Quantitative Glycome Analysis of N-Glycan Patterns in Bladder Cancer vs Normal Bladder Cells Using an Integrated Strategy

Yang, Ganglong; Tan, Zengqi; Lü, Wei; Guo, Jia; Yu, Hanjie; Yu, Jinhua; Sun, Chao; Qi, Xiaowei; Guan, Feng

doi:10.1021/pr5006026

Cited by 62 publications

(63 citation statements)

References 53 publications

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“…Lectin microarray technology has been widely used for glycosylation studies in recent years (Kang et al, 2012; Li, Y. et al, 2013; Qin et al, 2013; Xin et al, 2014; Yang et al, 2015). It is a high-throughput technique which could reveal glycoforms using minimal sample preparation without release or derivatization of glycans and it could observe multiple and distinct binding interactions simultaneously (Pilobello et al, 2005; Fry et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Assessment of Hepatocellular Carcinoma Metastasis Glycobiomarkers Using Advanced Quantitative N-glycoproteome Analysis

Liu

Shang

et al. 2017

Front. Physiol.

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Hepatocelluar carcinoma (HCC) is one of the most common malignant tumors with high incidence of metastasis. Glycosylation is involved in fundamental molecular and cell biology process occurring in cancer including metastasis formation. In this study, lectin microarray, lectin blotting, lectin affinity chromatography and tandem 18O stable isotope labeling coupled with liquid chromatography-mass spectrometer (LC-MS) analysis were applied to quantify the changes in N-glycosite occupancy for HCC metastasis serum. Firstly, lectin microarray was used to screen glycoforms and Phaseolus vulgaris Leucoagglutinin (PHA-L) reactive structure (β1,6-GlcNAc branched N-glycan) was found to be increased significantly in HCC patients with metastasis compared with those with non-metastasis. Then, PHA-L affinity glycoproteins were enriched followed by N-glycosite occupancy measurement with strategy of tandem 18O stable isotope labeling. 11 glycoproteins with significantly changed N-glycosite occupancy were identified, they were associated with cell migration, invasion and adhesion through p38 mitogen-activated protein kinase signaling pathway and nuclear factor kappa B signaling pathway. Quantification of N-glycosite occupancy for PHA-L reactive glycoproteins could help to discover important glycoproteins of potential clinically significance in terms of HCC etiology. Also, understanding of N-glycosite occupancy alterations will aid the characterization of molecular mechanism of HCC metastasis as well as establishment of novel glycobiomarkers.

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Section: Discussionmentioning

confidence: 99%

Assessment of Hepatocellular Carcinoma Metastasis Glycobiomarkers Using Advanced Quantitative N-glycoproteome Analysis

Liu

Shang

et al. 2017

Front. Physiol.

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“…A recent paper by Yang et al reported that the binding of many lectins differed significantly between a normal urothelial cell line (HCV29) and several bladder cancer cell lines, and went on to show increased binding of LCA and SNA and decreased binding of ConA to bladder cancer tissue relative to adjacent normal tissue [27]. The use of different reference cell lines (NHU-TERT and UROtsa) in our study may be the reason that we did not see clear differences between the non-cancer and cancer cell lines, although differences between individual cell lines were observed.…”

Section: Discussionmentioning

confidence: 99%

Use of Aleuria alantia Lectin Affinity Chromatography to Enrich Candidate Biomarkers from the Urine of Patients with Bladder Cancer

et al. 2015

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Developing a urine test to detect bladder tumours with high sensitivity and specificity is a key goal in bladder cancer research. We hypothesised that bladder cancer-specific glycoproteins might fulfill this role. Lectin-ELISAs were used to study the binding of 25 lectins to 10 bladder cell lines and serum and urine from bladder cancer patients and non-cancer controls. Selected lectins were then used to enrich glycoproteins from the urine of bladder cancer patients and control subjects for analysis by shotgun proteomics. None of the lectins showed a strong preference for bladder cancer cell lines over normal urothlelial cell lines or for urinary glycans from bladder cancer patients over those from non-cancer controls. However, several lectins showed a strong preference for bladder cell line glycans over serum glycans and are potentially useful for enriching glycoproteins originating from the urothelium in urine. Aleuria alantia lectin affinity chromatography and shotgun proteomics identified mucin-1 and golgi apparatus protein 1 as proteins warranting further investigation as urinary biomarkers for low-grade bladder cancer. Glycosylation changes in bladder cancer are not reliably detected by measuring lectin binding to unfractionated proteomes, but it is possible that more specific reagents and/or a focus on individual proteins may produce clinically useful biomarkers.

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“…Lectin microarray analysis was performed as described previously [39–41]. In brief, 37 commercial lectins from Vector Laboratories (Burlingame, CA, USA), Sigma-Aldrich (St Louis, MO, USA), and Calbiochem Merck (Darmstadt, Germany) were immobilized on a solid support at high spatial density.…”

Section: Methodsmentioning

confidence: 99%

Identification of aberrantly expressed glycans in gastric cancer by integrated lectin microarray and mass spectrometric analyses

Guan

et al. 2016

Oncotarget

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Cancer progression is usually associated with alterations of glycan expression patterns. Little is known regarding global glycomics in gastric cancer, the most common type of epithelial cancer. We integrated lectin microarray and mass spectrometry (MS) methods to profile glycan expression in three gastric cancer cell lines (SGC-7901, HGC-27, and MGC-803) and one normal gastric epithelial cell line (GES-1). Significantly altered glycans were confirmed by lectin staining and MALDI-TOF/TOF-MS. The three cancer cell lines showed increased levels of core-fucosylated N-glycans, GalNAcα-Ser/Thr (Tn antigen), and Sia2-6Galβ1-4GlcNAc N-glycans, but reduced levels of biantennary N-glycans, Galβ1-3GalNAcα-Ser/Thr (T antigen), and (GlcNAc)n N-glycans. Lectin histochemistry was used to validate aberrant expression of four representative glycans (core-fucosylation, Sia2-6Galβ1-4GlcNAc, biantennary N-glycans, T antigen, recognized respectively by lectins LCA, SNA, PHA-E+L, and ACA) in clinical gastric cancer samples. Lower binding capacity for ACA was correlated with significantly poorer patient prognosis. Our findings indicate for the first time that glycans recognized by LCA, ACA, and PHA-E+L are aberrantly expressed in gastric cancer, and suggest that ACA is a potential prognostic factor for gastric cancer.

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Quantitative Glycome Analysis of N-Glycan Patterns in Bladder Cancer vs Normal Bladder Cells Using an Integrated Strategy

Cited by 62 publications

References 53 publications

Assessment of Hepatocellular Carcinoma Metastasis Glycobiomarkers Using Advanced Quantitative N-glycoproteome Analysis

Assessment of Hepatocellular Carcinoma Metastasis Glycobiomarkers Using Advanced Quantitative N-glycoproteome Analysis

Use of Aleuria alantia Lectin Affinity Chromatography to Enrich Candidate Biomarkers from the Urine of Patients with Bladder Cancer

Identification of aberrantly expressed glycans in gastric cancer by integrated lectin microarray and mass spectrometric analyses

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