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

Sarah Ambrose, Naheema Gordon, James Goldsmith, Wenbin Wei, Maurice Zeegers, Nicholas James, Margaret Knowles, Richard Bryan, Douglas Ward

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)
102 Downloads (Pure)

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.
Original languageEnglish
Pages (from-to)266-282
Number of pages17
JournalProteomes
Volume3
Issue number3
Early online date3 Sep 2015
DOIs
Publication statusPublished - 2015

Keywords

  • bladder cancer;
  • urine
  • lectin
  • Biomarker
  • glycoproteome

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