Journal articles: 'S100A2'

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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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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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Mitrović Ajtić, Olivera, Tijana Subotički, Miloš Diklić, Dragoslava Đikić, Milica Vukotić, Teodora Dragojević, Emilija Živković, Darko Antić, and Vladan Čokić. "Regulation of S100As Expression by Inflammatory Cytokines in Chronic Lymphocytic Leukemia." International Journal of Molecular Sciences 23, no. 13 (June 22, 2022): 6952. http://dx.doi.org/10.3390/ijms23136952.

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The calcium-binding proteins S100A4, S100A8, and S100A9 are upregulated in chronic lymphocytic leukemia (CLL), while the S100A9 promotes NF-κB activity during disease progression. The S100-protein family has been involved in several malignancies as mediators of inflammation and proliferation. The hypothesis of our study is that S100A proteins are mediators in signaling pathways associated with inflammation-induced proliferation, such as NF-κB, PI3K/AKT, and JAK/STAT. The mononuclear cells (MNCs) of CLL were treated with proinflammatory IL-6, anti-inflammatory IL-10 cytokines, inhibitors of JAK1/2, NF-κB, and PI3K signaling pathways, to evaluate S100A4, S100A8, S100A9, and S100A12 expression as well as NF-κB activation by qRT-PCR, immunocytochemistry, and immunoblotting. The quantity of S100A4, S100A8, and S100A9 positive cells (p < 0.05) and their protein expression (p < 0.01) were significantly decreased in MNCs of CLL patients compared to healthy controls. The S100A levels were generally increased in CD19+ cells compared to MNCs of CLL. The S100A4 gene expression was significantly stimulated (p < 0.05) by the inhibition of the PI3K/AKT signaling pathway in MNCs. IL-6 stimulated S100A4 and S100A8 protein expression, prevented by the NF-κB and JAK1/2 inhibitors. In contrast, IL-10 reduced S100A8, S100A9, and S100A12 protein expressions in MNCs of CLL. Moreover, IL-10 inhibited activation of NF-κB signaling (4-fold, p < 0.05). In conclusion, inflammation stimulated the S100A protein expression mediated via the proliferation-related signaling and balanced by the cytokines in CLL.

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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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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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Nguyen, Nam Q., Andrew Ruszkiewicz, David Chang, Jenna Bambrick, and Andrew Victor Biankin. "Biomarker assessment from EUS-guided biopsy to predict outcomes and treatment in pancreatic cancer." Journal of Clinical Oncology 32, no. 3_suppl (January 20, 2014): 182. http://dx.doi.org/10.1200/jco.2014.32.3_suppl.182.

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182 Background: Current methods of pre-operative predicting outcome of pancreatic cancer and related pancreatectomy are limited. While several prognostic biomarkers, including S100A2 and S100A4, are associated with poor outcomes, these currently can only be assessed in operatively resected specimens. The amount of tissue from EUS guided fine needle aspirations is often insufficient for biomarker assessment. Procore needles aim to acquire larger volumes of tissue that may be suitable. We aim to (i) evaluate the feasibility of S100A2 and S100A4 assessment in EUS guided biopsy specimens using the Procore needle, and (ii) evaluate the relationship of these biomarkers with outcome. Methods: Clinico-pathological data from 79 patients (70 ± 2yrs; 44M:35F) with pancreatic ductal adenocarcinoma (PDAC) were prospectively acquired. All subjects had EUS guided biopsy with a 22G Procore needle and cell-block preparation was performed. Sections of cell-block material were assessed for S100A2 and S100A4 protein expression using immunohistochemistry. Results: Pre-operative biomarker assessments from EUS acquired specimens were possible in 90% (72/79) of patients, 14 of which then had pancreatectomy. Thirty-five (49%) of patients expressed S100A2 and S100A4, which were co-expressed in 97% of cases. Patients with S100A2/A4 tumours on EUS had a significantly shorter median survival (10.0 vs. 17.5 months, p=0.03). Among patients with S100A2/A4 expressing tumors, pancreatectomy (n=8) didn't lead to a survival benefit compared with those managed non-surgically (n=27) (12.5 vs. 10.0 months, p=0.70). Of patients who had pancreatectomy, those with S100A2/A4 expressing tumors (n=8) had shorter survival than those with S100A2/A4-negative tumors (n=6) (12.5 vs. 20.5 months; p = 0.04). Conclusions: Biomarker assessment from EUS guided biopsy specimens is feasible and successful in 90% of cases. The presence of S100A2 and S100A4 expression predicts both survival and response to pancreatectomy in patients with pancreatic cancer. These findings demonstrate a “proof-of-concept”, that pre-operative EUS guided biopsy could inform clinical decision-making, particularly with regard to selection for operative resection of PDAC.

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Gupta, Sanjay, Tajamul Hussain, Gregory T. MacLennan, Pingfu Fu, Jigar Patel, and Hasan Mukhtar. "Differential Expression of S100A2 and S100A4 During Progression of Human Prostate Adenocarcinoma." Journal of Clinical Oncology 21, no. 1 (January 1, 2003): 106–12. http://dx.doi.org/10.1200/jco.2003.03.024.

