Proteome and phosphoproteome of primary cultured pig urothelial cells

Epithelial tissue lining the inner side of the urinary bladder is the most common target for bladder cancer‐related diseases. Bladders of freshly slaughtered pigs were utilised for a comprehensive analysis of the proteome and phosphoproteome of bladder epithelial cells. Following protein separation...

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Bibliographic Details
Published in:Electrophoresis 2011-12, Vol.32 (24), p.3600-3611
Main Authors: Verma, Nisha, Bäuerlein, Carolin, Pink, Mario, Rettenmeier, Albert W., Schmitz-Spanke, Simone
Format: Article
Language:English
Subjects:
Animals
Bladder epithelial cells
Cells, Cultured
Electrophoresis, Gel, Two-Dimensional
Lanthanum
Phosphoproteins - analysis
Phosphoproteins - chemistry
Phosphoproteins - metabolism
Phosphoproteome
Proteome - analysis
Proteome - chemistry
Proteome - metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Swine
Two-dimensional electrophoresis
Urinary Bladder - chemistry
Urinary Bladder - cytology
Urinary Bladder - metabolism
Urothelium - chemistry
Urothelium - cytology
Urothelium - metabolism
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Summary:Epithelial tissue lining the inner side of the urinary bladder is the most common target for bladder cancer‐related diseases. Bladders of freshly slaughtered pigs were utilised for a comprehensive analysis of the proteome and phosphoproteome of bladder epithelial cells. Following protein separation by 2‐D gel electrophoresis and identification by matrix‐assisted laser desorption/ionisation time‐of‐flight mass spectrometry (MALDI‐TOF‐MS) the first proteome and phosphoproteome maps of pig urinary bladder epithelial cells (PUBEC) were established. A total of 120 selected protein spots were identified. By using the La3+ enrichment method further developed in our laboratory we identified 31 phosphoproteins with minimal contamination by non‐phosphopeptides. The 2‐DE map of pig urothelial cells may prove as a useful tool for studies on uroepithelial biology, and the analysed phosphoproteins expression pattern, together with the whole cell proteome, will be helpful for identifying the proteins involved in bladder‐related diseases.
ISSN:0173-0835
1522-2683
DOI:10.1002/elps.201100220