100A12 can be better prognostic markers for response to abatacept treatment than CRP in pJIA.Methods:Data are from a phase III trial of SC abatacept for the treatment of pJIA (NCT01844518).4 This 24-month, single-arm, open-label, international, multicentre, two-part study included male and female patients with pJIA aged 2–17 years. This analysis examined the correlation between biomarkers (S100A8/A9, S100A12 and high-sensitivity CRP [hsCRP]) and disease activity (measured using Juvenile Arthritis Disease Activity Score [JADAS]) at baseline, baseline biomarker values as predictors of future treatment response (ACR and JADAS endpoints), and the correlation between change from baseline in biomarker values and treatment response at Day 113.Results:Of 219 total patients, 158 (72%) had S100A8/A9 values and 155 (71%) had S100A12 values at baseline. Median S100A8/A9 and S100A12 values were 3295 ng/mL (normal range, 716–3004 ng/mL) and 176 ng/mL (normal range, 32–385 ng/mL), respectively. S100A8/A9, S100A12 and hsCRP (median 0.20 mg/dL; normal ≤0.6 mg/dL) had a low-to-moderate but significant association with disease activity at baseline; coefficients for associations between JADAS71-CRP low disease activity (LDA) and the biomarkers S100A8/A9, S100A12 and hsCRP were 0.23 (p=0.0038), 0.16 (p=0.0448) and 0.26 (p=0.0001), respectively. Baseline S100A8/A9 level above the median was associated with lower odds of ACR100 at Day 113 (p=0.0052). Figure 1 shows the associations of baseline biomarker values with Day 113 ACR and JADAS scores in the overall population. Baseline S100A8/A9 or S100A12 did not significantly influence ACR50 or ACR70 responses at Day 113, but high baseline values were associated with reduced odds of ACR90 (p=0.01), ACR100 (p=0.005), ACR-inactive disease (ID) (p=0.0001), and JADAS71-CRP (LDA) (p=0.02). By Day 477, elevated baseline S100A12 was still significantly associated with lower odds of ACR100 overall (0.467; p=0.0248) but baseline S100A8/A9 was not; at Day 645, neither was significantly associated with ACR100 response. At Day 113, changes from baseline in S100A8/A9 and S100A12 were correlated with ACR100 (coefficients of 0.22 [p=0.0082] and 0.26 [p=0.0015], respectively) and with ACR-ID (0.22 [p=0.0067] and 0.26 [p=0.0014], respectively); change in hsCRP was not significantly correlated with disease response.Conclusion:S100A8/A9 and S100A12 may serve as prognostic biomarkers to predict response to abatacept treatment at Day 113. Changes from baseline S100A8/A9 and S100A12 levels were more highly correlated with efficacy outcomes including ACR100 and ACR-ID at Day 113 compared with hsCRP.References:[1]Aljaberi N, et al. Pediatr Rheumatol Online J 2020;18:7.[2]Hammer H, et al. Arthritis Res Ther 2011;13:R178.[3]Nordal HH, et al. BMC Musculoskelet Disord 2014;15:335.[4]Brunner H, et al. Arthritis Rheumatol 2018;70:1144–1154.Acknowledgements:Professional medical writing and editorial assistance was provided by Rob Coover, MPH, at Caudex and was funded by Bristol Myers Squibb.Disclosure of Interests:Nicolino Ruperto Speakers bureau: NR has received honoraria for consultancies or speaker bureaus (< 10.000 USD each) from the following pharmaceutical companies in the past 3 years: Ablynx, Astrazeneca-Medimmune, Bayer, Biogen, Boehringer, Bristol Myers Squibb, Celgene, Eli Lilly, EMD Serono, GlaxoSmithKline, Hoffmann-La Roche, Janssen, Merck, Novartis, Pfizer, R-Pharma, Sinergie, Sobi and UCB, Consultant of: NR has received honoraria for consultancies or speaker bureaus (< 10.000 USD each) from the following pharmaceutical companies in the past 3 years: Ablynx, Astrazeneca-Medimmune, Bayer, Biogen, Boehringer, Bristol Myers Squibb, Celgene, Eli Lilly, EMD Serono, GlaxoSmithKline, Hoffmann-La Roche, Janssen, Merck, Novartis, Pfizer, R-Pharma, Sinergie, Sobi and UCB, Grant/research support from: The IRCCS Istituto Giannina Gaslini (IGG), where NR works as full-time public employee has received contributions (>10.000 USD each) from the following industries in the last 3 years: Bristol Myers Squibb, Eli Lilly, F Hoffmann-La Roche, GlaxoSmithKline, Janssen, Novartis, Pfizer, Sobi. This funding has been reinvested for the research activities of the hospital in a fully independent manner, without any commitment with third parties., Grant Schulert Speakers bureau: Novartis, Consultant of: SOBI, Alyssa Sproles: None declared, Sherry Thornton: None declared, Gabriel Vega Cornejo Speakers bureau: AbbVie, Grant/research support from: Bristol Myers Squibb, Eli Lilly, Janssen, Parexel, Sanofi, Jordi Anton Speakers bureau: AbbVie, Gebro, GlaxoSmithKline, Novartis, Pfizer, Roche, Sobi, Consultant of: AbbVie, Gebro, GlaxoSmithKline, Novartis, Pfizer, Roche, Sobi, Grant/research support from: AbbVie, Amgen, Gebro, GlaxoSmithKline, Lilly, Novartis, Novimmune, Pfizer, Roche, Sanofi, Sobi, Ruben Cuttica Speakers bureau: AbbVie, Bristol Myers Squibb, GlaxoSmithKline, Lilly, Novartis, Pfizer, Roche, UCB, Paid instructor for: AbbVie, Novartis, Pfizer, Roche, Consultant of: AbbVie, Bristol Myers Squibb, GlaxoSmithKline, Lilly, Novartis, Pfizer, Roche, UCB, Michael Henrickson: None declared, Ivan Foeldvari Consultant of: Bristol Myers Squibb, Gilead, Hexal, MEDAC, Novartis, Pfizer, Sanofi, Daniel Kingsbury Consultant of: Pfizer, Margarita Askelson Consultant of: Currently working for Syneos Health providing services to Bristol Myers Squibb, Jinqi Liu Shareholder of: Bristol Myers Squibb, Employee of: Bristol Myers Squibb, Sumanta Mukherjee Shareholder of: Bristol Myers Squibb, GlaxoSmithKline, Employee of: Bristol Myers Squibb, GlaxoSmithKline, Robert Wong Shareholder of: Bristol Myers Squibb, Employee of: Bristol Myers Squibb, Daniel J Lovell Speakers bureau: Genentech, Wyeth Pharm, Consultant of: Abbott, Amgen, AstraZeneca, Boehringer Ingelheim, Celgene, GlaxoSmithKline, Hoffman-La Roche, Novartis, Pfizer, Regeneron, Takeda, UBC, Wyeth Pharma, Xoma, Alberto Martini Speakers bureau: AbbVie, Novartis, Consultant of: AbbVie, Eli Lilly, EMD Serono, Idorsia, Janssen, Novartis, Pfizer, Alexei Grom Consultant of: AB2Bio, Novartis, Sobi (NovImmune), Grant/research support from: AB2Bio, Novartis, Sobi (NovImmune), Hermine Brunner Speakers bureau: GlaxoSmithKline, Novartis, Pfizer, Roche, Paid instructor for: Novartis, Pfizer (funds go to CCHMC/employer), Consultant of: Boehringer Ingelheim, Bristol Myers Squibb, GlaxoSmithKline, Janssen, Merck, Novartis, Pfizer, Roche, UCB (funds go to CCHMC/employer), Grant/research support from: Bristol Myers Squibb, Pfizer (funds go to CCHMC/employer).