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Purpose: To establish the clinical significance of calcium binding proteins S100A2 and S100A4 during progression of human prostate adenocarcinoma. Patients and Methods: Expression pattern of S100A2 and S100A4 was determined in normal human prostate epithelial cells (NHPE); virally transformed prostate epithelial cells (PZ-HPV-7); several human prostate carcinoma cells (22Rv1, DU145, LNCaP, and PC3); tissue samples obtained during transuretheral prostatic resection from patients with benign prostate hyperplasia (BPH), prostatitis, and adenocarcinoma; and paraffin-embedded sections from pair-matched benign and cancer specimens of different tumor grade. Results: High constitutive protein expression of S100A2 was observed in NHPE and PZ-HPV-7 cells, whereas its complete absence was observed in 22Rv1, DU145, LNCaP, and PC3 cells. Tissue samples of BPH and prostatitis exhibited higher mRNA and protein levels of S100A2 than low-grade cancer (Gleason score ≤ 6), whereas a complete loss was observed in high-grade cancer specimens (Gleason score > 6). Immunohistochemical analysis further confirmed high levels of S100A2 in benign tissues and a progressive loss with increasing tumor grade. The protein level of S100A4 was significantly higher in all carcinoma cells compared with NHPE and PZ-HPV-7 cells. The mRNA and protein level of S100A4 was significantly higher in high-grade cancer specimens compared with BPH, prostatitis, and low-grade cancer. The high levels of S100A4 observed in cancer tissue correlated with increasing tumor grade. Conclusion: Loss of S100A2 and increased expression of S100A4 may be an important event during progression of prostate cancer in humans.

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Yamamoto, Maho, Rina Kondo, Haruka Hozumi, Seita Doi, Miwako Denda, Masaki Magari, Naoki Kanayama, Naoya Hatano, Ryo Morishita, and Hiroshi Tokumitsu. "Identification and Biochemical Characterization of High Mobility Group Protein 20A as a Novel Ca2+/S100A6 Target." Biomolecules 11, no. 4 (March 30, 2021): 510. http://dx.doi.org/10.3390/biom11040510.

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During screening of protein-protein interactions, using human protein arrays carrying 19,676 recombinant glutathione s-transferase (GST)-fused human proteins, we identified the high-mobility protein group 20A (HMG20A) as a novel S100A6 binding partner. We confirmed the Ca2+-dependent interaction of HMG20A with S100A6 by the protein array method, biotinylated S100A6 overlay, and GST-pulldown assay in vitro and in transfected COS-7 cells. Co-immunoprecipitation of S100A6 with HMG20A from HeLa cells in a Ca2+-dependent manner revealed the physiological relevance of the S100A6/HMG20A interaction. In addition, HMG20A has the ability to interact with S100A1, S100A2, and S100B in a Ca2+-dependent manner, but not with S100A4, A11, A12, and calmodulin. S100A6 binding experiments using various HMG20A mutants revealed that Ca2+/S100A6 interacts with the C-terminal region (residues 311–342) of HMG20A with stoichiometric binding (HMG20A:S100A6 dimer = 1:1). This was confirmed by the fact that a GST-HMG20A mutant lacking the S100A6 binding region (residues 311–347, HMG20A-ΔC) failed to interact with endogenous S100A6 in transfected COS-7 cells, unlike wild-type HMG20A. Taken together, these results identify, for the first time, HMG20A as a target of Ca2+/S100 proteins, and may suggest a novel linkage between Ca2+/S100 protein signaling and HMG20A function, including in the regulation of neural differentiation.

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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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Zhu, Li, Futoshi Kohda, Takeshi Nakahara, Takahito Chiba, Gaku Tsuji, Junichi Hachisuka, Takamichi Ito, et al. "Aberrant expression of S100A6 and matrix metalloproteinase 9, but not S100A2, S100A4, and S100A7, is associated with epidermal carcinogenesis." Journal of Dermatological Science 72, no. 3 (December 2013): 311–19. http://dx.doi.org/10.1016/j.jdermsci.2013.07.005.

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Sugiyama, Takayuki, Tatsuya Takayama, Miki Miyazaki, Fumitake Kai, Naohiro Takaoka, Hiroshi Furuse, Soichi Mugiya, and Seiichiro Ozono. "Evaluation of the expression levels of S100A2 mRNA in renal cell carcinoma." Journal of Clinical Oncology 30, no. 5_suppl (February 10, 2012): 457. http://dx.doi.org/10.1200/jco.2012.30.5_suppl.457.

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457 Background: The human S100 proteins are a calcium-binding protein comprising around 20 sort, at least 16 of these genes included pseudogenes are clustering to chromosome 1q21 , known as the epidermal differentiation complex. We have reported that S100A1 and A10 are expressed in human renal cell carcinoma (RCC) (Teratani T et al; Cancer Lett 2002, Teratani T, et al; BBRC 2002, Domoto, et al Cancer Sci. 2007). Diminished expression of S100A2 has been reported in some kinds of cancers (ex. lung, breast, prostate), but not reported in renal cell carcinoma (RCC). The aim of the present study is to evaluate the expression level S100A2 mRNA in human renal cell carcinoma. Methods: Sixty-one patients, pathologically diagnosed for clear cell RCC performed nephrectomy, were used in this study. Genomic DNA and RNA were extracted from RCC part and matched normal part in each patient. First-strand cDNA was synthesized from 2 micrograms RNA using Superscript-2 reverse transcriptase (Invitorgen), and reverse transcription polymerase chain reaction (RT-PCR) were performed using specific primers for S100A2. We also check the CpG methylation in the promoter region of the S100A2 gene using COBRA assay (combined bisulfite restriction analysis). Results: 45 cases (73%) showed decreased S100A2 expression in RCC parts. In53 cases of clear cell RCC, S100A2 expression decreased in fourty-two (79%) cases. In contrast clear cell RCC, 5 cases showed expression S100A2 in non-clear RCC (8cases; 62%), and 2 cases of clear cell RCC in VHL disease patients also had expression of S100A2. 30 cases of clear cell RCC were used in COBRA assay, S100A2 methylation were seen in all cases. Conclusions: Diminished expression of S100A2 is frequently shows in RCC, especially clear cell RCC. It suggests that property of clear cell RCC is different from other type of RCC.

