- Volume 17 Issue 1
DOI QR Code
Clinicopathological Significance of S100A10 Expression in Lung Adenocarcinomas
- Katono, Ken (Department of Respiratory Medicine, School of Medicine, Kitasato University) ;
- Sato, Yuichi (Department of Molecular Diagnostics, School of Allied Health Sciences, Kitasato University) ;
- Jiang, Shi-Xu (Department of Pathology, School of Medicine, Kitasato University) ;
- Kobayashi, Makoto (Department of Molecular Diagnostics, School of Allied Health Sciences, Kitasato University) ;
- Saito, Keita (Department of Molecular Diagnostics, School of Allied Health Sciences, Kitasato University) ;
- Nagashio, Ryo (Department of Molecular Diagnostics, School of Allied Health Sciences, Kitasato University) ;
- Ryuge, Shinichiro (Department of Respiratory Medicine, School of Medicine, Kitasato University) ;
- Satoh, Yukitoshi (Department of Thoracic and Cardiovascular Surgery, School of Medicine, Kitasato University) ;
- Saegusa, Makoto (Department of Pathology, School of Medicine, Kitasato University) ;
- Masuda, Noriyuki (Department of Respiratory Medicine, School of Medicine, Kitasato University)
- Published : 2016.02.05
Background: S100A10, of the S100 protein family, is reported to be involved in cancer cell invasion and metastasis. The aims of the present study were to immunohistochemically examine S100A10 expression in surgically resected lung adenocarcinomas, and evaluate any relationships with clinicopathological parameters and prognosis of patients. Materials and Methods: S100A10 expression was immunohistochemically studied in 202 consecutive resected lung adenocarcinomas, and its associations with clinicopathological parameters were evaluated. Kaplan-Meier survival analysis and Cox proportional hazards models were used to estimate the effect of S100A10 expression on survival. Results: S100A10 expression was detected in 65 of the 202 (32.2%) lung adenocarcinomas, being significantly correlated with poorer differentiation (P =0.015), a higher pathological TNM stage (stages II and III) (P=0.004), more frequent and severe intratumoral vascular invasion (P=0.001), and a poorer prognosis (P=0.030). However, S100A10 expression was not an independent predictor of survival after controlling for clinicopathological factors. Conclusions: The present study reveals that S100A10 is expressed in a subset of lung adenocarcinomas, and this is related to some clinicopathological parameters, although further studies are required to confirm the correlation between S100A10 expression and prognosis of lung adenocarcinoma patients.
S100A10;plasminogen receptor;lung adenocarcinoma;prognosis
Supported by : JSPS
- Alberg AJ, Brock MV, Ford JG, et al (2013). Epidemiology of lung cancer: diagnosis and management of lung cancer, 3rd ed: american college of chest physicians evidence-based clinical practice guidelines. Chest, 143, 1-29. https://doi.org/10.1378/chest.12-2762
- Chen H, Xu C, Jin Q, et al (2014). S100 protein family in human cancer. Am J Cancer Res, 4, 89-115.
- Choi KS, Fogg DK, Yoon CS, et al (2003). p11 regulates extracellular plasmin production and invasiveness of HT1080 fibrosarcoma cells. FASEB J, 17, 235-46. https://doi.org/10.1096/fj.02-0697com
- Domoto T, Miyama Y, Suzuki H, et al (2007). Evaluation of S100A10, annexin II and B-FABP expression as markers for renal cell carcinoma. Cancer Sci, 98, 77-82. https://doi.org/10.1111/j.1349-7006.2006.00355.x
- Donato R (2001). S100: a multigenic family of calciummodulated proteins of the EF-hand type with intracellular and extracellular functional roles. Int J Biochem Cell Biol, 33, 637-68. https://doi.org/10.1016/S1357-2725(01)00046-2
- Godier A, Hunt BJ (2013). Plasminogen receptors and their role in the pathogenesis of inflammatory, autoimmune and malignant disease. J Thromb Haemost, 11, 26-34. https://doi.org/10.1111/jth.12064
- Goldstraw P, Crowley J, Chansky K, et al (2007). The IASLC lung cancer staging project: proposals for the revision of the TNM stage groupings in the forthcoming (seventh) edition of the TNM Classification of malignant tumours. J Thorac Oncol, 2, 706-14. https://doi.org/10.1097/JTO.0b013e31812f3c1a
- Hedhli N, Falcone DJ, Huang B, et al (2012). The annexin A2/S100A10 system in health and disease: emerging paradigms. J Biomed Biotechnol, 2012, 406273.
- Hsu SY, Kaipia A, Zhu L, et al (1997). Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11. Mol Endocrinol, 11, 1858-67.
