Asian Pacific Journal of Cancer Prevention

  • 제15권14호
  • /
  • Pages.5601-5605
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  • 2014
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  • 1513-7368(pISSN)
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  • 2476-762X(eISSN)
아시아태평양암예방학회 (Asian Pacific Journal of Cancer Prevention)
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Lectin from Agrocybe aegerita as a Glycophenotype Probe for Evaluation of Progression and Survival in Colorectal Cancer

  • Liang, Yi (Department of Clinical Immunology, Guangdong Medical College) ;
  • Chen, Hua (Sino-American Cancer Research Institute, Guangdong Medical College) ;
  • Zhang, Han-Bin (Sino-American Cancer Research Institute, Guangdong Medical College) ;
  • Jin, Yan-Xia (The College of Life Sciences, Wuhan University) ;
  • Guo, Hong-Qiang (The Affiliated Cancer Hospital of Zhengzhou University) ;
  • Chen, Xing-Gui (Cancer Center, the Affiliated Hospital of Guangdong Medical College) ;
  • Sun, Hui (The College of Life Sciences, Wuhan University)
  • 발행 : 2014.07.30
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Background: Agrocybe aegerita Lectin (AAL) has been identified to have high affinity for sulfated and ${\alpha}2$-3-linked sialic acid glycoconjugates, especially the sulfated and sialyl TF (Thomsen-Friedenreich) disaccharide. This study was conducted to investigate the clinicopathological and prognostic value of AAL in identifying aberrant glycosylation in colorectal cancer (CRC). Materials and Methods: Glycoconjugate expression in 59 CRC tissues were detected using AAL-histochemistry. Clinicopathological associates of expression were analyzed with chisquare test or Fisher's exact test. Relationships between expression and the various clinicopathological parameters was estimated using Kaplan-Meier analysis and Cox regression models. Results: AAL specific glycoconjugate expression was significantly higher in tumor than corresponding normal tissues (66.1% and 46.1%, respectively, p=0.037), correlating with depth of invasion (p=0.015) and TNM stage (p=0.024). Patients with lower expression levels had a significantly higher survival rate than those with higher expression (p=0.046 by log rank test and p=0.047 by Breslow test for overall survival; p=0.054 by log rank test and P=0.038 by Breslow test for progress free survival). A marginally significant association was found between AAL specific glycoconjugate expression and overall survival by univariate Cox regression analysis (p=0.059). Conclusions: Lower AAL specific glycoconjugate expression is a significant favorable prognostic factor for overall and progress free survival in CRC. This is the first report about the employment of AAL for histochemical analysis of cancer tissues. The binding characteristics of AAL means it has potential to become a powerful tool for the glycan investigation and clinical application.