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Holmannová, Drahomíra, Barbora Císařová, Pavel Borský, Zdeněk Fiala, Ctirad Andrýs, Květoslava Hamaková, Tereza Švadláková, et al. "Goeckerman Regimen Reduces Alarmin Levels and PASI Score in Paediatric Patients with Psoriasis." Acta Medica (Hradec Kralove, Czech Republic) 64, no. 4 (2021): 204–12. http://dx.doi.org/10.14712/18059694.2022.3.

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Background. Psoriasis is a chronic systemic inflammatory disease with (extra-)cutaneous manifestations. Inflammation is associated with cellular stress and tissue damage which lead to the release of alarmins (signals of danger). Goeckerman regimen (GR) is a highly efficacious treatment consisting of the application of pharmaceutical crude tar and UVB light exposure. The reduction of inflammatory processes in the skin is accompanied by changes in the levels of inflammatory markers - alarmins (HMBG-1, S100A7, S1000A8, S100A9, S100A12, IL-17, IL-22, and IL-33). Methods. The alarmin levels in sera of 19 paediatric patients with psoriasis were determined before and after GR using commercial ELISA kits. The Psoriasis area severity index (PASI) was used to determine the disease severity. Results. GR reduced both PASI and the levels of all measured alarmins. The levels of S100A7, S100A9, IL-22, IL-33, and HMGB-1 were significantly decreased. Positive correlations between IL-22 and PASI, between S100A9 and IL-17, S100A9 and IL-22, and a negative correlation between S100A8 and IL-33 were found. Conclusions. Goeckerman regimen is a very effective, safe and low-cost therapy. We confirmed, it modulates the immune system reactivity, ameliorates the severity of the disease and reduces the levels of alarmins reflecting the presence and intensity of inflammation.

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Ito, Y., H. Yoshida, C. Tomoda, T. Uruno, A. Miya, K. Kobayashi, F. Matsuzuka, K. Kakudo, K. Kuma, and A. Miyauchi. "Expression of S100A2 and S100A6 in thyroid carcinomas." Histopathology 46, no. 5 (May 2005): 569–75. http://dx.doi.org/10.1111/j.1365-2559.2005.02137.x.

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Chang, D. K., E. K. Colvin, C. J. Scarlett, M. Pajic, M. Pinese, A. J. Gill, E. A. Musgrove, R. Sutherland, J. Kench, and A. V. Biankin. "A molecular prognostic nomogram for resectable pancreatic cancer." Journal of Clinical Oncology 29, no. 4_suppl (February 1, 2011): 154. http://dx.doi.org/10.1200/jco.2011.29.4_suppl.154.

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154 Background: Defining clinically and biologically relevant phenotypes in other cancers has led to substantial improvements in the overall outcomes, but as yet none have been defined for pancreatic cancer (PC). About 80% of patients with pancreatic cancer succumb to the disease despite curative resection, many of whom within 6 months of surgery. There is a clear need to better define the biology and clinical behaviour of PC. This study aimed to evaluate the potential clinical utility of biologically relevant molecules as prognostic factors in resected PC. Methods: We assessed the relationship of aberrant S100A4 calcium-binding protein expression with survival in a cohort of 372 patients who underwent surgical resection for PC and derived a nomogram using clinicopathologic variables and aberrant expression of S100A4 and S100A2. Results: High S100A4 expression was an independent poor prognostic factor in both the training (n = 76; HR = 5.00, 95% CI = 2.29 – 10.9; p < 0.0001) and validation sets (n = 296; HR = 1.78, 95% CI = 1.29 – 2.46; p = 0.0004). Incorporating previously published data on S100A2, demonstrated that high expression of S100A4 was still an independent prognostic factor. Aberrant expression of these proteins stratified the cohort into three distinct prognostic groups. A preoperative nomogram using only variables that could be measured preoperatively (tumor size and molecular biomarkers), predicted survival better than nomograms derived from using clinicopathologic variables, which are only determined after examination of the resected specimen. Conclusions: Aberrant expression of S100A4 and S100A2 stratifies PC into distinct prognostic groups and improves the accuracy of prognostic nomograms using variables that can be determined preoperatively. The development and application of such nomograms in routine clinical practice has the potential to improve patient selection and as a consequence overall outcomes for PC. No significant financial relationships to disclose.

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Roszkowski, Leszek, Bożena Jaszczyk, Magdalena Plebańczyk, and Marzena Ciechomska. "S100A8 and S100A12 Proteins as Biomarkers of High Disease Activity in Patients with Rheumatoid Arthritis That Can Be Regulated by Epigenetic Drugs." International Journal of Molecular Sciences 24, no. 1 (December 31, 2022): 710. http://dx.doi.org/10.3390/ijms24010710.

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Rheumatoid arthritis (RA) is an autoimmune chronic inflammatory disease that is still not well understood in terms of its pathogenesis and presents diagnostic and therapeutic challenges. Monocytes are key players in initiating and maintaining inflammation through the production of pro-inflammatory cytokines and S100 proteins in RA. This study aimed to test a specific DNA methylation inhibitor (RG108) and activator (budesonide) in the regulation of pro-inflammatory mediators—especially the S100 proteins. We also searched for new biomarkers of high disease activity in RA patients. RNA sequencing analysis of healthy controls (HCs) and RA monocytes was performed. Genes such as the S100 family, TNF, and IL-8 were validated by qRT-PCR following DNA-methylation-targeted drug treatment in a monocytic THP-1 cell line. The concentrations of the S100A8, S100A11, and S100A12 proteins in the sera and synovial fluids of RA patients were tested and correlated with clinical parameters. We demonstrated that RA monocytes had significantly increased levels of S100A8, S100A9, S100A11, S100A12, MYD88, JAK3, and IQGAP1 and decreased levels of IL10RA and TGIF1 transcripts. In addition, stimulation of THP-1 cells with budesonide statistically reduced the expression of the S100 family, IL-8, and TNF genes. In contrast, THP-1 cells treated with RG108 had increased levels of the S100 family and TNF genes. We also revealed a significant upregulation of S100A8, S100A11, and S100A12 in RA patients, especially in early RA compared to HC sera. In addition, protein levels of S100A8, S100A11, and S100A12 in RA synovial fluids compared to HC sera were significantly increased. Overall, our data suggest that the S100A8 and S100A12 proteins are strongly elevated during ongoing inflammation, so they could be used as a better biomarker of disease activity than CRP. Interestingly, epigenetic drugs can regulate these S100 proteins, suggesting their potential use in targeting RA inflammation.

