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Proteomes 2015, 3(3), 266-282; doi:10.3390/proteomes3030266

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

1
School of Cancer Sciences, University of Birmingham, Birmingham B15 2TT, UK
2
Department of Complex Genetics, NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University Medical Centre, Maastricht 6200 MD, The Netherlands
3
Clinical Trials Unit, University of Warwick, Coventry CV4 7AL, UK
4
Section of Experimental Oncology, Leeds Institute of Cancer and Pathology, St James's' University Hospital, Beckett Street, Leeds LS9 7TF, UK
*
Author to whom correspondence should be addressed.
Academic Editor: Michael A. Tainsky
Received: 30 June 2015 / Revised: 25 August 2015 / Accepted: 27 August 2015 / Published: 3 September 2015
(This article belongs to the Special Issue Proteomic Cancer Biomarkers in Human Biofluids)
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Abstract

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. View Full-Text
Keywords: bladder cancer; urine; biomarker; lectin; glycoproteome bladder cancer; urine; biomarker; lectin; glycoproteome
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Ambrose, S.R.; Gordon, N.S.; Goldsmith, J.C.; Wei, W.; Zeegers, M.P.; James, N.D.; Knowles, M.A.; Bryan, R.T.; Ward, D.G. Use of Aleuria alantia Lectin Affinity Chromatography to Enrich Candidate Biomarkers from the Urine of Patients with Bladder Cancer. Proteomes 2015, 3, 266-282.

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