In this present work, we characterized the phosphoproteomes of pancreatic ductal adenocarcinoma (PDAC) cells and normal pancreatic duct cells by mass spectrometry using LTQ-Orbitrap. We identified more than 700 phosphoproteins from each sample, and revealed differential phosphorylation of many proteins involved in cell adhesion, cell junction, and cytoskeleton. Since post-translational phosphorylation is a common and important mechanism of acute and reversible regulation of protein function in mammalian cells, an understanding of differential phosphorylation of these proteins and resulting signal transduction changes in PDAC will help in comprehending the complex dynamics of tumor invasion and metastasis in pancreatic cancer.

PHOSPHOPROTEOMIC ANALYSIS OF PANCREATIC DUCTAL ADENOCARCINOMA CELLS REVEALS DIFFERENTIAL PHOSPHORYLATION OF CELL ADHESION, CELL JUNCTION AND STRUCTURAL PROTEINS

CAPELLO, Michela;FREDOLINI, CLAUDIA;NOVELLI, Francesco;
2011-01-01

Abstract

In this present work, we characterized the phosphoproteomes of pancreatic ductal adenocarcinoma (PDAC) cells and normal pancreatic duct cells by mass spectrometry using LTQ-Orbitrap. We identified more than 700 phosphoproteins from each sample, and revealed differential phosphorylation of many proteins involved in cell adhesion, cell junction, and cytoskeleton. Since post-translational phosphorylation is a common and important mechanism of acute and reversible regulation of protein function in mammalian cells, an understanding of differential phosphorylation of these proteins and resulting signal transduction changes in PDAC will help in comprehending the complex dynamics of tumor invasion and metastasis in pancreatic cancer.
2011
4
170
178
http://dx.doi.org/10.4172/jpb.1000186
Phosphoproteomics; PAncreatic cancer
Zhou W; Capello M; Fredolini C; Racanicchi L; Piemonti L; Liotta LA.; Novelli F ; Petricoin EF
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2318/132503
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