Serum S100A6, S100A8, S100A9 and S100A11 proteins in colorectal neoplasia: results of a single centre prospective study

References

• International Agency for Research on Cancer. GLOBOCAN 2012: Estimated Cancer Incidence, Mortality and Prevalence Worldwide in 2012, IARC, Lyon, France, 2013. [online]. Available from: http://globocan.iarc.fr/Pages/fact_sheets_population.aspx.
   Google Scholar
• Zhang J, Cheng Z, Ma Y, et al. Effectiveness of screening modalities in colorectal cancer: a network meta-analysis. Clin Colorectal Cancer. 2017;16(4):252–263.
   PubMed Web of Science ®Google Scholar
• Ferlay J, Colombet M, Soerjomataram I, et al. Cancer incidence and mortality patterns in Europe: Estimates for 40 countries and 25 major cancers in 2018. Eur J Cancer. 2018;103:356–387.
   PubMed Web of Science ®Google Scholar
• Bresnick AR, Weber DJ, Zimmer DB. S100 proteins in cancer. Nat Rev Cancer. 2015;15(2):96–109.
   PubMed Web of Science ®Google Scholar
• Nasser MW, Elbaz M, Ahirwar DK, et al. Conditioning solid tumor microenvironment through inflammatory chemokines and S100 family proteins. Cancer Lett. 2015;365(1):11–22.
   PubMed Web of Science ®Google Scholar
• Peng F, Huang Y, Li MY, et al. Dissecting characteristics and dynamics of differentially expressed proteins during multistage carcinogenesis of human colorectal cancer. WJG. 2016;22(18):4515–4528.
   PubMed Web of Science ®Google Scholar
• Zha H, Sun H, Li X, et al. S100A8 facilitates the migration of colorectal cancer cells through regulating macrophages in the inflammatory microenvironment. Oncol Rep. 2016;36(1):279–290.
   PubMed Web of Science ®Google Scholar
• Moravkova P, Kohoutova D, Rejchrt S, et al. Role of S100 proteins in colorectal carcinogenesis. Gastroenterol Res Pract. 2016;2016:1–7.
   Web of Science ®Google Scholar
• Stulík J, Osterreicher J, Koupilová K, et al. Differential expression of Ca2+ binding S100A6 protein in normal, preneoplastic and neoplastic mucosa. Eur J Cancer. 2000;36:1050–1059.
   PubMed Web of Science ®Google Scholar
• Komatsu K, Andoh A, Ishiguro S, et al. Increased expression of S100A6 (Calcyclin), a calcium-binding protein of the S100 family, in human colorectal adenocarcinomas. Clin Cancer Res. 2000;6(1):172–177.
   PubMed Web of Science ®Google Scholar
• Yu J, Li X, Zhong C, et al. High-throughput proteomics integrated with gene microarray for discovery of colorectal cancer potential biomarkers. Oncotarget. 2016;7(46):75279–75292.
   PubMedGoogle Scholar
• Masuda T, Ishikawa T, Mogushi K, et al. Overexpression of the S100A2 protein as a prognostic marker for patients with stage II and III colorectal cancer. Int J Oncol. 2016;48(3):975–982.
   PubMed Web of Science ®Google Scholar
• Parkkila S, Pan P, Ward A, et al. The calcium-binding protein S100P in normal and malignant human tissues. BMC Clin Pathol. 2008;8(1):2.
   PubMedGoogle Scholar
• Melle C, Ernst G, Schimmel B, et al. Different expression of calgizzarin (S100A11) in normal colonic epithelium, adenoma and colorectal carcinoma. Int J Oncol. 2006;28:195–200.
   PubMed Web of Science ®Google Scholar
• Duan L, Wu R, Zou Z, et al. S100A6 stimulates proliferation and migration of colorectal carcinoma cells through activation of the MAPK pathways. Int J Oncol. 2014;44(3):781–790.
   PubMed Web of Science ®Google Scholar
• Ichikawa M, Williams R, Wang L, et al. S100A8/A9 activate key genes and pathways in colon tumor progression. Mol Cancer Res. 2011;9(2):133–148.
   PubMed Web of Science ®Google Scholar
• Moravkova P, Kohoutova D, Drahosova M, et al. Serum concentration of S100P protein with colorectal cancer. Gastroent Hepatol. 2017;71:293–298. [Article in Czech].
   Google Scholar
• Valentin MA, Ma S, Zhao A, et al. Validation of immunoassay for protein biomarkers: bioanalytical study plan implementation to support pre-clinical and clinical studies. J Pharm Biomed Anal. 2011;55(5):869–877.
   PubMed Web of Science ®Google Scholar
• Stulík J, Koupilová K, Österreicher J, et al. Protein abundance alterations in matched sets of macroscopically normal colon mucosa and colorectal carcinoma. Electrophoresis. 1999;20(18):3638–3646.
   PubMed Web of Science ®Google Scholar
• Stulík J, Osterreicher J, Koupilová K, et al. The analysis of S100A9 and S100A8 expression in matched sets of macroscopically normal colon mucosa and colorectal carcinoma: the S100A9 and S100A8 positive cells underlie and invade tumor mass. Electrophoresis. 1999;20(4–5):1047–1054.
   PubMed Web of Science ®Google Scholar
• Wang XH, Du H, Li L, et al. Increased expression of S100A6 promotes cell proliferation in gastric cancer cells. Oncol Lett. 2017;13(1):222–230.