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Nordal, HH, JG Brun, A.-K. Halse, TM Madland, MK Fagerhol, and R. Jonsson. "Calprotectin (S100A8/A9), S100A12, and EDTA-resistant S100A12 complexes (ERAC) in primary Sjögren’s syndrome." Scandinavian Journal of Rheumatology 43, no. 1 (December 3, 2013): 76–78. http://dx.doi.org/10.3109/03009742.2013.848930.
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Casertano, M., S. Cenni, A. M. Caprio, F. Oglio, D. Pacella, E. Miele, M. Martinelli, A. Staiano, and C. Strisciuglio. "P214 Faecal S100A12 as a non-invasive marker of inflammatory activity in pediatric Inflammatory Bowel Disease." Journal of Crohn's and Colitis 15, Supplement_1 (May 1, 2021): S271—S272. http://dx.doi.org/10.1093/ecco-jcc/jjab076.340.
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Abstract Background Calgranulin-C (S100A12) is a new faecal marker of inflammation that is potentially more specific for Inflammatory Bowel Disease (IBD) than calprotectin, since it is only released by activated granulocytes. In recent years it has been confirmed that the S100A12 has comparable sensitivity and specificity to fecal calprotectin (FC) in adult patients with IBD. The aim of our study was to evaluate concentration of faecal S100A12 and calprotectin (FC) to see which of the two tests best correlated to inflammation in IBD children. Methods Between September 2019 and March 2020, we prospectively enrolled all IBD pediatric patients, both Crohn’s Disease (CD) and Ulcerative Colitis (UC). Blood and faecal samples were collected in order to evaluate serological markers of inflammation, faecal S100A12A and FC. S100A12 and FC were determined by enzyme-linked immunosorbent assay (ELISA). Results One hundred seventeen consecutive children, 46 (39%) with CD and 71 (61%) with UC were enrolled in the study. The mean age was 14.6 years (range:5–18), 44% female. Twenty three children were in clinical relapse (20%). No significant differences in S100 A12A levels were found between the UC and the CD groups (mean ±ds 25 ±32mcg/ml vs 34 ±27 mcg/ml respectively, p=0.22).In the UC group we found a statistically significant correlation of both calprotectin and S100A12 with CRP (r=0.253, p=0.044 and r=0.252, p=0.040, respectively). In CD group we found that both calprotectin and S100A12 correlated with hemoglobin (r= -0.343, p=0,024; r=-0.401, p 0.008 respectively), hematocrit (r=-0.361, p=0,046; r=-0.434, p=0.015, respectively), fibrinogen (r=0.499, p< 0,001; r=0.325, p =0.038, respectively), and white blood cells count (r=0.309, p=0.044; r=0.394, p=0.021, respectively). Moreover, in CD group, FC correlated with CRP (r=0.431, p=0.004) and erythrocyte sedimentation rate (r=0.430, p=0.004). Finally, S100A12 correlated with platelet count both in CD and UC group (r=0.351, p=0.021and r=0.254, p=0.038, respectively) IBD children in clinical relapse had higher values of S100A12 and FC than patients in remission (66±47 mcg/ml vs 43±42 mcg/ml, p=0.05 and 260±192 mg/Kg vs 166±169 mg/Kg, p=0.046, respectively) Conclusion Our preliminary data show that both faecal S100A12 and FC are useful non-invasive biomarkers which reflect inflammatory activity of IBD children. Our future aim is to evaluate the correlation of S100A12 and endoscopic finding in order to further clarify its role in the diagnosis and the management of pediatric IBD.
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Azzaoui, Imane, Fabrice Uhel, Delphine Rossille, Céline Pangault, Joelle Dulong, Jerome Le Priol, Thierry Lamy, et al. "T-Cell Defect in Diffuse Large B-Cell Lymphomas Involves Expansion of Myeloid Derived Suppressor Cells Expressing IL-10, PD-L1, and S100A12." Blood 126, no. 23 (December 3, 2015): 1478. http://dx.doi.org/10.1182/blood.v126.23.1478.1478.
