Asian Pacific Journal of Cancer Prevention

  • 제13권11호
  • /
  • Pages.5653-5657
  • /
  • 2012
  • /
  • 1513-7368(pISSN)
  • /
  • 2476-762X(eISSN)
아시아태평양암예방학회 (Asian Pacific Journal of Cancer Prevention)
권호 표지
DOI QR코드

DOI QR Code

ppGalNAc T1 as a Potential Novel Marker for Human Bladder Cancer

  • Ding, Ming-Xia (Department of Urology, The Second Affiliated Hospital of Kunming Medical University, Yunnan Institute of Urology) ;
  • Wang, Hai-Feng (Department of Urology, The Second Affiliated Hospital of Kunming Medical University, Yunnan Institute of Urology) ;
  • Wang, Jian-Song (Department of Urology, The Second Affiliated Hospital of Kunming Medical University, Yunnan Institute of Urology) ;
  • Zhan, Hui (Department of Urology, The Second Affiliated Hospital of Kunming Medical University, Yunnan Institute of Urology) ;
  • Zuo, Yi-Gang (Department of Urology, The Second Affiliated Hospital of Kunming Medical University, Yunnan Institute of Urology) ;
  • Yang, De-Lin (Department of Urology, The Second Affiliated Hospital of Kunming Medical University, Yunnan Institute of Urology) ;
  • Liu, Jing-Yu (Department of Urology, The Second Affiliated Hospital of Kunming Medical University, Yunnan Institute of Urology) ;
  • Wang, Wei (Department of Urology, The Second Affiliated Hospital of Kunming Medical University, Yunnan Institute of Urology) ;
  • Ke, Chang-Xing (Department of Urology, The Second Affiliated Hospital of Kunming Medical University, Yunnan Institute of Urology) ;
  • Yan, Ru-Ping (Department of Urology, The Second Affiliated Hospital of Kunming Medical University, Yunnan Institute of Urology)
  • 발행 : 2012.11.30
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

Objectives: To investigate the effect of glycopeptide-preferring polypeptide GalNAc transferase 1 (ppGalNAc T1 ) targeted RNA interference (RNAi) on the growth and migration of human bladder carcinoma EJ cells in vitro and in vivo. Methods: DNA microarray assays were performed to determine ppGalNAc Ts(ppGalNAc T1-9) expression in human bladder cancer and normal bladder tissues. We transfected the EJ bladder cancer cell line with well-designed ppGalNAc T1 siRNA. Boyden chamber and Wound healing assays were used to investigate changes of shppGalNAc T1-EJ cell migration. Proliferation of shppGalNAc T1-EJ cells in vitro was assessed using [3H]-thymidine incorporation assay and soft agar colony formation assays. Subcutaneous bladder tumors in BALB/c nude mice were induced by inoculation of shppGalNAc T1-EJ cells and after inoculation diameters of tumors were measured every 5 days to determine gross tumor volumes. Results: ppGalNAc T1 mRNA in bladder cancer tissues was 11.2-fold higher than in normal bladder tissues. When ppGalNAc T1 expression in EJ cells was knocked down through transfection by pSUPER-shppGalNAc T1 vector, markedly reduced incorporation of [3H]-thymidine into DNA of EJ cells was observed at all time points compared with the empty vector transfected control cells. However, ppGalNAc T1 knockdown did not significantly inhibited cell migration (only 12.3%). Silenced ppGalNAc T1 expression significantly inhibited subcutaneous tumor growth compared with the control groups injected with empty vector transfected control cells. At the end of observation course (40 days), the inhibitory rate of cancerous growth for ppGalNAc T1 knockdown was 52.5%. Conclusion: ppGalNAc T1 might be a potential novel marker for human bladder cancer. Although ppGalNAc T1 knockdown caused no remarkable change in cell migration, silenced expression significantly inhibited proliferation and tumor growth of the bladder cancer EJ cell line.

