Stanniocalcin 2 (STC2) expression promotes post-radiation survival, migration and invasion of nasopharyngeal carcinoma cells

References

• Ishibashi K, Miyamoto K, Taketani Y, et al. Molecular cloning of a second human stanniocalcin homologue (STC2). Biochem Biophys Res Commun. 1998;250(2):252–258. doi:10.1006/bbrc.1998.93009753616
   PubMed Web of Science ®Google Scholar
• Chang AC-M, Janosi J, Hulsbeek M, et al. A novel human cDNA highly homologous to the fish hormone stanniocalcin. Mol Cell Endocrinol. 1995;112(2):241–247.7489828
   PubMed Web of Science ®Google Scholar
• Olsen HS, Cepeda MA, Zhang -Q-Q, et al. Human stanniocalcin: a possible hormonal regulator of mineral metabolism. Proc Natl Acad Sci. 1996;93(5):1792–1796.8700837
   PubMed Web of Science ®Google Scholar
• Madsen KL, Tavernini MM, Yachimec C, et al. Stanniocalcin: a novel protein regulating calcium and phosphate transport across mammalian intestine. Am J Physiol Gastrointest Liver Physiol. 1998;274(1):G96–G102. doi:10.1152/ajpgi.1998.274.1.G96
   Web of Science ®Google Scholar
• Pacheco J, Vaca L. STIM-TRP Pathways and Microdomain Organization: auxiliary proteins of the STIM/Orai complex Adv Exp Med Biol. 2017:993:189–210.
   Google Scholar
• Zeiger W, Ito D, Swetlik C, et al. Stanniocalcin 2 is a negative modulator of store-operated calcium entry. Mol Cell Biol. 2011;31(18):3710–3722. doi:10.1128/MCB.05140-1121746875
   PubMed Web of Science ®Google Scholar
• Lin S, Guo Q, Wen J, et al. Survival analyses correlate stanniocalcin 2 overexpression to poor prognosis of nasopharyngeal carcinomas. J Exp Clin Cancer Res. 2014;33(1):26. doi:10.1186/1756-9966-33-2624606961
   PubMedGoogle Scholar
• Law AY, Wong CK. Stanniocalcin-2 promotes epithelial-mesenchymal transition and invasiveness in hypoxic human ovarian cancer cells. Exp Cell Res. 2010;316(20):3425–3434. doi:10.1016/j.yexcr.2010.06.02620619259
   PubMed Web of Science ®Google Scholar
• Esseghir S, Kennedy A, Seedhar P, et al. Identification of NTN4, TRA1, and STC2 as prognostic markers in breast cancer in a screen for signal sequence encoding proteins. Clin Cancer Res. 2007;13(11):3164–3173. doi:10.1158/1078-0432.CCR-07-022417545519
   PubMed Web of Science ®Google Scholar
• Volland S, Kugler W, Schweigerer L, Wilting J, Becker J. Stanniocalcin 2 promotes invasion and is associated with metastatic stages in neuroblastoma. Int J Cancer. 2009;125(9):2049–2057. doi:10.1002/ijc.2456419582875
   PubMed Web of Science ®Google Scholar
• Tamura K, Furihata M, Chung SY, et al. Stanniocalcin 2 overexpression in castration-resistant prostate cancer and aggressive prostate cancer. Cancer Sci. 2009;100(5):914–919. doi:10.1111/j.1349-7006.2009.01117.x19298603
   PubMed Web of Science ®Google Scholar
• Kita Y, Mimori K, Iwatsuki M, et al. STC2: a predictive marker for lymph node metastasis in esophageal squamous-cell carcinoma. Ann Surg Oncol. 2011;18(1):261–272. doi:10.1245/s10434-010-1271-120734150
   PubMed Web of Science ®Google Scholar
• Yokobori T, Mimori K, Ishii H, et al. Clinical significance of stanniocalcin 2 as a prognostic marker in gastric cancer. Ann Surg Oncol. 2010;17(10):2601–2607. doi:10.1245/s10434-010-1086-020422456
   PubMed Web of Science ®Google Scholar
• Na SS, Aldonza MB, Sung H-J, et al. Stanniocalcin-2 (STC2): a potential lung cancer biomarker promotes lung cancer metastasis and progression. Biochim Biophys Acta Proteins Proteom. 2015;1854(6):668–676. doi:10.1016/j.bbapap.2014.11.002
   PubMed Web of Science ®Google Scholar
• Ieta K, Tanaka F, Yokobori T, et al. Clinicopathological significance of stanniocalcin 2 gene expression in colorectal cancer. Int J Cancer. 2009;125(4):926–931. doi:10.1002/ijc.2445319415750
   PubMed Web of Science ®Google Scholar
• Meyer HA, Tolle A, Jung M, et al. Identification of stanniocalcin 2 as prognostic marker in renal cell carcinoma. Eur Urol. 2009;55(3):669–678. doi:10.1016/j.eururo.2008.04.00118450365
   PubMed Web of Science ®Google Scholar
• Bouras T, Southey MC, Chang AC, et al. Stanniocalcin 2 is an estrogen-responsive gene coexpressed with the estrogen receptor in human breast cancer. Cancer Res. 2002;62(5):1289–1295.11888893
   PubMed Web of Science ®Google Scholar
• Joensuu K, Heikkila P, Andersson LC. Tumor dormancy: elevated expression of stanniocalcins in late relapsing breast cancer. Cancer Lett. 2008;265(1):76–83. doi:10.1016/j.canlet.2008.02.02218355956
   PubMed Web of Science ®Google Scholar
• Choudhry H, Harris AL. Advances in hypoxia-inducible factor biology. Cell Metab. 2017;27(2):281–298. doi:10.1016/j.cmet.2017.10.00529129785
   PubMed Web of Science ®Google Scholar