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Abstract Introduction: In diffuse large B-cell lymphoma (DLBCL), the number of circulating monocytes and neutrophils represents an independent prognostic factor. These cells include monocytic and granulocytic myeloid derived suppressor cells (M- and G-MDSCs) defined by their ability to suppress T-cell responses. MDSCs are a heterogeneous population described in inflammatory or infectious diseases as well as in numerous tumors including multiple myeloma, chronic lymphocytic leukemia and DLBCL. However, their mechanisms of action in DLBCL remain unclear. The aim of the study was to investigate the presence and mechanisms of suppression of MDSC subsets in DLBCL. Methods: Whole blood from 56 DLBCL at diagnosis and 45 healthy donors (HD) were analyzed by flow cytometry. Quantitative Real Time PCR were analyzed on Taqman@ array microfluidic cards. Cytokine levels in plasma and culture supernatants were measured by Luminex and Elisa. T-cell proliferation after monocyte depletion or treatment with inhibitors, was analyzed by CFSE assay. Results: By flow cytometry, we identified an expansion of G-MDSC (Linneg HLA-DRneg CD33pos CD11bpos) and M-MDSC (CD14pos HLA-DRlow) in DLBCL compared to HD (p<0.001). Interestingly, only M-MDSC number was correlated with the International Prognostic Index (IPI), the event-free survival (EFS), and the number of circulating Treg. Furthermore, T-cell proliferation was restored after monocyte depletion. To identify the mechanism of suppression involved, we evaluated the gene expression of key enzymes (ARG1, IDO1, NOS2, HO-1 and PTGS2) or immunomodulatory molecules (IL10, TGF β1, CD274/PD-L1, S100A8, S100A9, S100A12) involved in MDSC biology. ARG1, IDO1, IL10, CD274/PD-L1 and S100A12 were significantly up-regulated in DLBCL (p<0.05). At the protein level arginase 1, IL-10 and S100A12 were increased in DLBCL plasma, whereas PD-L1 expression on monocyte was increased in DLBCL compared to HD (p=0.03). Arginase 1 and IDO activities where increased in DLBCL patients. In DLBCL, IL-10 and S100A12 were detected in culture supernatants from stimulated PBMC and these molecules were decreased after CD14pos depletion (p<0.05). Finally, we defined 2 groups of DLBCL depending on M-MDSC content and analyzed the percentage of proliferating T cells after CD3/CD28 stimulation in the presence of various inhibitors or blocking antibodies (L-1MT, nor-NOHA, anti-IL-10, anti-PD-1 and anti-S100A12). In the group of patients with circulating MDSC, neutralizing IL-10, PDL-1 and S100A12 resulted in an increase of CD4 and/or CD8 T-cell proliferation. Conclusion: In summary, we identified MDSC subsets expanded in DLBCL as well as new mechanisms of immunosuppression in DLBCL. Myeloid-dependent T-cell suppression is attributed to a release of IL-10 and S100A12 and an increase of PD-L1 expression. Disclosures Cartron: Roche: Consultancy, Honoraria; GSK: Honoraria; Celgene: Honoraria; Sanofi: Honoraria; Gilead: Honoraria.
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Baillet, A. "Protéines S100A8, S100A9 et S100A12 : marqueurs inflammatoires ou acteurs physiopathologiques de la polyarthrite rhumatoïde." La Revue de Médecine Interne 31, no. 6 (June 2010): 458–61. http://dx.doi.org/10.1016/j.revmed.2009.10.435.
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Shepherd, C. E., J. Goyette, V. Utter, F. Rahimi, Z. Yang, C. L. Geczy, and G. M. Halliday. "Inflammatory S100A9 and S100A12 proteins in Alzheimer's disease." Neurobiology of Aging 27, no. 11 (November 2006): 1554–63. http://dx.doi.org/10.1016/j.neurobiolaging.2005.09.033.
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Däbritz, Jan, Dirk Foell, Stefan Wirth, and Andreas Jenke. "Fecal S100A12." Journal of Pediatric Gastroenterology and Nutrition 57, no. 2 (August 2013): 204–10. http://dx.doi.org/10.1097/mpg.0b013e3182946eb2.
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Kishimoto, Kazuya, Satoshi Kaneko, Kenji Ohmori, Tadafumi Tamura, and Kazuhide Hasegawa. "Olopatadine Suppresses the Migration of THP-1 Monocytes Induced by S100A12 Protein." Mediators of Inflammation 2006 (2006): 1–5. http://dx.doi.org/10.1155/mi/2006/42726.
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Olopatadine hydrochloride (olopatadine) is an antiallergic drug with histamineH1receptor antagonistic activity. Recently, olopatadine has been shown to bind to S100A12 which is a member of the S100 family of calcium-binding proteins, and exerts multiple proinflammatory activities including chemotaxis for monocytes and neutrophils. In this study, we examined the possibility that the interaction of olopatadine with S100A12 inhibits the proinflammatory effects of S100A12. Pretreatment of olopatadine with S100A12 reduced migration of THP-1, a monocyte cell line, induced by S100A12 alone, but did not affect recombinant human regulated upon activation, normal T cell expressed and secreted (RANTES)-induced migration. Amlexanox, which also binds to S100A12, inhibited the THP-1 migration induced by S100A12. However, ketotifen, another histamineH1receptor antagonist, had little effect on the activity of S100A12. These results suggest that olopatadine has a new mechanism of action, that is, suppression of the function of S100A12, in addition to histamineH1receptor antagonistic activity.
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Borsky, Pavel, Zdenek Fiala, Ctirad Andrys, Martin Beranek, Kvetoslava Hamakova, Andrea Malkova, Tereza Svadlakova, et al. "Alarmins HMGB1, IL-33, S100A7, and S100A12 in Psoriasis Vulgaris." Mediators of Inflammation 2020 (April 15, 2020): 1–7. http://dx.doi.org/10.1155/2020/8465083.
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Background. Psoriasis vulgaris is a chronic autoimmune disease associated with systemic inflammation. Increased levels of numerous cytokines, chemokines, growth factors, and other molecules were found in the skin and in the circulation of psoriatic patients. Alarmins, also known as danger signals, are intracellular proteins, which are released to an extracellular space after infection or damage. They are the markers of cell destructive processes. Objective. The aim of the present study was to evaluate the suitability of selected alarmins (HMGB1, IL-33, S100A7, and S100A12) as potential biomarkers of severity of psoriasis and to explore possible relationships between these proteins for the purpose of better understanding their roles in the immunopathology of psoriasis. Methods. The serum levels of selected alarmins were measured in 63 psoriatic patients and 95 control individuals. The levels were assessed by the ELISA technique using commercial kits. The data were statistically processed with MedCalc version 19.0.5. Results. In psoriatic patients, we found significantly increased levels of HMGB1 (p<0.05), IL-33 (p<0.01), S100A7 (p<0.0001), and S100A12 (p<0.0001). In addition, we found a significant relationship between HMGB1 and S100A7 (Spearman’s rho=0.276, p<0.05) in the patients and significant relationship between HMGB1 and IL-33 in the controls (Spearman’s rho=0.416, p<0.05). We did not find any relationship between observed alarmins and the disease severity. Conclusions. The alarmins HMGB1, IL-33, S100A7, and S100A12 were significantly elevated in the serum of patients, which states the hypothesis that they play specific roles in the immunopathology of psoriasis. However, we have not yet found a relationship between observed alarmins and the disease severity. The discovery of the relationship between HMGB1 and S100A7 is a novelty that should be studied in the future to further clarify its role and importance.