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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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Roszkowski, L., B. Jaszczyk, and M. Ciechomska. "AB0058 NOVEL BIOMARKERS FROM THE S100 PROTEIN FAMILY OF RHEUMATOID ARTHRITIS PROGRESSION WHICH CAN BE REGULATED BY EPIGENETIC DRUGS." Annals of the Rheumatic Diseases 82, Suppl 1 (May 30, 2023): 1208.2–1208. http://dx.doi.org/10.1136/annrheumdis-2023-eular.549.

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BackgroundMonocytes are key players in initiating and maintaining inflammation by producing proinflammatory cytokines and S100 proteins in rheumatoid arthritis (RA). Several studies demonstrated that epigenetic drugs affecting DNA methylation can modulate the production of proinflammatory mediators.ObjectivesThis study aimed to test specific DNA methylation inhibitor (RG108) and activator (budesonide) in the regulation of proinflammatory cytokines and S100 proteins in RA monocytes. Our study also looked for new and better biomarkers of high disease activity in RA patients.MethodsRNA sequencing (RNA-seq) analysis of healthy controls (HC) and RA monocytes was performed. Cell viability was determined in THP-1 monocytic cell line following RG108 and budesonide treatment. Pro- and anti-inflammatory genes such as the S100 family, TNF, IL-8 were validated by qRT-PCR following DNA methylation-targeted drug treatment. The concentrations of proteins from the S100 family in serum and synovial fluid were tested with ELISA assays and their correlation with clinical parameters was carried out.ResultsBased on the RNA-seq analysis, RA monocytes had significantly increased levels of S100A8 (2,2-fold, p=0,024), S100A9 (1,9-fold, p=0,017), S100A11 (1,2-fold, p=0,007), S100A12 (1,6-fold, p=0,007), MYD88 (1,2-fold, p=0,008), JAK3 (1,8-fold, p=0,009), IQGAP1 (1,4-fold, p=0,02), and decreased level of IL10RA (0,7-fold, p=0,011), TGIF1 (0,3-fold, p=0,046) transcripts. In addition, stimulation of THP-1 cells with budesonide (DNA methylation activator) statistically reduced expression of S100A8 (3,0-fold, p= 0,0390), S100A9 (4,4-fold, p= 0,0317), S100A12 (3,3-fold, p= 0,0260), IL-8 (6,8-fold, p= 0,0286) and TNF (7,5-fold, p= 0,0260) genes. In contrast, THP-1 monocytic cell line treated with RG108 (DNA methylation inhibitor) had an increased level of S100 family (S100A8, -A9, -A11, -A12) and TNF genes. ELISAs analysis also revealed significant increased levels of S100A8 (p = 0.0116), S100A11 (p = 0.0138), and S100A12 (p = 0.0296) proteins in RA patients compared to HC sera, similar in early RA sera compared to HC S100A8 (p = 0.0024), S100A11 (p = 0.0020) and S100A12 (p = 0.0059). Moreover, protein levels of S100A8 (p=0.0005), S100A11 (p=0.0007) and S100A12 (p=0.0005) in the synovial fluid of advanced RA patients compared to HC serum were significantly elevated. All these data suggest that a protein of the S100 family may be a promising biomarker of RA progression. In ROC analyses, serum levels of S100A8 and S100A12 proteins were more specific {area under the curve (AUC)=0.78, p=0.006 and AUC=0.87, p=0.0006} respectively in RA patients than CRP levels. In addition, results indicate that S100A8 and S100A12 can serve as a better biomarker of high disease activity than CRP levels.ConclusionWe have demonstrated that S100 family proteins are increased in RA monocytes (transcriptomics) similar to enhanced S100 production in sera and synovial fluids (ELISA) in RA patients. Our data suggest that the proteins S100A8 and S100A12 in particular are strongly increased during ongoing inflammation, so they could be used as a better biomarker of disease activity than CRP. Interestingly, S100 proteins can be regulated by epigenetic drugs, suggesting their potential use in the targeting of RA inflammation.AcknowledgementsThis work was supported by a grant from National Science Centre (2018/30/E/NZ5/00104).Disclosure of InterestsNone Declared.

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Wang, Huiling, Xin Hu, Feng Yang, and Hui Xiao. "miR-325-3p Promotes the Proliferation, Invasion, and EMT of Breast Cancer Cells by Directly Targeting S100A2." Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics 28, no. 7 (September 7, 2021): 731–44. http://dx.doi.org/10.3727/096504020x16100888208039.

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This study was designed to investigate the precise mechanisms of miR-325-3p/S100A2 axis in breast cancer (BC). In this study, we found that the level of miR-325-3p was dramatically increased in BC tissues and cell lines, and the expression of S100A2 was significantly decreased. Also, the high level of miR-325-3p was closely associated with low expression of S100A2 in BC tissues. Moreover, introduction of miR-325-3p significantly promoted proliferation, invasion, and EMT of BC cells. Bioinformatics analysis predicted that the S100A2 was a potential target gene of miR-325-3p. Luciferase reporter assay demonstrated that miR-325-3p could directly target S100A2. In addition, miR-325-3p overexpression had similar effects with knockdown of S100A2 on BC cells. Overexpression of S100A2 in BC cells partially reversed the promoted effects of miR-325-3p mimic. Overexpression of miR-325-3p promoted cell proliferation, invasion, and EMT of BC cells by directly downregulating S100A2 expression.

