Asian Pacific Journal of Cancer Prevention

Asian Pacific Journal of Cancer Prevention (아시아태평양암예방학회)
권호 표지
DOI QR코드

DOI QR Code

β3GnT8 Regulates Laryngeal Carcinoma Cell Proliferation Via Targeting MMPs/TIMPs and TGF-β1

  • Hua, Dong (The Fourth Affiliated Hospital of Soochow University) ;
  • Qin, Fang (Department of Biochemistry and Mollecular Biology, School of Medicine, Soochow University) ;
  • Shen, Li (Department of Biochemistry and Mollecular Biology, School of Medicine, Soochow University) ;
  • Jiang, Zhi (Department of Biochemistry and Mollecular Biology, School of Medicine, Soochow University) ;
  • Zou, Shi-Tao (Department of Biochemistry and Mollecular Biology, School of Medicine, Soochow University) ;
  • Xu, Lan (Department of Biochemistry and Mollecular Biology, School of Medicine, Soochow University) ;
  • Cheng, Zhi-Hong (The Fourth Affiliated Hospital of Soochow University) ;
  • Wu, Shi-Liang (Department of Biochemistry and Mollecular Biology, School of Medicine, Soochow University)
  • Published : 2012.05.30
Download PDF
⟨ Previous Next ⟩

Abstract

Previous evidence showed ${\beta}1$, 3-N-acetylglucosaminyltransferase 8 (${\beta}3GnT8$), which can extend polylactosamine on N-glycans, to be highly expressed in some cancer cell lines and tissues, indicating roles in tumorigenesis. However, so far, the function of ${\beta}3GnT8$ in laryngeal carcinoma has not been characterized. To test any contribution, Hep-2 cells were stably transfected with sense or interference vectors to establish cell lines that overexpressed or were deficient in ${\beta}3GnT8$. Here we showed that cell proliferation was increased in ${\beta}3GnT8$ overexpressed cells but decreased in ${\beta}3GnT8$ knockdown cells using MTT. Furthermore, we demonstrated that change in ${\beta}3GnT8$ expression had significant effects on tumor growth in nude mice.We further provided data suggesting that overexpression of ${\beta}3GnT8$ enhanced the expression of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) at both the mRNA and protein levels, associated with shedding of tissue inhibitors of metalloproteinase TIMP-2. In addition, it caused increased production of transforming growth factor beta 1 (TGF-${\beta}1$), whereas ${\beta}3GnT8$ gene knockdown caused the reverse effect. The results may indicate a novel mechanism by which effects of ${\beta}3GnT8$ in regulating cellular proliferation are mediated, at least in partvia targeting MMPs/TIMPs and TGF-${\beta}1$ in laryngeal carcinoma Hep-2 cells. The finding may lay a foundation for further investigations into the ${\beta}3GnT8$ as a potential target for therapy of laryngeal carcinoma.