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Zhang, Xiaoxiao, Chihyean Ong, Guowei Su, Jian Liu, and Ding Xu. "Characterization and engineering of S100A12–heparan sulfate interactions." Glycobiology 30, no. 7 (January 14, 2020): 463–73. http://dx.doi.org/10.1093/glycob/cwz111.
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Abstract S100A12, an EF-hand calcium-binding protein, can be secreted by a variety of cell types and plays proinflammatory roles in a number of pathological conditions. Although S100A12 has been shown to interact with heparan sulfate (HS), the molecular detail of the interaction remains unclear. Here we investigate the structural basis of S100A12–HS interaction and how the interaction is regulated by the availability of divalent cations and the oligomeric states of S100A12. We discovered that S100A12–HS interaction requires calcium, while zinc can further enhance binding by inducing S100A12 hexamerization. In contrast, the apo form and zinc-induced tetramer form were unable to bind HS. Guided by the crystal structures of S100A12, we have identified the HS-binding site of S100A12 by site-directed mutagenesis. Characterization of the HS-binding site of S100A12 allowed us to convert the non-HS-binding apo and tetramer forms of S100A12 into a high affinity HS-binding variant by engineering a single-point mutation. Using a HS oligosaccharide microarray, we demonstrated that the N43K mutant displayed markedly enhanced selectivity toward longer HS oligosaccharides compared to the WT S100A12, likely due to the expanded dimension of the reengineered HS-binding site in the mutant. This unexpected finding strongly suggests that HS-binding sites of proteins might be amenable for engineering.
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Isoyama, Naohito, Anna Machowska, Abdul Rashid Qureshi, Tae Yamamoto, Björn Anderstam, Olof Heimburger, Peter Barany, Peter Stenvinkel, and Bengt Lindholm. "Elevated Circulating S100A12 Associates with Vascular Disease and Worse Clinical Outcome in Peritoneal Dialysis Patients." Peritoneal Dialysis International: Journal of the International Society for Peritoneal Dialysis 36, no. 3 (May 2016): 269–76. http://dx.doi.org/10.3747/pdi.2014.00121.
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Background The pro-inflammatory receptor of advanced glycation end-products (RAGE)-ligand S100A12 is thought to promote, whereas anti-inflammatory soluble RAGE (sRAGE) may protect against, vascular disease. We evaluated circulating S100A12 and sRAGE in relation to vascular disease, inflammation, nutritional status, and mortality risk in peritoneal dialysis (PD) patients. Methods Plasma S100A12 and sRAGE, biomarkers of inflammation, nutritional status, and comorbidities were analyzed in 82 prevalent PD patients (median age 65 years; 70% men; median vintage 12 months) and, for comparative analysis, also in 190 hemodialysis (HD) patients and 50 control subjects. Associations between mortality risk and concentrations of S100A12 and sRAGE were assessed in PD and HD patients after a mean follow-up period of 31 and 29 months respectively using a competing risk Cox regression model. Results In PD patients, median S100A12, sRAGE and S100A12/sRAGE were markedly higher than in controls, and S100A12 was 1.9 times higher and median sRAGE 14% lower compared with HD patients. In PD patients, S100A12 associated with C-reactive protein (ρ = 0.46; p < 0.001) and interleukin-6 (ρ = 0.38; p < 0.001), and, negatively, with s-albumin (ρ = -0.27; p < 0.05) whereas sRAGE associated negatively with body mass index (ρ = -0.37; p < 0.001), fat body mass index (ρ = -0.34; p < 0.001), and lean body mass index (ρ = -0.36; p < 0.001). Peripheral vascular disease or cerebrovascular disease (PCVD) was present in 28% of PD patients and, in multivariate analysis, associated mainly with high S100A12 (odds ratio [OR] 3.52, p = 0.04). In both PD and HD patients, the highest versus other tertiles of S100A12 associated with increased mortality. In contrast, sRAGE did not associate with PCVD or mortality in PD and HD patients. Conclusions Plasma S100A12 and sRAGE are markedly elevated in PD patients. Soluble RAGE was inversely related to body mass indices while S100A12 associated with increased inflammation, PCVD, and mortality, suggesting that S100A12 may identify PD patients at high risk for vascular disease and increased mortality.
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Buyukterzi, Zafer, Ummugulsum Can, Sertac Alpaydin, Asuman Guzelant, Sukru Karaarslan, Duygu Kocyigit, and Kadri Murat Gurses. "Enhanced S100A9 and S100A12 expression in acute coronary syndrome." Biomarkers in Medicine 11, no. 3 (March 2017): 229–37. http://dx.doi.org/10.2217/bmm-2016-0253.
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Robinson, Matthew J., and Nancy Hogg. "A Comparison of Human S100A12 with MRP-14 (S100A9)." Biochemical and Biophysical Research Communications 275, no. 3 (September 2000): 865–70. http://dx.doi.org/10.1006/bbrc.2000.3407.
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Gunaldi, Meral, Yildiz Okuturlar, Asuman Gedikbasi, Cevher Akarsu, Mehmet Karabulut, and Alev Kural. "Diagnostic importance of S100A9 and S100A12 in breast cancer." Biomedicine & Pharmacotherapy 76 (December 2015): 52–56. http://dx.doi.org/10.1016/j.biopha.2015.10.029.
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Lou, Yueyan, Yu Zheng, Bijun Fan, Liyan Zhang, Feng Zhu, Xiaodong Wang, Zhiwei Chen, and Xiaoming Tan. "Serum S100A12 levels are correlated with clinical severity in patients with dermatomyositis-associated interstitial lung disease." Journal of International Medical Research 48, no. 4 (December 23, 2019): 030006051988784. http://dx.doi.org/10.1177/0300060519887841.
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Objective S100A12 is an emerging inflammatory disease biomarker. Interstitial lung disease (ILD) is a common, severe complication of dermatomyositis (DM). This study was performed to investigate the association between S100A12 and disease activity and prognosis in patients with DM-associated ILD (i.e., DM-ILD). Methods Serum S100A12 levels were measured using enzyme-linked immunosorbent assays in patients with stable DM-ILD, patients with acute exacerbation of DM-ILD (AE DM-ILD), and healthy controls (HCs). The relationships of serum S100A12 levels with C-reactive protein (CRP), erythrocyte sedimentation rate (ESR), ferritin, high-resolution computed tomography (HRCT) scores, and pulmonary functions were evaluated by multiple unpaired t-tests and Pearson correlation. Results Serum S100A12 levels were higher in patients with stable DM-ILD and those with AE DM-ILD than in HCs. Serum S100A12 levels in patients with stable DM-ILD and those with AE DM-ILD were positively correlated with CRP, ESR, and ferritin. S100A12 levels were positively correlated with HRCT scores in patients with stable DM-ILD and those with AE DM-ILD, while they were negatively correlated with predicted percentages of forced vital capacity and predicted percentages of carbon monoxide diffusing capacity in those patients. Conclusion Our findings demonstrate the usefulness of serum S100A12 levels for assessing clinical severity and prognosis of DM-ILD.