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Naz, Sarwat, Prathibha Ranganathan, Priyanka Bodapati, Arun H. Shastry, Laxmi N. Mishra, and Paturu Kondaiah. "Regulation of S100A2 expression by TGF-β-induced MEK/ERK signalling and its role in cell migration/invasion." Biochemical Journal 447, no. 1 (September 12, 2012): 81–91. http://dx.doi.org/10.1042/bj20120014.

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S100A2, an EF hand calcium-binding protein, is a potential biomarker in several cancers and is also a TGF-β (transforming growth factor-β)-regulated gene in melanoma and lung cancer cells. However, the mechanism of S100A2 regulation by TGF-β and its significance in cancer progression remains largely unknown. In the present study we report the mechanism of S100A2 regulation by TGF-β and its possible role in TGF-β-mediated tumour promotion. Characterization of the S100A2 promoter revealed an AP-1 (activator protein-1) element at positions −1161 to −1151 as being the most critical factor for the TGF-β1 response. Chromatin immunoprecipitation and electrophoretic mobility-shift assays confirmed the functional binding of the AP-1 complex, predominantly JunB, to the S100A2 promoter in response to TGF-β1 in HaCaT keratinocytes. JunB overexpression markedly stimulated the S100A2 promoter which was blocked by the dominant–negative JunB and MEK1 [MAPK (mitogen-activated protein kinase)/ERK (extracellular-signal-regulated kinase) kinase 1] inhibitor, PD98059. Intriguingly, despite the presence of a putative SMAD-binding element, S100A2 regulation by TGF-β1 was found to be SMAD3 independent. Interestingly, p53 protein and TGF-β1 show synergistic regulation of the S100A2 promoter. Finally, knockdown of S100A2 expression compromised TGF-β1-induced cell migration and invasion of Hep3B cells. Together our findings highlight an important link between the TGF-β1-induced MAPK and p53 signalling pathways in the regulation of S100A2 expression and pro-tumorigenic actions.

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Mandinova, A., D. Atar, B. W. Schafer, M. Spiess, U. Aebi, and C. W. Heizmann. "Distinct subcellular localization of calcium binding S100 proteins in human smooth muscle cells and their relocation in response to rises in intracellular calcium." Journal of Cell Science 111, no. 14 (July 30, 1998): 2043–54. http://dx.doi.org/10.1242/jcs.111.14.2043.

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Changes in cytosolic Ca2+ concentration control a wide range of cellular responses, and intracellular Ca2+-binding proteins are the key molecules to transduce Ca2+ signaling via interactions with different types of target proteins. Among these, S100 Ca2+-binding proteins, characterized by a common structural motif, the EF-hand, have recently attracted major interest due to their cell- and tissue-specific expression pattern and involvement in various pathological processes. The aim of our study was to identify the subcellular localization of S100 proteins in vascular smooth muscle cell lines derived from human aorta and intestinal smooth muscles, and in primary cell cultures derived from arterial smooth muscle tissue under normal conditions and after stimulation of the intracellular Ca2+ concentration. Confocal laser scanning microscopy was used with a specially designed colocalization software. Distinct intracellular localization of S100 proteins was observed: S100A6 was present in the sarcoplasmic reticulum as well as in the cell nucleus. S100A1 and S100A4 were found predominantly in the cytosol where they were strongly associated with the sarcoplasmic reticulum and with actin stress fibers. In contrast, S100A2 was located primarily in the cell nucleus. Using a sedimentation assay and subsequent electron microscopy after negative staining, we demonstrated that S100A1 directly interacts with filamentous actin in a Ca2+-dependent manner. After thapsigargin (1 microM) induced increase of the intracellular Ca2+ concentration, specific vesicular structures in the sarcoplasmic reticulum region of the cell were formed with high S100 protein content. In conclusion, we demonstrated a distinct subcellular localization pattern of S100 proteins and their interaction with actin filaments and the sarcoplasmic reticulum in human smooth muscle cells. The specific translocation of S100 proteins after intracellular Ca2+ increase supports the hypothesis that S100 proteins exert several important functions in the regulation of Ca2+ homeostasis in smooth muscle cells.

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Gimona, M., Z. Lando, Y. Dolginov, J. Vandekerckhove, R. Kobayashi, A. Sobieszek, and D. M. Helfman. "Ca2+-dependent interaction of S100A2 with muscle and nonmuscle tropomyosins." Journal of Cell Science 110, no. 5 (March 1, 1997): 611–21. http://dx.doi.org/10.1242/jcs.110.5.611.

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Zero-length chemical crosslinking with 1-ethyl-3-[3-(dimethyl amino)propyl]carbodiimide (EDC) indicated an association of the Ca2+-binding protein S100A2 with tropomyosin (TM) in vitro. The mobility of the crosslinked product on SDS-PAGE gels indicated the formation of a 1:1 complex between S100A2 and TM and the interaction was Ca2+ dependent. Monoclonal antibodies were raised against S100A2 and used to determine its cellular localization in the porcine epithelial cell line LLC PK1. It was found that the localization of S100A2 depended on the differentiation state of the cells, being absent from actin stress fibers in sparsely seeded cultures, but present in the actin-containing microvilli characteristic of differentiated cells. Immunoprecipitations of [35S]methionine-labeled extracts using S100A2 as well as TM-specific antibodies failed to co-precipitate TM and S100A2, indicating a transient association between these two molecules in solution. Affinity chromatography of cell extracts on immobilized recombinant TMs, however, confirmed the Ca2+-dependent interaction between S100A2 and both muscle TMs as well as with high and low molecular mass nonmuscle TMs, suggesting that the binding site resides in one of the conserved regions of TM. Our data demonstrate the possible interaction of S100A2 with TM that is not bound to the microfilaments and indicate a differentiation-related function for S100A2 in LLC PK1 cells. The possible functional implications of this interaction are discussed.