- Ito Y, Arai K, Nozawa R, et al (2007). S100A10 expression in thyroid neoplasms originating from the follicular epithelium: contribution to the aggressive characteristic of anaplastic carcinoma. Anticancer Res, 27, 2679-83.
- Kawai H, Minamiya Y, Takahashi N (2011). Prognostic impact of S100A9 overexpression in non-small cell lung cancer. Tumour Biol, 32, 641-6. https://doi.org/10.1007/s13277-011-0163-8
- Kobayashi S, Boggon TJ, Dayaram T, et al (2005). EGFR mutation and resistance of non-small-cell lung cancer to gefitinib. N Engl J Med, 352, 786-92. https://doi.org/10.1056/NEJMoa044238
- Liu Y, Myrvang HK, Dekker LV, et al (2015). Annexin A2 complexes with S100 proteins: structure, function and pharmacological manipulation. Br J Pharmacol, 172, 1664-76. https://doi.org/10.1111/bph.12978
- Madureira PA, O'Connell PA, Surette AP, et al (2012). The biochemistry and regulation of S100A10: a multifunctional plasminogen receptor involved in oncogenesis. J Biomed Biotechnol, 2012, 353687.
- Parkin DM (2001). Global cancer statistics in the year 2000. Lancet Oncol, 2, 533-43. https://doi.org/10.1016/S1470-2045(01)00486-7
- Phipps KD, Surette AP, O'Connell PA, et al (2011). Plasminogen receptor S100A10 is essential for the migration of tumorpromoting macrophages into tumor sites. Cancer Res, 71, 6676-83. https://doi.org/10.1158/0008-5472.CAN-11-1748
- Sayeed S, Asano E, Ito S, et al (2013). S100A10 is required for the organization of actin stress fibers and promotion of cell spreading. Mol Cell Biochem, 374, 105-11. https://doi.org/10.1007/s11010-012-1509-2
- Shang J, Zhang Z, Song W, et al (2013). S100A10 as a novel biomarker in colorectal cancer. Tumour Biol, 34, 3785-90. https://doi.org/10.1007/s13277-013-0962-1
- Surette AP, Madureira PA, Phipps KD, et al (2011). Regulation of fibrinolysis by S100A10 in vivo. Blood, 118, 3172-81. https://doi.org/10.1182/blood-2011-05-353482
- Tan Y, Ma SY, Wang FQ, et al (2011). Proteomic-based analysis for identification of potential serum biomarkers in gallbladder cancer. Oncol Rep, 26, 853-9.
- Travis WD, Coby TV, Corrin B, et al (1999). World health organization international histological classification of tumors; histological typing of lung and pleural tumors. Springer.
- Tsuna M, Kageyama S, Fukuoka J, et al (2009). Significance of S100A4 as a prognostic marker of lung squamous cell carcinoma. Anticancer Res, 29, 2547-54.
- Wang H, Zhang Z, Li R, et al (2005). Overexpression of S100A2 protein as a prognostic marker for patients with stage I non small cell lung cancer. Int J Cancer, 116, 285-90. https://doi.org/10.1002/ijc.21035
- Yoshino I, Yoshida S, Miyaoka E, et al (2012). Surgical outcome of stage IIIA- cN2/pN2 non-small-cell lung cancer patients in Japanese lung cancer registry study in 2004. J Thorac Oncol, 7, 850-5. https://doi.org/10.1097/JTO.0b013e31824c945b
- Zhang L, Fogg DK, Waisman DM (2004). RNA interferencemediated silencing of the S100A10 gene attenuates plasmin generation and invasiveness of Colo 222 colorectal cancer cells. J Biol Chem, 279, 2053-62. https://doi.org/10.1074/jbc.M310357200
- Quantitative proteomics identify Tenascin-C as a promoter of lung cancer progression and contributor to a signature prognostic of patient survival vol.114, pp.28, 2017, https://doi.org/10.1073/pnas.1707054114
- A pathology atlas of the human cancer transcriptome vol.357, pp.6352, 2017, https://doi.org/10.1126/science.aan2507
- Prognostic Roles of mRNA Expression of S100 in Non-Small-Cell Lung Cancer vol.2018, pp.2314-6141, 2018, https://doi.org/10.1155/2018/9815806
- CPT1A-mediated succinylation of S100A10 increases human gastric cancer invasion pp.15821838, 2018, https://doi.org/10.1111/jcmm.13920
- iTRAQ-based proteomic analysis of DMH-induced colorectal cancer in mice reveals the expressions of β-catenin, decorin, septin-7, and S100A10 expression in 53 cases of human hereditary polyposis colorectal cancer pp.1699-3055, 2018, https://doi.org/10.1007/s12094-018-1912-6