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Fuellen, Georg, Dirk Foell, Wolfgang Nacken, Clemens Sorg, and Claus Kerkhoff. "Absence of S100A12 in mouse: implications for RAGE–S100A12 interaction." Trends in Immunology 24, no. 12 (December 2003): 622–24. http://dx.doi.org/10.1016/j.it.2003.10.004.
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Chen, Chia-Sheng, Li-Wei Lin, Chia-Chang Hsieh, Guang-Wei Chen, Wen-Huang Peng, and Ming-Tsuen Hsieh. "Differential Gene Expression in Hemodialysis Patients with "Cold" Zheng." American Journal of Chinese Medicine 34, no. 03 (January 2006): 377–85. http://dx.doi.org/10.1142/s0192415x06003916.
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The aim of the present study was to search for the differential gene expression and measure the serum level of a number of biochemical parameters in the cold Zheng (CZ) and non-cold Zheng (NCZ) in patients receiving hemodialysis. Hemodialysis (HD) patients were randomly selected from the CZ and NCZ groups. The between-group differences in gene expression were assessed using complementary DNA (cDNA) microarray. Differential gene expression was further validated by real-time reverse transcriptase polymerase chain reaction (RT-PCR). Our results demonstrated that the up-regulation of the inflammation-associated genes, ALOX5AP, S100A8 and S100A12, down-regulation of the genes related to immunity (DEFA4), metabolism (GNG11, PYGB, PRKAR2B), and growth/proliferation (HSF2, DDR2, TK1) were found in the CZ group. Furthermore, the CZ HD patients had significantly lower serum albumin levels compared with their NCZ counterparts (3.31 ± 0.08 g/dL versus 4.18 ± 0.12 g/dL ). It appears reasonable to conclude that up-regulated inflammatory-gene expression (ALOX5AP, S100A8 and S100A12) may play an important role in CZ HD patients.
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Meijer, B., R. B. Gearry, and A. S. Day. "The Role of S100A12 as a Systemic Marker of Inflammation." International Journal of Inflammation 2012 (2012): 1–6. http://dx.doi.org/10.1155/2012/907078.
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S100A12 is a member of the S100 family of calcium-binding proteins with important extracellular activities. In recent years, investigators across a number of fields have delineated the patterns of S100A12 expression in a variety of conditions. These data suggest that S100A12 can be used as a valuable serum inflammatory marker.
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Day, A. S., M. Ehn, R. B. Gearry, D. A. Lemberg, and S. T. Leach. "Fecal S100A12 in Healthy Infants and Children." Disease Markers 35 (2013): 295–99. http://dx.doi.org/10.1155/2013/873582.
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Background and Aims. Fecal S100A12 is shown to be a useful noninvasive marker of gut inflammation. However, the studies to date have not characterised the patterns of expression in healthy young children. This study aimed to determine S100A12 levels in infants and children without symptoms of underlying gut disease.Methods. Stool samples were collected from healthy infants (<12 months) and children without gastrointestinal symptoms. Faecal S100A12 was measured by immunoassay.Results. Fifty-six children were recruited. Serial samples were obtained from seven term infants over the first 6 months of life. Single samples were obtained from 49 healthy children ranging from 0.16 to 13.8 years of age. Median S100A12 levels were 0.5 mg/kg (ranging from 0.39 to 25) in the healthy children, with high values (>10 mg/kg) in five infants only. There was no variation between gender. Median S100A12 levels in healthy infants remained below the established normal cut-off from birth to six months of age.Conclusion. S100A12 levels in well infants and children are almost exclusively lower than the standard cut-off. Transiently higher levels may be seen in early infancy. An elevated level of S100A12 in children older than 12 months of age is likely to represent organic gut disease.
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Carvalho, Alexandre, Jacky Lu, Jamisha D. Francis, Rebecca E. Moore, Kathryn P. Haley, Ryan S. Doster, Steven D. Townsend, Jeremiah G. Johnson, Steven M. Damo, and Jennifer A. Gaddy. "S100A12 in Digestive Diseases and Health: A Scoping Review." Gastroenterology Research and Practice 2020 (February 26, 2020): 1–11. http://dx.doi.org/10.1155/2020/2868373.
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Calgranulin proteins are an important class of molecules involved in innate immunity. These members of the S100 class of the EF-hand family of calcium-binding proteins have numerous cellular and antimicrobial functions. One protein in particular, S100A12 (also called EN-RAGE or calgranulin C), is highly abundant in neutrophils during acute inflammation and has been implicated in immune regulation. Structure-function analyses reveal that S100A12 has the capacity to bind calcium, zinc, and copper, processes that contribute to nutritional immunity against invading microbial pathogens. S100A12 is a ligand for the receptor for advanced glycation end products (RAGE), toll-like receptor 4 (TLR4), and CD36, which promote cellular and immunological pathways to alter inflammation. We conducted a scoping review of the existing literature to define what is known about the association of S100A12 with digestive disease and health. Results suggest that S100A12 is implicated in gastroenteritis, necrotizing enterocolitis, gastritis, gastric cancer, Crohn’s disease, irritable bowel syndrome, inflammatory bowel disease, and digestive tract cancers. Together, these results reveal S100A12 is an important molecule broadly associated with the pathogenesis of digestive diseases.
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Pulsipher, Abigail, Brock M. Davis, Kristine A. Smith, Shaelene Ashby, Xuan Qin, Matt Firpo, Richard R. Orlandi, and Jeremiah A. Alt. "Calgranulin C (S100A12) Is Differentially Expressed in Subtypes of Chronic Rhinosinusitis." American Journal of Rhinology & Allergy 32, no. 5 (June 26, 2018): 380–87. http://dx.doi.org/10.1177/1945892418782238.