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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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Lee, Ok-Jae, Seung-Mo Hong, Mohammad H. Razvi, Dunfa Peng, Steven M. Powell, Mark Smoklin, Christopher A. Moskaluk, and Wael El-Rifai. "Expression of Calcium-Binding Proteins S100A2, S100A4 in Barrett's Adenocarcinomas." Neoplasia 8, no. 10 (October 2006): 843–50. http://dx.doi.org/10.1593/neo.06481.

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Wasuworawong, Kasima, Sittiruk Roytrakul, Atchara Paemanee, Kattaleeya Jindapornprasert, and Waraporn Komyod. "Comparative Proteomic Analysis of Human Cholangiocarcinoma Cell Lines: S100A2 as a Potential Candidate Protein Inducer of Invasion." Disease Markers 2015 (2015): 1–6. http://dx.doi.org/10.1155/2015/629367.

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Cholangiocarcinoma (CCA) is a bile duct cancer, commonly found in Asia including Thailand and especially in the northeastern region of Thailand. To identify the proteins involved in carcinogenesis and metastasis of CCA, protein expression profiles of high-invasive KKU-M213 and low-invasive KKU-100 cell lines were compared using a comparative GeLC-MS/MS proteomics analysis. A total of 651 differentially expressed proteins were detected of which 27 protein candidates were identified as having functions involved in cell motility. A total of 22 proteins were significantly upregulated in KKU-M213, whereas 5 proteins were downregulated in KKU-M213. S100A2, a calcium-binding protein in S100 protein family, is upregulated in KKU-M213. S100A2 is implicated in metastasis development in several cancers. The protein expression level of S100A2 was verified by Western blot analysis. Intriguingly, high-invasive KKU-M213 cells showed higher expression of S100A2 than KKU-100 cells, consistent with proteomic data, suggesting that S100A2 may be a key protein involved in the progression of CCA. However, the biological function of S100A2 in cholangiocarcinoma remains to be elucidated. S100A2 might be a potential biomarker as well as a novel therapeutic target in CCA metastasis.

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Klopper, Joshua P., Vibha Sharma, Reid Bissonnette, and Bryan R. Haugen. "Combination PPARγand RXR Agonist Treatment in Melanoma Cells: Functional Importance of S100A2." PPAR Research 2010 (2010): 1–8. http://dx.doi.org/10.1155/2010/729876.

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Nuclear hormone receptors, including RXR and PPARγ, represent novel therapeutic targets in melanoma. We have previously shown that the DRO subline of the amelanotic melanoma A375 responds to rexinoid and thiazolidinedione (TZD) treatmentin vitroandin vivo. We performed microarray analysis of A375(DRO) after TZD and combination rexinoid/TZD treatment in which the calcium binding protein S100A2 had increased expression after rexinoid or TZD treatment and a synergistic increase to combination treatment. Increased S100A2 expression is dependent on an intact PPARγreceptor, but it is not sufficient to mediate the antiproliferative effects of rexinoid/TZD treatment. Over expression of S100A2 enhanced the effect of rexinoid and TZD treatment while inhibition of S100A2 expression attenuated the response to rexinoid/TZD treatment, suggesting that S100A2 is necessary for optimal response to RXR and PPARγactivation by respective ligands. In summary, we have identified potential downstream mediators of rexinoid and TZD treatment in a poorly differentiated melanoma and found that alterations in S100A2 expression affect RXR and PPARγsignaling in A375(DRO) cells. These studies provide insight into potential mechanisms of tumor response or resistance to these novel therapies.

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Sugino, Hitomi, and Yu Sawada. "Influence of S100A2 in Human Diseases." Diagnostics 12, no. 7 (July 20, 2022): 1756. http://dx.doi.org/10.3390/diagnostics12071756.

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S100 proteins are a family of low-molecular-weight proteins characterized by two calcium-binding sites with a helix-loop-helix (“EF-hand-type”) domain. The S100 family of proteins is distributed across various organs and can interact with diverse molecules. Among the proteins of the S100 family, S100 calcium-binding protein A2 (S100A2) has been identified in mammary epithelial cells, glands, lungs, kidneys, and prostate gland, exhibiting various physiological and pathological actions in human disorders, such as inflammatory diseases and malignant tumors. In this review, we introduce basic knowledge regarding S100A2 regulatory mechanisms. Although S100A2 is a tumor suppressor, we describe the various influences of S100A2 on cancer and inflammatory diseases.

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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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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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Delangre, Etienne, Ezia Oppliger, Serkan Berkcan, Monika Gjorgjieva, Marta Correia de Sousa, and Michelangelo Foti. "S100 Proteins in Fatty Liver Disease and Hepatocellular Carcinoma." International Journal of Molecular Sciences 23, no. 19 (September 20, 2022): 11030. http://dx.doi.org/10.3390/ijms231911030.

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Non-alcoholic fatty liver disease (NAFLD) is a highly prevalent and slow progressing hepatic pathology characterized by different stages of increasing severity which can ultimately give rise to the development of hepatocellular carcinoma (HCC). Besides drastic lifestyle changes, few drugs are effective to some extent alleviate NAFLD and HCC remains a poorly curable cancer. Among the deregulated molecular mechanisms promoting NAFLD and HCC, several members of the S100 proteins family appear to play an important role in the development of hepatic steatosis, non-alcoholic steatohepatitis (NASH) and HCC. Specific members of this Ca2+-binding protein family are indeed significantly overexpressed in either parenchymal or non-parenchymal liver cells, where they exert pleiotropic pathological functions driving NAFLD/NASH to severe stages and/or cancer development. The aberrant activity of S100 specific isoforms has also been reported to drive malignancy in liver cancers. Herein, we discuss the implication of several key members of this family, e.g., S100A4, S100A6, S100A8, S100A9 and S100A11, in NAFLD and HCC, with a particular focus on their intracellular versus extracellular functions in different hepatic cell types. Their clinical relevance as non-invasive diagnostic/prognostic biomarkers for the different stages of NAFLD and HCC, or their pharmacological targeting for therapeutic purpose, is further debated.