Keywords

References

  1. Biswas MH, Du C, Zhang C, et al (2010). Protein kinase D1 inhibits cell proliferation through matrix metalloproteinase-2 and matrix metalloproteinase-9 secretion in prostate cancer. Cancer Res, 70, 2095-104. https://doi.org/10.1158/0008-5472.CAN-09-4155
  2. Calle Y, Palomares T, Castro B, et al (2000). Removal of N-glycans from cell surface proteins induces apoptosis by reducing intracellular glutathione levels in the rhabdomyosarcoma cell line S4MH. Biol Cell, 92, 639-46. https://doi.org/10.1016/S0248-4900(01)01114-5
  3. Dahlgaard K, Jung A, Qvortrup K, et al (2012). Neurofibromatosis-like phenotype in Drosophila caused by lack of glucosylceramide extension. Proc Natl Acad Sci U S A, 109, 6987-92. https://doi.org/10.1073/pnas.1115453109
  4. Decock J, Thirkettle S, Wagstaff L, et al (2011). Matrix metalloproteinases: protective roles in cancer. J Cell Mol Med, 15, 1254-65. https://doi.org/10.1111/j.1582-4934.2011.01302.x
  5. Dhawan P, Singh AB, Deane NG, et al (2005). Claudin-1 regulates cellular transformation and metastatic behavior in colon cancer. J Clin Invest, 115, 1765-76. https://doi.org/10.1172/JCI24543
  6. Gao CF, Xie Q, Su YL, et al (2005). Proliferation and invasion: plasticity in tumor cells. Proc Natl Acad Sci USA, 102, 10528-33. https://doi.org/10.1073/pnas.0504367102
  7. Gao M, Zhang JH, Zhou FX, et al (2012). Angelica sinensis suppresses human lung adenocarcinoma A549 cell metastasis by regulating MMPs/TIMPs and TGF-beta1. Oncol Rep, 27, 585-93.
  8. Gialeli C, Theocharis AD, Karamanos NK (2011). Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting. FEBS J, 278, 16-27. https://doi.org/10.1111/j.1742-4658.2010.07919.x
  9. Giannelli G, Bergamini C, Marinosci F, et al (2002). Clinical role of MMP-2/TIMP-2 imbalance in hepatocellular carcinoma. Int J Cancer, 97, 425-31. https://doi.org/10.1002/ijc.1635
  10. Gomes LR, Terra LF, Wailemann RA, et al (2012). TGF-beta1 modulates the homeostasis between MMPs and MMP inhibitors through p38 MAPK and ERK1/2 in highly invasive breast cancer cells. BMC Cancer, 12, 26.
  11. Guo HB, Lee I, Kamar M, Pierce M (2003). N-acetylglucosaminyltransferase V expression levels regulate cadherin-associated homotypic cell-cell adhesion and intracellular signaling pathways. J Biol Chem, 278, 52412-24. https://doi.org/10.1074/jbc.M308837200
  12. Hossler P, Khattak SF, Li, ZJ, et al (2009). Optimal and consistent protein glycosylation in mammalian cell culture. Glycobiology, 19, 936-49. https://doi.org/10.1093/glycob/cwp079
  13. Huang C, Zhou J, Wu S, Shan Y, et al (2004). Cloning and tissue distribution of the human B3GALT7 gene, a member of the beta1,3-Glycosyltransferase family. Glycoconj J, 21, 267-73. https://doi.org/10.1023/B:GLYC.0000045098.78968.4c
  14. Ishida H, Togayachi A, Sakai T, et al (2005). A novel beta1, 3-N-acetylglucosaminyltransferase (beta3Gn-T8), which synthesizes poly-N-acetyllactosamine, is dramatically upregulated in colon cancer. FEBS Lett, 579, 71-8. https://doi.org/10.1016/j.febslet.2004.11.037
  15. Jiang Z, Ge Y, Zhou J, et al (2010). Subcellular localization and tumor distribution of human beta3-galactosyltransferase by beta3GalT7 antiserum. Hybridoma (Larchmt), 29, 141-6. https://doi.org/10.1089/hyb.2009.0064
  16. Kalathas D, Triantaphyllidou IE, Mastronikolis NS, et al (2010). The chondroitin/dermatan sulfate synthesizing and modifying enzymes in laryngeal cancer: expressional and epigenetic studies. Head Neck Oncol, 2, 27. https://doi.org/10.1186/1758-3284-2-27
  17. Kim JH, Cho CS, Jun HO, et al (2010). Differential roles of matrix metalloproteinase-9 and -2, depending on proliferation or differentiation of retinoblastoma cells. Invest Ophthalmol Vis Sci, 51, 1783-8. https://doi.org/10.1167/iovs.09-3990
  18. Kuhns WJ, Schoentag R (1981). Carcinoma-related alterations of glycosyltransferases in human tissues. Cancer Res, 41, 2767-72.
  19. Liu Z, Shen L, Xu L, et al (2011). Down-regulation of beta- 1,3-N-acetylglucosaminyltransferase-8 by siRNA inhibits the growth of human gastric cancer. Mol Med Report, 4, 497-503.