   PubMed Web of Science ®Google Scholar
• Chen X, Liu X, Lang H, et al. S100 calcium-binding protein A6 promotes epithelial-mesenchymal transition through β-catenin in pancreatic cancer cell line. PLoS One. 2015;10(3):e0121319.
   PubMed Web of Science ®Google Scholar
• Zihao G, Jie Z, Yan L, et al. Analyzing S100A6 expression in endoscopic ultrasonography-guided fine-needle aspiration specimens: a promising diagnostic method of pancreatic cancer. J Clin Gastroenterol. 2013;47(1):69–75.
   PubMed Web of Science ®Google Scholar
• Feng S, Zhou Q, Yang B, et al. The effect of S100A6 on nuclear translocation of CacyBP/SIP in colon cancer cells. PLoS One. 2018;13(3):e0192208.
   PubMed Web of Science ®Google Scholar
• Zhang J, Zhang K, Jiang X, et al. S100A6 as a potential serum prognostic biomarker and therapeutic target in gastric cancer. Dig Dis Sci. 2014;59(9):2136–2144.
   PubMed Web of Science ®Google Scholar
• Nishi M, Matsumoto K, Kobayashi M, et al. Serum expression of S100A6 is a potential detection marker in patients with urothelial carcinoma in the urinary bladder. Biomed Res. 2014;35(6):351–356.
   PubMed Web of Science ®Google Scholar
• Wang T, Liang Y, Thakur A, et al. Diagnostic significance of S100A2 and S100A6 levels in sera of patients with non-small cell lung cancer. Tumor Biol. 2016;37(2):2299–2304.
   PubMedGoogle Scholar
• Loosen SH, Benz F, Niedeggen J, et al. Serum levels of S100A6 are unaltered in patients with resectable cholangiocarcinoma. Clin Transl Med. 2016;5(1):39
   PubMedGoogle Scholar
• Onsurathum S, Haonon O, Pinlaor P, et al. Proteomics detection of S100A6 in tumor tissue interstitial fluid and evaluation of its potential as a biomarker of cholangiocarcinoma. Tumour Biol. 2018;40(4):101042831876719.
   Google Scholar
• Kilańczyk E, Graczyk A, Ostrowska H, et al. S100A6 is transcriptionally regulated by β-catenin and interacts with a novel target, lamin A/C, in colorectal cancer cells. Cell Calcium. 2012;51(6):470–477.
   PubMed Web of Science ®Google Scholar
• DeVries G, McDonald JR, Walsh MP. Calmodulin-like Ca(2+)-binding proteins of smooth muscle. In: Fiskum G, editor. Cell Calcium Metabolism. GWUMC Department of Biochemistry Annual Spring Symposia. Boston, MA: Springer; 1989. p. 427–437.
   Google Scholar
• Tanaka M, Adzuma K, Iwami M, et al. Human calgizzarin; one colorectal cancer-related gene selected by a large scale random cDNA sequencing and northern blot analysis. Cancer Lett. 1995;89(2):195–200.
   PubMed Web of Science ®Google Scholar
• Melle C, Ernst G, Schimmel B, et al. Colon-derived liver metastasis, colorectal carcinoma, and hepatocellular carcinoma can be discriminated by the Ca(2+)-binding proteins S100A6 and S100A11. PLoS One. 2008;3(12):e3767.
   PubMed Web of Science ®Google Scholar
• Inada H, Naka M, Tanaka T, et al. Human S100A11 exhibits differential steady-state RNA levels in various tissues and a distinct subcellular localization. Biochem Biophys Res Commun. 1999;263(1):135–138.
   PubMed Web of Science ®Google Scholar
• He H, Li J, Weng S, et al. S100A11: diverse function and pathology corresponding to different target proteins. Cell Biochem Biophys. 2009;55(3):117–126.
   PubMed Web of Science ®Google Scholar
• Cross SS, Hamdy FC, Deloulme JC, et al. Expression of S100 proteins in normal human tissues and common cancers using tissue microarrays: S100A6, S100A8, S100A9 nad S100A11 are all overexpressed in common cancers. Histopathology. 2005;46(3):256–269.
   PubMed Web of Science ®Google Scholar
• Kristinsson J, Røseth A, Fagerhol MK, et al. Fecal calprotectin concentration in patients with colorectal carcinoma. Dis Colon Rectum. 1998;41(3):316–321.
   PubMed Web of Science ®Google Scholar
• Kristinsson J, Armbruster CH, Ugstad M, et al. Fecal excretion of calprotectin in colorectal cancer: relationship to tumor characteristics. Scand J Gastroenterol. 2001;36(2):202–207.
   PubMed Web of Science ®Google Scholar
• Lehmann FS, Trapani F, Fueglistaler I, et al. Clinical and histopathological correlations of fecal calprotectin release in colorectal carcinoma. WJG. 2014;20(17):4994–4999.
   PubMed Web of Science ®Google Scholar
• Pezzilli R, Barassi A, Morselli Labate AM, et al. Fecal calprotectin levels in patients with colonic polyposis. Dig Dis Sci. 2008;53(1):47–51.
   PubMed Web of Science ®Google Scholar
• Duan L, Wu R, Ye L, et al. S100A8 and S100A9 are associated with colorectal carcinoma progression and contribute to colorectal carcinoma cell survival and migration via Wnt/β-catenin pathway. PLoS One. 2013;8(4):e62092.
   PubMed Web of Science ®Google Scholar
• Kim K, Kim KH, Roh K, et al. Antitumor effects of calgranulin B internalized in human colon cancer cells. Oncotarget. 2016;7:20368–20380.
   PubMedGoogle Scholar