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Kwon, Yong-Wook, In Ho Chang, Kyung Do Kim, Young Sun Kim, Soon-Chul Myung, Mi-Kyung Kim, and Tae-Hyoung Kim. "Significance of S100A2 and S100A4 Expression in the Progression of Prostate Adenocarcinoma." Korean Journal of Urology 51, no. 7 (2010): 456. http://dx.doi.org/10.4111/kju.2010.51.7.456.

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Kizawa, K., M. Toyoda, M. Ito, and M. Morohashi. "Aberrantly differentiated cells in benign pilomatrixoma reflect the normal hair follicle: immunohistochemical analysis of Ca2+-binding S100A2, S100A3 and S100A6 proteins." British Journal of Dermatology 152, no. 2 (February 2005): 314–20. http://dx.doi.org/10.1111/j.1365-2133.2004.06391.x.

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Rehman, Ishtiaq, Simon S. Cross, James W. F. Catto, Aaron Leiblich, Abir Mukherjee, Abdel-Rahmene Azzouzi, Hing Y. Leung, and Freddie C. Hamdy. "Promoter hyper-methylation of calcium binding proteins S100A6 and S100A2 in human prostate cancer." Prostate 65, no. 4 (December 1, 2005): 322–30. http://dx.doi.org/10.1002/pros.20302.

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Koch, Michael, Shibani Bhattacharya, Torsten Kehl, Mario Gimona, Milan Vašák, Walter Chazin, Claus W. Heizmann, Peter M. H. Kroneck, and Günter Fritz. "Implications on zinc binding to S100A2." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1773, no. 3 (March 2007): 457–70. http://dx.doi.org/10.1016/j.bbamcr.2006.12.006.

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Li, Changyou, Siyuan Li, Changkai Jia, Lingling Yang, Zicheng Song, and Yiqiang Wang. "Low Concentration of S100A8/9 Promotes Angiogenesis-Related Activity of Vascular Endothelial Cells: Bridges among Inflammation, Angiogenesis, and Tumorigenesis?" Mediators of Inflammation 2012 (2012): 1–8. http://dx.doi.org/10.1155/2012/248574.

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Previous studies showed that several members of the S100A family are involved in neovascularization and tumor development. This study checked whether low concentrations of S100A8 or S100A9 has any effect on the behaviour of vascular endothelial cells. A human umbilical vascular endothelial cell (HUVEC) line was used to measure vascular endothelial cell bioactivity related to angiogenesis, such as cell proliferation, migration, and vessel formation. In the low concentration range up to 10 μg/mL, either each alone or in combination, S100A8 and S100A9 proteins promoted proliferation of HUVEC cells in a dose-dependent manner. The presence of both proteins in culture showed additive effects over each single protein. Both proteins enhanced HUVEC cells to migrate across the transwell membrane and to form tube-like structures on the Matrigel surface. When mixed in Matrigel and injected subcutaneously in Balb/c mice, both proteins increased vessel development in the gel plugs. Microarray assay of HUVEC cells treated with 10 μg/mL S100A8 revealed that ribosome pathway, pathogenicEscherichia coliinfection pathway, apoptosis, and stress response genes were modulated by S100A8 treatment. We propose that S100A8 and S100A9 proteins from either infiltrating inflammatory cells or tumor cells play an important role in the interplay among inflammation, angiogenesis, and tumorigenesis.

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Matsumoto, Kazumasa, Akira Irie, Takefumi Satoh, Junichiro Ishii, Keiichi Iwabuchi, Masatsugu Iwamura, Shin Egawa, and Shiro Baba. "Expression of S100A2 and S100A4 Predicts for Disease Progression and Patient Survival in Bladder Cancer." Urology 70, no. 3 (September 2007): 602–7. http://dx.doi.org/10.1016/j.urology.2007.04.007.

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Moravkova, Paula, Darina Kohoutova, Jaroslava Vavrova, and Jan Bures. "Serum S100A6, S100A8, S100A9 and S100A11 proteins in colorectal neoplasia: results of a single centre prospective study." Scandinavian Journal of Clinical and Laboratory Investigation 80, no. 3 (December 19, 2019): 173–78. http://dx.doi.org/10.1080/00365513.2019.1704050.

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Moravkova, Paula, Darina Kohoutova, Jaroslava Vávrová, and Jan Bures. "Tu1943 - Serum S100A6, S100A8, S100A9 and S100A11 in Colorectal Neoplasia: Results of a Single Centre Prospective Study." Gastroenterology 154, no. 6 (May 2018): S—1060—S—1061. http://dx.doi.org/10.1016/s0016-5085(18)33546-7.

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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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Fuh, Kenneth F., Jessica Withell, Robert D. Shepherd, and Kristina D. Rinker. "Fluid Flow Stimulation Modulates Expression of S100 Genes in Normal Breast Epithelium and Breast Cancer." Cellular and Molecular Bioengineering 15, no. 1 (October 27, 2021): 115–27. http://dx.doi.org/10.1007/s12195-021-00704-w.