  20. Lu L, Qiu J, Liu S, Luo W (2008). Vitamin D3 analogue EB1089 inhibits the proliferation of human laryngeal squamous carcinoma cells via p57. Mol Cancer Ther, 7, 1268-74. https://doi.org/10.1158/1535-7163.MCT-07-2222
  21. Mallis A, Teymoortash A, Mastronikolis NS, et al (2012). MMP- 2 expression in 102 patients with glottic laryngeal cancer. Eur Arch Otorhinolaryngol, 269, 639-42. https://doi.org/10.1007/s00405-011-1625-8
  22. Marioni G, Marchese-Ragona R, Cartei G, et al (2006). Current opinion in diagnosis and treatment of laryngeal carcinoma. Cancer Treat Rev, 32, 504-15. https://doi.org/10.1016/j.ctrv.2006.07.002
  23. Papadas TA, Alexopoulos EC, Mallis A, et al (2010). Survival after laryngectomy: a review of 133 patients with laryngeal carcinoma. Eur Arch Otorhinolaryngol, 267, 1095-101. https://doi.org/10.1007/s00405-009-1156-8
  24. Risinger GM, Jr, Updike DL, et al (2010). TGF-beta suppresses the upregulation of MMP-2 by vascular smooth muscle cells in response to PDGF-BB. Am J Physiol Cell Physiol, 298, C191-201. https://doi.org/10.1152/ajpcell.00417.2008
  25. Seko A, Yamashita K (2005). Characterization of a novel galactose beta1, 3-N-acetylglucosaminyltransferase (beta3Gn-T8): the complex formation of beta3Gn-T2 and beta3Gn-T8 enhances enzymatic activity. Glycobiology, 15, 943-51. https://doi.org/10.1093/glycob/cwi082
  26. Sun Y, Liu M, Yang B, et al (2008). Inhibition of laryngeal cancer cell invasion and growth with lentiviral-vector delivered short hairpin RNA targeting human MMP-9 gene. Cancer Invest, 26, 984-9. https://doi.org/10.1080/07357900802072897
  27. Sun Y, Liu M, Yang B, et al (2008). Role of siRNA silencing of MMP-2 gene on invasion and growth of laryngeal squamous cell carcinoma. Eur Arch Otorhinolaryngol, 265, 1385-91. https://doi.org/10.1007/s00405-008-0684-y
  28. Uloza V, Liutkevicius V, Pangonyte D, et al (2011). Expression of matrix metalloproteinases (MMP-2 and MMP-9) in recurrent respiratory papillomas and laryngeal carcinoma: clinical and morphological parallels. Eur Arch Otorhinolaryngol, 268, 871-8. https://doi.org/10.1007/s00405-011-1494-1
  29. Van Belle S (2008). How to implement the multidisciplinary approach in prostate cancer management: the Belgian model. BJU Int, 101, 2-4.
  30. Vischer P, Buddecke E (1985). Alteration of glycosyltransferase activities during proliferation of cultivated arterial endothelial cells and smooth muscle cells. Exp Cell Res, 158, 15-28. https://doi.org/10.1016/0014-4827(85)90427-6
  31. Wang C, Kovanen V, Raudasoja P, et al (2009). The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability. J Cell Mol Med, 13, 508-21. https://doi.org/10.1111/j.1582-4934.2008.00286.x
  32. Wiercinska E, Naber HP, Pardali E, et al (2011). The TGF-beta/ Smad pathway induces breast cancer cell invasion through the up-regulation of matrix metalloproteinase 2 and 9 in a spheroid invasion model system. Breast Cancer Res Treat, 128, 657-66. https://doi.org/10.1007/s10549-010-1147-x
  33. Yoshida T, Yoshimura E, Numata H, et al (1999). Involvement of tenascin-C in proliferation and migration of laryngeal carcinoma cells. Virchows Arch, 435, 496-500. https://doi.org/10.1007/s004280050433
  34. Zhang JF, Zhang YP, Hao FY, et al (2005). DNA ploidy analysis and expression of MMP-9, TIMP-2, and E-cadherin in gastric carcinoma. World J Gastroenterol, 11, 5592-a600. https://doi.org/10.3748/wjg.v11.i36.5592

Cited by

  1. High expression of β3GnT8 is associated with the metastatic potential of human glioma vol.33, pp.6, 2014, https://doi.org/10.3892/ijmm.2014.1736
  2. Knockdown of β3GnT8 reverses 5-fluorouracil resistance in human colorectal cancer cells via inhibition the biosynthesis of polylactosamine-type N-glycans vol.45, pp.6, 2014, https://doi.org/10.3892/ijo.2014.2672
  3. B3GNT3 Expression Is a Novel Marker Correlated with Pelvic Lymph Node Metastasis and Poor Clinical Outcome in Early-Stage Cervical Cancer vol.10, pp.12, 2015, https://doi.org/10.1371/journal.pone.0144360
  4. B3GNT3 overexpression is associated with unfavourable survival in non-small cell lung cancer vol.71, pp.7, 2018, https://doi.org/10.1136/jclinpath-2017-204860