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Background Calgranulin C (S100A12) is an innate immune peptide at the air–mucosal interface associated with neutrophil involvement, which when overexpressed has been implicated as a biomarker of inflammatory diseases. Decreased epithelial expression of certain innate immune peptides has been reported in chronic rhinosinusitis (CRS). We hypothesized that S100A12 is differentially expressed in the sinonasal mucosa of patients with CRS compared to controls and that S100A12 is a potential biomarker of CRS-specific quality of life (QOL) and disease severity. Methods A prospective observational study was conducted which included 70 patients: 17 controls, 28 having CRS without (CRSsNP), and 25 with (CRSwNP) nasal polyps. The expression of S100A12 and human neutrophil elastase (HNE) was assessed in the anterior ethmoid tissues from all patients using enzyme-linked immunosorbent assay (ELISA) and immunohistochemical (IHC) analyses. Disease-specific QOL (Rhinosinusitis Disability Index) and disease severity (computed tomography [CT] and endoscopy) were evaluated and correlated to the expression levels of S100A12. Results S100A12 and HNE were significantly elevated in patients with CRSsNP compared to normal controls ( P < .05 and P < .001, respectively) and patients with CRSwNP ( P < .05 and P < .001, respectively), as measured by ELISA and IHC analyses. Patients with CRS exhibited worse CRS-specific disease severity compared to normal controls ( P < .05), and the increased protein levels of S100A12 were significantly correlated to disease severity, represented by CT scores ( P < .05). Conclusions S100A12 is differentially expressed in CRS subtypes and is significantly elevated in patients with CRSsNP and associated with CRS-specific disease severity.
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Böni, R., G. Burg, E. C. Ilg, B. W. Schäfer, A. Doguoglu, R. Dummer, and C. W. Heizmann. "STAINING PATTERN OF THE Ca2+-BINDING PROTEINS S100A1, S100A2, S100A3, S100A4 AND S100A6 IN HUMAN SKIN AND MELANOCYTIC LESIONS." American Journal of Dermatopathology 19, no. 5 (October 1997): 494. http://dx.doi.org/10.1097/00000372-199710000-00022.
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Lim, Mann Ying, and Paul S. Thomas. "Biomarkers in Exhaled Breath Condensate and Serum of Chronic Obstructive Pulmonary Disease and Non-Small-Cell Lung Cancer." International Journal of Chronic Diseases 2013 (2013): 1–15. http://dx.doi.org/10.1155/2013/578613.
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Chronic obstructive pulmonary disease (COPD) and lung cancer are leading causes of deaths worldwide which are associated with chronic inflammation and oxidative stress. Lung cancer, in particular, has a very high mortality rate due to the characteristically late diagnosis. As such, identification of novel biomarkers which allow for early diagnosis of these diseases could improve outcome and survival rate. Markers of oxidative stress in exhaled breath condensate (EBC) are examples of potential diagnostic markers for both COPD and non-small-cell lung cancer (NSCLC). They may even be useful in monitoring treatment response. In the serum, S100A8, S100A9, and S100A12 of the S100 proteins are proinflammatory markers. They have been indicated in several inflammatory diseases and cancers including secondary metastasis into the lung. It is highly likely that they not only have the potential to be diagnostic biomarkers for NSCLC but also prognostic indicators and therapeutic targets.
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Wang, Yin-na, Yi Sun, Ying Wang, and Yan-li Jia. "Serum S100A12 and Progression of Coronary Artery Calcification Over 4 Years in Hemodialysis Patients." American Journal of Nephrology 42, no. 1 (2015): 4–13. http://dx.doi.org/10.1159/000438869.
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Background/Aim: Vascular calcification is common and contributes to increased cardiovascular mortality in hemodialysis (HD) patients. In this prospective study, we aimed to investigate the associations of serum S100A12 in the presence of severe coronary artery calcification (CAC) and the progression of CAC in HD patients. Methods: Sixty maintenance HD patients and 30 controls were enrolled. Serum S100A12 levels were measured using ELISA. CAC scores (CACs) were measured twice at a 4-year interval using multislice spiral CT. The HD patients were classified as rapid progressors or slow progressors according to the change in the CACs across these 2 measurements (ΔCACs). Results: The incidences of rapid progression of CAC in patients with baseline CACs ≤10, CACs >10 and CACs >400 were 12.5, 40.0 and 64.3%, respectively. Both baseline and 4-year serum S100A12 levels were significantly higher in the rapid progressors than in the slow progressors (medians of 45.6 vs. 30.2 ng/ml, p < 0.001 and 62.3 vs. 39.4 ng/ml, p = 0.002, respectively). The serum S100A12 levels were significantly correlated with baseline CACs (r = 0.466, p < 0.001), 4-year CACs (r = 0.440, p < 0.001) and ΔCACs (r = 0.392, p < 0.001). Importantly, the ΔCACs were significantly correlated with ΔS100A12 levels (r = 0.396, p < 0.001). Logistic regression analysis revealed that the serum S100A12 level was as an independent determinant of the presence of severe CAC and that the increment in the serum S100A12 level was a factor that was significantly independently associated with the progression of CAC. Conclusions: Serum S100A12 levels were significantly associated with the presence of severe CAC, and the increment in serum S100A12 levels was an independent determinant of the progression of CAC.
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Bae, Chang-Bum, Chang-Hee Suh, Jeong-Mi An, Ju-Yang Jung, Ja-Young Jeon, Jin-Young Nam, and Hyoun-Ah Kim. "Serum S100A12 May Be a Useful Biomarker of Disease Activity in Adult-onset Still’s Disease." Journal of Rheumatology 41, no. 12 (October 1, 2014): 2403–8. http://dx.doi.org/10.3899/jrheum.140651.
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Objective.S100A12 and soluble receptor for advanced glycation endproducts (sRAGE) have been suggested as biomarkers of disease activity in patients with systemic juvenile idiopathic arthritis. We investigated the clinical significance of these markers in adult-onset Still’s disease (AOSD).Methods.Blood samples were collected from 37 patients with active AOSD and 38 healthy controls (HC). Of the patients with AOSD, followup samples were collected from 19 patients after resolution of disease activity.Results.Serum S100A12 (547.9 ± 148.4 ng/ml) in patients with AOSD was higher than those of HC (272.3 ± 133 ng/ml, p < 0.001). The sRAGE levels of AOSD (514.1 ± 273.6 pg/ml) were lower than those of HC (850.3 ± 405.8 pg/ml, p < 0.001). Serum S100A12 correlated with serum sRAGE (r = −0.228, p = 0.049). Serum S100A12 correlated with erythrocyte sedimentation rate (ESR), C-reactive protein (CRP), ferritin, and systemic score, whereas sRAGE did not correlate with any disease activity markers. In addition, the level of S100A12 was decreased after disease activity was resolved in followed-up patients with AOSD (505.7 ± 161.3 ng/ml vs 361.3 ± 162.5 ng/ml, p = 0.01). Further, the change of S100A12 was well correlated with that of ESR, CRP, and systemic score.Conclusion.S100A12 levels showed strong correlations with known disease activity markers such as ESR, CRP, ferritin, and systemic score. In the followup patients with AOSD, most patients showed decreased S100A12 levels after resolution of disease activity. These results suggest that serum S100A12 can be a reliable clinical marker for monitoring disease activity and treatment response.