키워드

참고문헌

  1. Banks DD (2011). The effect of glycosylation on the folding kinetics of erythropoietin. J Mol Biol, 412, 536-50. https://doi.org/10.1016/j.jmb.2011.07.061
  2. Boscher C, Dennis JW, Nabi IR (2011). Glycosylation, galectins and cellular signaling. Curr Opin Cell Biol, 23, 383-92. https://doi.org/10.1016/j.ceb.2011.05.001
  3. Brooks SA, Carter TM, Bennett EP, et al (2007). Immunolocalisation of members of the polypeptide N-acetylgalactosaminyl transferase (ppGalNAc-T) family is consistent with biologically relevant altered cell surface glycosylation in breast cancer. Acta Histochem, 109, 273-84. https://doi.org/10.1016/j.acthis.2007.02.009
  4. Gallagher DJ, Milowsky MI, Gerst SR, et al (2010). Phase II study of sunitinib in patients with metastatic urothelial cancer. J Clin Oncol, 28, 1373-79. https://doi.org/10.1200/JCO.2009.25.3922
  5. Gao Y, Tu YB, Guo Y, et al (2011). PpGalNacT2 participating in vanadium-induced HL-60 cell differentiation. Mol Biol Rep, 38, 1483-9. https://doi.org/10.1007/s11033-010-0255-3
  6. Gerken TA, Jamison O, Perrine CL, et al (2011). Emerging paradigms for the initiation of mucin-type protein O-glycosylation by the polypeptide GalNAc transferase family of glycosyltransferases. J Biol Chem, 286, 14493-507. https://doi.org/10.1074/jbc.M111.218701
  7. Kato K, Takeuchi H, Kanoh A, et al (2010). Loss of UDPGalNAc: polypeptide N-acetylgalactosaminyltransferase 3 and reduced O-glycosylation in colon carcinoma cells selected for hepatic metastasis. Glycoconj J, 27, 267-76. https://doi.org/10.1007/s10719-009-9275-4
  8. Liu C, Lin D, Xu L, et al (2011). An anti-human ppGalNAcT-2 monoclonal antibody. Hybridoma (Larchmt), 30, 549-54. https://doi.org/10.1089/hyb.2011.0022
  9. Perrine CL, Ganguli A, Wu P, et al (2009). Glycopeptidepreferring polypeptide GalNAc transferase 10 (ppGalNAcT10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2. J Biol Chem, 284, 20387-97. https://doi.org/10.1074/jbc.M109.017236
  10. Platt FM, Hurst CD, Taylor CF, et al(2009). Spectrum of phosphatidylinositol 3-kinase pathway gene alterations in bladder cancer. Clin Cancer Res, 15, 6008-17. https://doi.org/10.1158/1078-0432.CCR-09-0898
  11. Topaz O, Bergman R, Mandel U, et al(2005). Absence of intraepidermal glycosyltransferase ppGalNac-T3 expression in familial tumoral calcinosis. Am J Dermatopathol, 27, 211-5. https://doi.org/10.1097/01.dad.0000158298.02545.a5
  12. Tran DT, Lim JM, Liu M, et al (2012). Glycosylation of ${\alpha}$-dystroglycan: O-mannosylation influences the subsequent addition of GalNAc by UDP-GalNAc polypeptide N-acetylgalactosaminyltransferases. J Biol Chem, 287, 20967-74. https://doi.org/10.1074/jbc.M112.370387
  13. Zlocowski N, Sendra VG, Lorenz V, et al (2011). Catalytic and glycan-binding abilities of ppGalNAc-T2 are regulated by acetylation. Biochem Biophys Res Commun, 410, 140-5. https://doi.org/10.1016/j.bbrc.2011.05.125

피인용 문헌

  1. A Pilot Study on the Potential of RNA-Associated to Urinary Vesicles as a Suitable Non-Invasive Source for Diagnostic Purposes in Bladder Cancer vol.6, pp.1, 2014, https://doi.org/10.3390/cancers6010179
  2. Can Recurrence and Progression be Predicted by HYAL-1 Expression in Primary T1 Bladder Cancer? vol.15, pp.23, 2015, https://doi.org/10.7314/APJCP.2014.15.23.10401
  3. Differentially Expressed Genes in Metastatic Advanced Egyptian Bladder Cancer vol.16, pp.8, 2015, https://doi.org/10.7314/APJCP.2015.16.8.3543
  4. Aberrant methylation of CDH11 predicts a poor outcome for patients with bladder cancer pp.1792-1082, 2015, https://doi.org/10.3892/ol.2015.3337
  5. Epithelial Mesenchymal Transition Induces Aberrant Glycosylation through Hexosamine Biosynthetic Pathway Activation vol.291, pp.25, 2016, https://doi.org/10.1074/jbc.M116.729236
  6. RNA interference-mediated silencing of ppGalNAc-T1 and ppGalNAc-T2 inhibits invasion and increases chemosensitivity potentially by reducing terminal α2,3 sialylation and MMP14 expression in triple-negative breast cancer cells vol.15, pp.6, 2017, https://doi.org/10.3892/mmr.2017.6449
  7. Hyperglycemia exacerbates colon cancer malignancy through hexosamine biosynthetic pathway vol.6, pp.3, 2017, https://doi.org/10.1038/oncsis.2017.2
  8. -acetylgalactosaminyltransferase 6 (GalNAc-T6) in colon adenocarcinoma inhibits the differentiation of colonic epithelium vol.293, pp.4, 2017, https://doi.org/10.1074/jbc.M117.812826
  9. Glycogene expression profiles based on microarray data from cervical carcinoma HeLa cells with partially silenced E6 and E7 HPV oncogenes vol.13, pp.1, 2018, https://doi.org/10.1186/s13027-018-0197-2
  10. Long non-coding RNA-SNHG7 acts as a target of miR-34a to increase GALNT7 level and regulate PI3K/Akt/mTOR pathway in colorectal cancer progression vol.11, pp.1, 2018, https://doi.org/10.1186/s13045-018-0632-2