Pinellia pedatisecta agglutinin‑based lectin blot analysis distinguishes between glycosylation patterns in various cancer cell lines

Li,Na; Dong,Guoping; Wang,Shuanghui; Zhu,Shiping; Shen,Yi; Li,Gongchu

doi:10.3892/ol.2014.2201

Pinellia pedatisecta agglutinin‑based lectin blot analysis distinguishes between glycosylation patterns in various cancer cell lines

Authors:
- Na Li
- Guoping Dong
- Shuanghui Wang
- Shiping Zhu
- Yi Shen
- Gongchu Li
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Affiliations: College of Life Sciences, Zhejiang Sci‑Tech University, Hangzhou, Zhejiang 310018, P.R. China
Published online on: May 30, 2014 https://doi.org/10.3892/ol.2014.2201
Pages: 837-840

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Abstract

The analysis of altered glycosylation patterns may provide biomarkers for various types of cancer. The present study developed a Pinellia pedatisecta agglutinin (PPA)‑based lectin blot analysis technique, which was used to analyze the glycosylation patterns in various types of cancer cells. Results showed that a typical band located between 47 and 85 kDa was obtained in the HL60 leukemia cells, whereas three typical bands located between 20 and 47 kDa were observed in the Kasumi‑1 leukemia cells. For the PLC, BEL‑7404, Huh7 and H1299 solid tumor cell lines, different band patterns were detected, with bands typically located between 55 and 100 kDa. The findings of the present study show that PPA‑based lectin blot analysis is capable of distinguishing between glycosylation patterns in leukemia and solid tumor cell lines. The glycofiles detected using PPA‑based lectin blot analysis may provide a ‘glycosylation fingerprint’ for a variety of cancer cells, which may be valuable for cancer prognosis and diagnosis.

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1	Mattaini KR and Vander Heiden MG: Cancer. Glycosylation to adapt to stress. Science. 337:925–926. 2012.
2	Kim YS, Ahn YH, Song KJ, et al: Overexpression and β-1,6-N-acetylglucosaminylation-initiated aberrant glycosylation of TIMP-1: a ‘double whammy’ strategy in colon cancer progression. J Biol Chem. 287:32467–32478. 2012.
3	Saeland E, Belo AI, Mongera S, et al: Differential glycosylation of MUC1 and CEACAM5 between normal mucosa and tumour tissue of colon cancer patients. Int J Cancer. 131:117–128. 2012.
4	Sharon N and Lis H: Lectins as cell recognition molecules. Science. 246:227–234. 1989.
5	Fry SA, Afrough B, Lomax-Browne HJ, et al: Lectin microarray profiling of metastatic breast cancers. Glycobiology. 21:1060–1070. 2011.
6	Drake PM, Schilling B, Niles RK, et al: Lectin chromatography/mass spectrometry discovery workflow identifies putative biomarkers of aggressive breast cancers. J Proteome Res. 11:2508–2520. 2012.
7	Wu J, Xie X, Liu Y, et al: Identification and confirmation of differentially expressed fucosylated glycoproteins in the serum of ovarian cancer patients using a lectin array and LC-MS/MS. J Proteome Res. 11:4541–4552. 2012.
8	Li C, Simeone DM, Brenner DE, et al: Pancreatic cancer serum detection using a lectin/glyco-antibody array method. J Proteome Res. 8:483–492. 2009.
9	Batabyal SK, Majhi R and Basu PS: Clinical utility of the interaction between lectin and serum prostate specific antigen in prostate cancer. Neoplasma. 56:68–71. 2009.
10	Ahn YH, Shin PM, Oh NR, et al: A lectin-coupled, targeted proteomic mass spectrometry (MRM MS) platform for identification of multiple liver cancer biomarkers in human plasma. J Proteomics. 75:5507–5515. 2012.
11	Li GC, Li N, Zhang YH, et al: Mannose-exposing myeloid leukemia cells detected by the sCAR-PPA fusion protein. Int J Hematol. 89:611–617. 2009.
12	Chen K, Yang X, Wu L, et al: Pinellia pedatisecta agglutinin targets drug resistant K562/ADR leukemia cells through binding with sarcolemmal membrane associated protein and enhancing macrophage phagocytosis. PLoS One. 8:e743632013.
13	Lu Q, Li N, Luo J, et al: Pinellia pedatisecta agglutinin interacts with the methylosome and induces cancer cell death. Oncogenesis. 1:e292012.
14	Cao J, Guo S, Arai K, Lo EH and Ning M: Studying extracellular signaling utilizing a glycoproteomic approach: lectin blot surveys, a first and important step. Methods Mol Biol. 1013:227–233. 2013.
15	Qiu Y, Patwa TH, Xu L, et al: Plasma glycoprotein profiling for colorectal cancer biomarker identification by lectin glycoarray and lectin blot. J Proteome Res. 7:1693–1703. 2008.
16	Ferguson RE, Jackson DH, Hutson R, et al: Detection of glycosylation changes in serum and tissue proteins in cancer by lectin blotting. Adv Exp Med Biol. 564:113–114. 2005.
17	Clark D and Mao L: Cancer biomarker discovery: lectin-based strategies targeting glycoproteins. Dis Markers. 33:1–10. 2012.
18	Mun JY, Lee KJ, Kim YJ, et al: Development of fluorescent probes for the detection of fucosylated N-glycans using an Aspergillus oryzae lectin. Appl Microbiol Biotechnol. 93:251–260. 2012.
19	Park SY, Lee SH, Kawasaki N, et al: α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: a combinatorial approach for development of glycan biomarkers. Int J Cancer. 130:2366–2376. 2012.
20	Xu Q, Isaji T, Lu Y, et al: Roles of N-acetylglucosaminyltransferase III in epithelial-to-mesenchymal transition induced by transforming growth factor β1 (TGF-β1) in epithelial cell lines. J Biol Chem. 287:16563–16574. 2012.