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Abdallah, Zeinab Y., Mona Ibrahim, Manal M. Thomas, Hisham Megahed, Ghada Nour Eldeen, Khaled Hamed, Mohamed Fares, Mahmoud ElHefnawi, and Hala T. El-Bassyouni. "Clinical Implications of S100A12 and Resolvin D1 Serum Levels, and Related Genes in Children with Familial Mediterranean Fever." Journal of Child Science 11, no. 01 (January 2021): e163-e169. http://dx.doi.org/10.1055/s-0041-1731303.
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AbstractThe aim of this article was to study the role of S100A12 and resolvin D1-related genes and serum levels in the diagnosis and detection of subclinical inflammation in children with familial Mediterranean fever (FMF) during the quiescent stage of the disease. Seventy-eight children with FMF during the silent state and 60 healthy control were studied. Serum S100A12 and resolvin D1 were quantitatively measured using enzyme-linked immunosorbent assay. In addition, the levels of C-reactive protein, erythrocyte sedimentation rate, and hemoglobin were determined. The clinical severity was evaluated. The link between the Mediterranean fever (MEFV) gene and the genes related to the two studied biomarkers was also assessed. Correlation between S100A12 and resolvin D1 and the clinical severity was assessed. The mean serum levels of S100A12 and resolvin D1 were 847.4 and 793.3, respectively, which were highly significantly increased (p = 0.001) compared with the controls (324.3 and 235.1, respectively). The receiver operating characteristic curve test showed that S100A12 had a sensitivity of 97.4% and specificity of 80% with cutoff value of 529.5, while resolvin D1 showed a sensitivity of 100% and specificity of 50% with cutoff value of 231.2. A correlation was detected between the clinical severity and S100A12 and resolvin D1. This study delineated that S100A12 and resolvin D1 are sensitive biomarkers to detect the degree of inflammation in children with FMF during the silent period. Consequently, we recommend adjusting the colchicine dose to ameliorate the disease's symptoms and to improve the quality of life in these patients.
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Davies, Jennifer C., Angela Midgley, Emil Carlsson, Sean Donohue, Ian N. Bruce, Michael W. Beresford, and Christian M. Hedrich. "Urine and serum S100A8/A9 and S100A12 associate with active lupus nephritis and may predict response to rituximab treatment." RMD Open 6, no. 2 (July 2020): e001257. http://dx.doi.org/10.1136/rmdopen-2020-001257.
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BackgroundApproximately 30% of patients with the systemic autoimmune/inflammatory disorder systemic lupus erythematosus (SLE) develop lupus nephritis (LN) that affects treatment and prognosis. Easily accessible biomarkers do not exist to reliably predict renal disease. The Maximizing SLE Therapeutic Potential by Application of Novel and Systemic Approaches and the Engineering Consortium aims to identify indicators of treatment responses in SLE. This study tested the applicability of calcium-binding S100 proteins in serum and urine as biomarkers for disease activity and response to treatment with rituximab (RTX) in LN.MethodsS100A8/A9 and S100A12 proteins were quantified in the serum and urine of 243 patients with SLE from the British Isles Lupus Assessment Group Biologics Register (BILAG-BR) study and 48 controls matched for age using Meso Scale Discovery’s technology to determine whether they perform as biomarkers for active LN and/or may be used to predict response to treatment with RTX. Renal disease activity and response to treatment was based on BILAG-BR scores and changes in response to treatment.ResultsSerum S100A12 (p<0.001), and serum and urine S100A8/A9 (p<0.001) levels are elevated in patients with SLE. While serum and urine S100 levels do not correlate with global disease activity (SLE Disease Activity Index), levels in urine and urine/serum ratios are elevated in patients with active LN. S100 proteins perform better as biomarkers for active LN involvement in patients with SLE who tested positive for anti-double-stranded DNA antibodies. Binary logistic regression and area under the curve analyses suggest the combination of serum S100A8/A9 and S100A12 can predict response to RTX treatment in LN after 6 months.ConclusionsFindings from this study show promise for clinical application of S100 proteins to predict active renal disease in SLE and response to treatment with RTX.
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Baillet, A., C. Trocme, S. Berthier, M. Arlotto, L. Grange, J. Chenau, S. Quetant, et al. "Synovial fluid proteomic fingerprint: S100A8, S100A9 and S100A12 proteins discriminate rheumatoid arthritis from other inflammatory joint diseases." Rheumatology 49, no. 4 (January 25, 2010): 671–82. http://dx.doi.org/10.1093/rheumatology/kep452.
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Ruse, Monica, Adam Lambert, Nancy Robinson, David Ryan, Ki-Joon Shon, and Richard L. Eckert. "S100A7, S100A10, and S100A11 Are Transglutaminase Substrates†." Biochemistry 40, no. 10 (March 2001): 3167–73. http://dx.doi.org/10.1021/bi0019747.
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Wang, Xiangming, Tingting Xu, Deeraj Mungun, Chuanwei Zhou, Zhimin Zha, Miao Lu, Chuyan Fen, and Yan Guo. "The Relationship between Plasma Soluble Receptor for Advanced Glycation End Products and Coronary Artery Disease." Disease Markers 2019 (June 2, 2019): 1–10. http://dx.doi.org/10.1155/2019/4528382.