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Abstract Introduction S100 proteins are intracellular calcium ion sensors that participate in cellular processes, some of which are involved in normal breast functioning and breast cancer development. Despite several S100 genes being overexpressed in breast cancer, their roles during disease development remain elusive. Human mammary epithelial cells (HMECs) can be exposed to fluid shear stresses and implications of such interactions have not been previously studied. The goal of this study was to analyze expression profiles of S100 genes upon exposing HMECs to fluid flow. Methods HMECs and breast cancer cell lines were exposed to fluid flow in a parallel-plate bioreactor system. Changes in gene expression were quantified using microarrays and qPCR, gene-gene interactions were elucidated using network analysis, and key modified genes were examined in three independent clinical datasets. Results S100 genes were among the most upregulated genes upon flow stimulation. Network analysis revealed interactions between upregulated transcripts, including interactions between S100P, S100PBP, S100A4, S100A7, S100A8 and S100A9. Overexpression of S100s was also observed in patients with early stage breast cancer compared to normal breast tissue, and in most breast cancer patients. Finally, survival analysis revealed reduced survival times for patients with elevated expression of S100A7 and S100P. Conclusion This study shows that exposing HMECs to fluid flow upregulates genes identified clinically to be overexpressed during breast cancer development, including S100A7 and S100P. These findings are the first to show that S100 genes are flow-responsive and might be participating in a fundamental adaptation pathway in normal tissue that is also active in breast cancer.

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Tsvetkov, P. O., F. Devred, and A. A. Makarov. "Thermodynamics of zinc binding to human S100A2." Molecular Biology 44, no. 5 (October 2010): 832–35. http://dx.doi.org/10.1134/s0026893310050213.

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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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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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Koch, Michael, Joachim Diez, Armin Wagner, and Günter Fritz. "Crystallization and calcium/sulfur SAD phasing of the human EF-hand protein S100A2." Acta Crystallographica Section F Structural Biology and Crystallization Communications 66, no. 9 (August 26, 2010): 1032–36. http://dx.doi.org/10.1107/s1744309110030691.

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Human S100A2 is an EF-hand protein and acts as a major tumour suppressor, binding and activating p53 in a Ca2+-dependent manner. Ca2+-bound S100A2 was crystallized and its structure was determined based on the anomalous scattering provided by six S atoms from methionine residues and four calcium ions present in the asymmetric unit. Although the diffraction data were recorded at a wavelength of 0.90 Å, which is usually not assumed to be suitable for calcium/sulfur SAD, the anomalous signal was satisfactory. A nine-atom substructure was determined at 1.8 Å resolution usingSHELXD, andSHELXEwas used for density modification and phase extension to 1.3 Å resolution. The electron-density map obtained was well interpretable and could be used for automated model building byARP/wARP.

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Haase-Kohn, Cathleen, Susann Wolf, Jens Lenk, and Jens Pietzsch. "Copper-mediated cross-linking of S100A4, but not of S100A2, results in proinflammatory effects in melanoma cells." Biochemical and Biophysical Research Communications 413, no. 3 (September 2011): 494–98. http://dx.doi.org/10.1016/j.bbrc.2011.08.132.

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Wang, Ting, Yiqian Liang, Asmitananda Thakur, Shuo Zhang, Tian Yang, Tianjun Chen, Lei Gao, Mingwei Chen, and Hui Ren. "Diagnostic significance of S100A2 and S100A6 levels in sera of patients with non-small cell lung cancer." Tumor Biology 37, no. 2 (September 11, 2015): 2299–304. http://dx.doi.org/10.1007/s13277-015-4057-z.

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Kazakov, Alexey S., Evgenia I. Deryusheva, Andrey S. Sokolov, Maria E. Permyakova, Ekaterina A. Litus, Victoria A. Rastrygina, Vladimir N. Uversky, Eugene A. Permyakov, and Sergei E. Permyakov. "Erythropoietin Interacts with Specific S100 Proteins." Biomolecules 12, no. 1 (January 12, 2022): 120. http://dx.doi.org/10.3390/biom12010120.

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Erythropoietin (EPO) is a clinically significant four-helical cytokine, exhibiting erythropoietic, cytoprotective, immunomodulatory, and cancer-promoting activities. Despite vast knowledge on its signaling pathways and physiological effects, extracellular factors regulating EPO activity remain underexplored. Here we show by surface plasmon resonance spectroscopy, that among eighteen members of Ca2+-binding proteins of the S100 protein family studied, only S100A2, S100A6 and S100P proteins specifically recognize EPO with equilibrium dissociation constants ranging from 81 nM to 0.5 µM. The interactions occur exclusively under calcium excess. Bioinformatics analysis showed that the EPO-S100 interactions could be relevant to progression of neoplastic diseases, including cancer, and other diseases. The detailed knowledge of distinct physiological effects of the EPO-S100 interactions could favor development of more efficient clinical implications of EPO. Summing up our data with previous findings, we conclude that S100 proteins are potentially able to directly affect functional activities of specific members of all families of four-helical cytokines, and cytokines of other structural superfamilies.

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Wolf, Susann, Cathleen Haase-Kohn, and Jens Pietzsch. "S100A2 in cancerogenesis: a friend or a foe?" Amino Acids 41, no. 4 (June 3, 2010): 849–61. http://dx.doi.org/10.1007/s00726-010-0623-2.

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Liu, Ying-Fu, Qing-Qing Liu, Xuan Wang, and Chun-Hua Luo. "Clinical significance of S100A2 expression in gastric cancer." Tumor Biology 35, no. 4 (December 7, 2013): 3731–41. http://dx.doi.org/10.1007/s13277-013-1495-3.

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Heo, Sun-Hee, Young-Jin Choi, Ji-Hyun Lee, Jae-Mok Lee, and Je-Yoel Cho. "S100A2 level changes are related to human periodontitis." Molecules and Cells 32, no. 5 (September 9, 2011): 445–50. http://dx.doi.org/10.1007/s10059-011-0132-5.

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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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Journal articles on the topic 'S100A2'

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