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참고문헌

  1. Adamczyk B, Tharmalingam T, Rudd PM (2011). Glycans as cancer biomarkers. Biochim Biophys Acta, 1820, 1347-53.
  2. Allen HJ, Ahmed H, Matta KL (1998). Binding of synthetic sulfated ligands by human splenic galectin 1, a beta­galactoside-binding lectin. Glycoconj J, 15, 691-5. https://doi.org/10.1023/A:1006988515346
  3. Baldus SE, Zirbes TK, Hanisch FG, et al (2000) Thomsen-Friedenreich antigen presents as a prognostic factor incolorectal carcinoma: A clinicopathologic study of 264patients. Cancer, 88, 1536-43. https://doi.org/10.1002/(SICI)1097-0142(20000401)88:7<1536::AID-CNCR6>3.0.CO;2-W
  4. Balog CI, Stavenhagen K, Fung WL, et al (2012). N-glycosylation of colorectal cancer tissues: a liquid chromatographyand mass spectrometry-based investigation. Mol Cell Proteomics, 11, 571-85. https://doi.org/10.1074/mcp.M111.011601
  5. Chandrasekaran EV, Xue J, Neelamegham S, Matta KL (2006). The pattern of glycosyl- and sulfotransferase activitiesin cancer cell lines: a predictor of individual cancer-associated distinct carbohydrate structures for the structural identification of signature glycans. Carbohydr Res, 341,983-94. https://doi.org/10.1016/j.carres.2006.02.017
  6. Essentials of Glycobiology (2009). Cold Spring HarborLaboratory Press, Cold Spring Harbor (NY).
  7. Feng L, Sun H, Zhang Y, et al (2010). Structural insights into the recognition mechanism between an antitumor galectin AA Land the Thomsen-Friedenreich antigen. FASEB J, 24, 3861-8. https://doi.org/10.1096/fj.10-159111
  8. Ferlay J, Soerjomataram I, Ervik M, et al (2013). GLOBOCAN 2012 v1.0, Cancer incidence and mortality Worldwide: IARC Cancer Base, No. 11.
  9. Gunderson LL, Jessup JM, Sargent DJ, et al (2010). Revised TNcategorization for colon cancer based on national survival outcomes data. J Clin Oncol, 28, 264-71. https://doi.org/10.1200/JCO.2009.24.0952
  10. Huang GL, Guo HQ, Yang F, et al (2012) Activating transcriptionfactor 1 is a prognostic marker of colorectal cancer. Asian Pac J Cancer Prev, 13, 1053-7. https://doi.org/10.7314/APJCP.2012.13.3.1053
  11. Ideo H, Seko A, Ohkura T, et al (2002). High-affinity binding of recombinant human galectin-4 to SO(3)(-)-->3Galbeta1­->3GalNAc pyranoside. Glycobiology, 12, 199-208. https://doi.org/10.1093/glycob/12.3.199
  12. Ideo H, Seko A, Yamashita K (2005). Galectin-4 binds to sulfatedglycosphingolipids and carcinoembryonic antigen in patcheson the cell surface of human colon adenocarcinoma cells. J Biol Chem, 280, 4730-7. https://doi.org/10.1074/jbc.M410362200
  13. Indramanee S, Silsirivanit A, Pairojkul C, et al (2012). Aberrant glycosylation in cholangiocarcinoma demonstrated by lectin­histochemistry. Asian Pac J Cancer Prev, 13, 119-24.
  14. Itzkowitz SH, Yuan M, Montgomery CK, et al (1989). Expressionof Tn, sialosyl-Tn, and T antigens in human colon cancer. Cancer Res, 49, 197-204.
  15. Liang Y, Feng L, Tong X, et al (2009). Importance of nuclear localization for the apoptosis-induced activity of a fungal galectin AAL (Agrocybe aegerita lectin). Biochem BiophysRes Commun, 386, 437-42. https://doi.org/10.1016/j.bbrc.2009.06.054
  16. Meany DL, Chan DW (2011). Aberrant glycosylation associatedwith enzymes as cancer biomarkers. Clin Proteomics, 8, 7. https://doi.org/10.1186/1559-0275-8-7
  17. Qiu Y, Patwa TH, Xu L, et al (2008). Plasma glycoproteinprofiling for colorectal cancer biomarker identificationby lectin glycoarray and lectin blot. J Proteome Res, 7,1693-703. https://doi.org/10.1021/pr700706s
  18. Rambaruth ND, Greenwell P, Dwek MV (2012). The lectinHelix pomatia agglutinin recognizes O-GlcNAc containing glycoproteins in human breast cancer. Glycobiology, 22,839-48. https://doi.org/10.1093/glycob/cws051
  19. Reis CA, Osorio H, Silva L, et al (2010). Alterations inglycosylation as biomarkers for cancer detection. J Clin Pathol, 63, 322-9. https://doi.org/10.1136/jcp.2009.071035
  20. Schneider F, Kemmner W, Haensch W, et al (2001). Overexpressionof sialyltransferase CMP-sialic acid:Galbeta1, 3GalNAc-R alpha6-Sialyltransferase is related to poor patient survival in human colorectal carcinomas. Cancer Res, 61, 4605-11.
  21. Sethi MK, Thaysen-Andersen M, Smith JT, et al (2013). Comparative N-glycan profiling of colorectal cancer cell lines reveals unique bisecting GlcNAc and alpha-2,3-linkedsialic acid determinants are associated with membrane proteins of the more metastatic/aggressive cell lines. J Proteome Res, 13, 277-88.
  22. Storr SJ, Royle L, Chapman CJ, et al (2008). The O-linkedglycosylation of secretory/shed MUC1 from an advanced breast cancer patient's serum. Glycobiology, 18, 456-62. https://doi.org/10.1093/glycob/cwn022
  23. Szajda SD, Jankowska A, Zwierz K (2008). Carbohydratemarkers in colon carcinoma. Dis Markers, 25, 233-42. https://doi.org/10.1155/2008/206510
  24. Yehezkel G, Cohen L, Kliger A, et al (2012). O-linked beta-N­acetylglucosaminylation (O-GlcNAcylation) in primary andmetastatic colorectal cancer clones and effect of N-acetyl­beta-D-glucosaminidase silencing on cell phenotype andtranscriptome. J Biol Chem, 287, 28755-69. https://doi.org/10.1074/jbc.M112.345546
  25. Zhao C, Sun H, Tong X, Qi Y (2003). An antitumour lectinfrom the edible mushroom Agrocybe aegerita. Biochem J,374, 321-7. https://doi.org/10.1042/BJ20030300

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