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Background. Inflammation is involved in the development and progression of coronary artery disease (CAD). The role of the receptor for advanced glycation end products (RAGE) in the development of CAD has been recognized. The expression of sRAGE and S100A12 in patients with coronary artery disease from different studies was inconsistent. We attempted to determine the expression of sRAGE and S100A12 and their relationship in the subjects with different severity levels of CAD. Methods. A total of 259 patients undergoing coronary angiography were enrolled from the Department of Geriatric Cardiology in the First Affiliated Hospital of Nanjing Medical University from January 2014 to December 2016. Groups were divided as follows: normal coronary artery (control group), nonobstructive coronary atherosclerosis (<50% stenosis in all coronary vessels, NOCA group), stable angina (SAP group), and acute coronary syndrome (ACS group). During CAG or PCI, peripheral arterial blood was collected from all the patients. Plasma sRAGE and S100A12 levels were measured by ELISA. We calculated the SYNTAX score of each patient with CAD according to the result of CAG. Results. The levels of sRAGE were significantly elevated in the ACS group compared with those in the control group, the NOCA group, and the SAP group. sRAGE levels were similar among the control group, the NOCA group, and the SAP group. Plasma S100A12 levels were significantly higher in the ACS group than in the control group and the NOCA group. Baseline correlations between plasma levels of sRAGE and plasma S100A12 in the ACS group were significant. Plasma sRAGE concentration was increasing in patients with ACS and was significantly positively correlated with the increasing SYNTAX score. ROC curve analysis revealed that the combination of sRAGE and S100A12 had a good performance in the prediction of high-risk CAD patients. Conclusion. The plasma levels of sRAGE and S100A12 can be increased in patients with ACS. The elevated sRAGE concentration may be independently associated with the severity of CAD and the inflammatory process. sRAGE combined with S100A12 may be used as a predictor of severe coronary heart disease.
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Whitehead, Simon John, Clare Ford, Rousseau Mariano Gama, Ala Ali, Brian McKaig, Jenna Louise Waldron, Helen Steed, and Matthew James Brookes. "Effect of faecal calprotectin assay variability on the management of inflammatory bowel disease and potential role of faecal S100A12." Journal of Clinical Pathology 70, no. 12 (July 22, 2017): 1049–56. http://dx.doi.org/10.1136/jclinpath-2017-204340.
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AimsTo prospectively evaluate whether between-assay variability of different faecal calprotectin (f-Cp) assays influences diagnostic accuracy for inflammatory bowel disease (IBD) in a cohort of patients with confirmed IBD and irritable bowel syndrome (IBS). To also evaluate the diagnostic accuracy of faecal S100A12 (f-S100A12) against f-Cp in the same patient cohort and assess whether f-S100A12 offers additional diagnostic value.MethodsF-Cp using four commercially available f-Cp assays, f-S100A12 and blood biomarkers were measured in patients, recruited from the local IBD clinic, who had established IBS or active ulcerative colitis (UC) and Crohn’s disease (CD). Diagnostic sensitivities and specificities for each assay and biomarker were calculated and compared.ResultsMedian f-Cp levels in all assays were significantly higher in UC (347–884 µg/g; n=28) and CD (377–838 µg/g; n=15) compared with IBS (6–27 µg/g; n=17). Sensitivities and specificities at 50 µg/g were 94%–100% and 82%–100%, respectively. Median f-S100A12 levels were significantly higher in UC (81.0 µg/g; IQR 38.3–159.8) and CD (47.2 µg/g; IQR 5.3–108.9) compared with IBS (0.7 µg/g; IQR 0.5–0.8). At 2.8 µg/g, f-S100A12 had a sensitivity of 97% and specificity of 94%. The blood biomarkers demonstrated sensitivities and specificities of 44%–63% and 80%–92%, respectively.ConclusionsThe diagnostic sensitivity of the calprotectin assays was similar despite inter-kit variability in absolute values. There is a need for f-Cp assay standardisation, but in its absence assay-specific cut-off values may optimise their diagnostic performance. F-S100A12 demonstrated comparable sensitivity and specificity to f-Cp and although a research tool at present, may have a future role to play in the diagnosis and management of these patients.
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Al-Bassam, Wasan W., Ali H. Ad'hiah, and Khadier Z. Mayouf. "Significance of calgranulins (S100A8, S100A9 and S100A12), ferritin and toll-like receptor 4 in juvenile idiopathic arthritis children." Egyptian Rheumatologist 42, no. 2 (April 2020): 147–52. http://dx.doi.org/10.1016/j.ejr.2019.08.005.
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Gohar, Faekah, Janneke Anink, Halima Moncrieffe, Lisette W. A. Van Suijlekom-Smit, Femke H. M. Prince, Marion A. J. van Rossum, Koert M. Dolman, et al. "S100A12 Is Associated with Response to Therapy in Juvenile Idiopathic Arthritis." Journal of Rheumatology 45, no. 4 (January 15, 2018): 547–54. http://dx.doi.org/10.3899/jrheum.170438.
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Objective.Around one-third of patients with juvenile idiopathic arthritis (JIA) fail to respond to first-line methotrexate (MTX) or anti-tumor necrosis factor (TNF) therapy, with even fewer achieving ≥ American College of Rheumatology Pediatric 70% criteria for response (ACRpedi70), though individual responses cannot yet be accurately predicted. Because change in serum S100-protein myeloid-related protein complex 8/14 (MRP8/14) is associated with therapeutic response, we tested granulocyte-specific S100-protein S100A12 as a potential biomarker for treatment response.Methods.S100A12 serum concentration was determined by ELISA in patients treated with MTX (n = 75) and anti-TNF (n = 88) at baseline and followup. Treatment response (≥ ACRpedi50 score), achievement of inactive disease, and improvement in Juvenile Arthritis Disease Activity Score (JADAS)-10 score were recorded.Results.Baseline S100A12 concentration was measured in patients treated with anti-TNF [etanercept n = 81, adalimumab n = 7; median 200, interquartile range (IQR) 133–440 ng/ml] and MTX (median 220, IQR 100–440 ng/ml). Of the patients in the anti-TNF therapy group, 74 (84%) were also receiving MTX. Responders to MTX (n = 57/75) and anti-TNF (n = 66/88) therapy had higher baseline S100A12 concentration compared to nonresponders: median 240 (IQR 125–615) ng/ml versus 150 (IQR 87–233) ng/ml, p = 0.021 for MTX, and median 308 (IQR 150–624) ng/ml versus 151 (IQR 83–201) ng/ml, p = 0.002, for anti-TNF therapy. Followup S100A12 could be measured in 44/75 MTX-treated patients (34/44 responders) and 39/88 anti-TNF-treated patients (26/39 responders). Responders had significantly reduced S100A12 concentration (MTX: p = 0.031, anti-TNF: p < 0.001) at followup versus baseline. Baseline serum S100A12 in both univariate and multivariate regression models for anti-TNF therapy and univariate analysis alone for MTX therapy was significantly associated with change in JADAS-10.Conclusion.Responders to MTX or anti-TNF treatment can be identified by higher pretreatment S100A12 serum concentration levels.