Premium
Proteome and phosphoproteome of primary cultured pig urothelial cells
Author(s) -
Verma Nisha,
Bäuerlein Carolin,
Pink Mario,
Rettenmeier Albert W.,
SchmitzSpanke Simone
Publication year - 2011
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201100220
Subject(s) - proteome , proteomics , biology , two dimensional gel electrophoresis , bladder cancer , gel electrophoresis , mass spectrometry , microbiology and biotechnology , chemistry , biochemistry , cancer , chromatography , genetics , gene
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 La 3+ 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.