• Song H, Xu B, Yi J. Clinical significance of stanniocalcin-1 detected in peripheral blood and bone marrow of esophageal squamous cell carcinoma patients. J Exp Clin Cancer Res. 2012;31:35. doi:10.1186/1756-9966-31-9522537917
   PubMed Web of Science ®Google Scholar
• Hu T, He N, Yang Y, et al. DEC2 expression is positively correlated with HIF-1 activation and the invasiveness of human osteosarcomas. J Exp Clin Cancer Res. 2015;34:22. doi:10.1186/s13046-015-0135-825884381
   PubMed Web of Science ®Google Scholar
• MacLachlan TK, Sang N, Giordano A. Cyclins, cyclin-dependent kinases and cdk inhibitors: implications in cell cycle control and cancer. Crit Rev Eukaryot Gene Expr. 1995;5(2):127–156. doi:10.1615/CritRevEukarGeneExpr.v5.i2.208845581
   PubMed Web of Science ®Google Scholar
• Bakkenist CJ, Kastan MB. DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation. Nature. 2003;421(6922):499–506. doi:10.1038/nature0136812556884
   PubMed Web of Science ®Google Scholar
• Matsuoka S, Ballif BA, Smogorzewska A, et al. ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007;316(5828):1160–1166. doi:10.1126/science.114032117525332
   PubMed Web of Science ®Google Scholar
• Liang D, Kong X, Sang N. Effects of histone deacetylase inhibitors on HIF-1. Cell Cycle. 2006;5(21):2430–2435. doi:10.4161/cc.5.21.340917102633
   PubMed Web of Science ®Google Scholar
• Meng M, Chen S, Lao T, Liang D, Sang N. Nitrogen anabolism underlies the importance of glutaminolysis in proliferating cells. Cell Cycle. 2010;9(19):3921–3932. doi:10.4161/cc.9.19.1313920935507
   PubMed Web of Science ®Google Scholar
• Yin C, Qie S, Sang N. Carbon source metabolism and its regulation in cancer cells. Crit Rev Eukaryot Gene Expr. 2012;22(1):17–35. doi:10.1615/CritRevEukarGeneExpr.v22.i1.2022339657
   PubMed Web of Science ®Google Scholar
• Chen S, Yin C, Lao T, et al. AMPK-HDAC5 pathway facilitates nuclear accumulation of HIF-1α and functional activation of HIF-1 by deacetylating Hsp70 in the cytosol. Cell Cycle. 2015;14(15):2520–2536. doi:10.1080/15384101.2015.105542626061431
   PubMed Web of Science ®Google Scholar
• Chen S, Sang N. Hypoxia-inducible factor-1: a critical player in the survival strategy of stressed cells. J Cell Biochem. 2016;117(2):267–278. doi:10.1002/jcb.2528326206147
   PubMed Web of Science ®Google Scholar
• Yin C, He D, Chen S, Tan X, Sang N. Exogenous pyruvate facilitates cancer cell adaptation to hypoxia by serving as an oxygen surrogate. Oncotarget. 2016;7(30):47494. doi:10.18632/oncotarget.v7i3027374086
   PubMedGoogle Scholar
• Law AY, Lai KP, Ip CK, et al. Epigenetic and HIF-1 regulation of stanniocalcin-2 expression in human cancer cells. Exp Cell Res. 2008;314(8):1823–1830. doi:10.1016/j.yexcr.2008.03.00118394600
   PubMed Web of Science ®Google Scholar
• Law AY, Wong CK. Stanniocalcin-2 is a HIF-1 target gene that promotes cell proliferation in hypoxia. Exp Cell Res. 2010;316(3):466–476. doi:10.1016/j.yexcr.2009.09.01819786016
   PubMed Web of Science ®Google Scholar
• Qie S, Liang D, Yin C, et al. Glutamine depletion and glucose depletion trigger growth inhibition via distinctive gene expression reprogramming. Cell Cycle. 2012;11(19):3679–3690. doi:10.4161/cc.2194422935705
   PubMed Web of Science ®Google Scholar
• Garnett CT, Palena C, Chakraborty M, et al. Sublethal irradiation of human tumor cells modulates phenotype resulting in enhanced killing by cytotoxic T lymphocytes. Cancer Res. 2004;64(21):7985–7994. doi:10.1158/0008-5472.CAN-04-152515520206
   PubMed Web of Science ®Google Scholar
• Ito D, Walker JR, Thompson CS, et al. Characterization of stanniocalcin 2, a novel target of the mammalian unfolded protein response with cytoprotective properties. Mol Cell Biol. 2004;24(21):9456–9469. doi:10.1128/MCB.24.21.9456-9469.200415485913
   PubMed Web of Science ®Google Scholar
• Bao S, Wu Q, McLendon RE, et al. Glioma stem cells promote radioresistance by preferential activation of the DNA damage response. Nature. 2006;444(7120):756–760. doi:10.1038/nature0523617051156
   PubMed Web of Science ®Google Scholar
• Bartkova J, Hořejší Z, Koed K, et al. DNA damage response as a candidate anti-cancer barrier in early human tumorigenesis. Nature. 2005;434(7035):864–870. doi:10.1038/nature0348215829956
   PubMed Web of Science ®Google Scholar
• Clapham DE. Calcium signaling. Cell. 2007;131(6):1047–1058. doi:10.1016/j.cell.2007.11.02818083096
   PubMed Web of Science ®Google Scholar
• Willoughby D, Cooper DM. Organization and Ca2+ regulation of adenylyl cyclases in cAMP microdomains. Physiol Rev. 2007;87(3):965–1010. doi:10.1152/physrev.00049.200617615394
   PubMed Web of Science ®Google Scholar