Mass spectrometry analysis of the post-translational modifications of r-enolase from pancreatic ductal adenocarcinoma cells

Weidong Zhou; Michela Capello; Claudia Fredolini; Lorenzo Piemonti; Lance A. Liotta; Francesco Novelli; Emanuel F. Petricoin

doi:10.1021/pr901109w

Mass spectrometry analysis of the post-translational modifications of r-enolase from pancreatic ductal adenocarcinoma cells

Weidong Zhou^*, Michela Capello, Claudia Fredolini, Lorenzo Piemonti, Lance A. Liotta, Francesco Novelli, Emanuel F. Petricoin

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

64 Scopus citations

Abstract

Enolase is a key glycolytic enzyme that catalyzes the dehydration of 2-phosphoglycerate to phosphoenolpyruvate. Recently, enolase was revealed as an important protein in pathophysiological processes since it was found on the surface of hematopoietic cells and overexpressed in several tumor cells. Our previous studies demonstrated that R-enolase is up-regulated in pancreatic ductal adenocarcinoma (PDAC). In this present work, we further characterized the R-enolase from PDAC and normal pancreatic duct cells by mass spectrometry using LTQ-Orbitrap and identified multiple post-translational modifications of R-enolase, such as phosphorylation, acetylation, and methylation. The result showed that more acetylated lysines, methylated aspartic acids, and glutamic acids were found in PDAC cells than that of normal pancreatic duct cells.

Original language	English
Pages (from-to)	2929-2936
Number of pages	8
Journal	Journal of Proteome Research
Volume	9
Issue number	6
DOIs	https://doi.org/10.1021/pr901109w
State	Published - 4 Jun 2010
Externally published	Yes

Keywords

LTQ-Orbitrap
acetylation
enolase
mass spectrometry
methylation
pancreatic ductal adenocarcinoma
phosphorylation
post-translational modification

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10.1021/pr901109w

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title = "Mass spectrometry analysis of the post-translational modifications of r-enolase from pancreatic ductal adenocarcinoma cells",

abstract = "Enolase is a key glycolytic enzyme that catalyzes the dehydration of 2-phosphoglycerate to phosphoenolpyruvate. Recently, enolase was revealed as an important protein in pathophysiological processes since it was found on the surface of hematopoietic cells and overexpressed in several tumor cells. Our previous studies demonstrated that R-enolase is up-regulated in pancreatic ductal adenocarcinoma (PDAC). In this present work, we further characterized the R-enolase from PDAC and normal pancreatic duct cells by mass spectrometry using LTQ-Orbitrap and identified multiple post-translational modifications of R-enolase, such as phosphorylation, acetylation, and methylation. The result showed that more acetylated lysines, methylated aspartic acids, and glutamic acids were found in PDAC cells than that of normal pancreatic duct cells.",

keywords = "LTQ-Orbitrap, acetylation, enolase, mass spectrometry, methylation, pancreatic ductal adenocarcinoma, phosphorylation, post-translational modification",

author = "Weidong Zhou and Michela Capello and Claudia Fredolini and Lorenzo Piemonti and Liotta, {Lance A.} and Francesco Novelli and Petricoin, {Emanuel F.}",

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doi = "10.1021/pr901109w",

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T1 - Mass spectrometry analysis of the post-translational modifications of r-enolase from pancreatic ductal adenocarcinoma cells

AU - Zhou, Weidong

AU - Capello, Michela

AU - Fredolini, Claudia

AU - Piemonti, Lorenzo

AU - Liotta, Lance A.

AU - Novelli, Francesco

AU - Petricoin, Emanuel F.

PY - 2010/6/4

Y1 - 2010/6/4

N2 - Enolase is a key glycolytic enzyme that catalyzes the dehydration of 2-phosphoglycerate to phosphoenolpyruvate. Recently, enolase was revealed as an important protein in pathophysiological processes since it was found on the surface of hematopoietic cells and overexpressed in several tumor cells. Our previous studies demonstrated that R-enolase is up-regulated in pancreatic ductal adenocarcinoma (PDAC). In this present work, we further characterized the R-enolase from PDAC and normal pancreatic duct cells by mass spectrometry using LTQ-Orbitrap and identified multiple post-translational modifications of R-enolase, such as phosphorylation, acetylation, and methylation. The result showed that more acetylated lysines, methylated aspartic acids, and glutamic acids were found in PDAC cells than that of normal pancreatic duct cells.

AB - Enolase is a key glycolytic enzyme that catalyzes the dehydration of 2-phosphoglycerate to phosphoenolpyruvate. Recently, enolase was revealed as an important protein in pathophysiological processes since it was found on the surface of hematopoietic cells and overexpressed in several tumor cells. Our previous studies demonstrated that R-enolase is up-regulated in pancreatic ductal adenocarcinoma (PDAC). In this present work, we further characterized the R-enolase from PDAC and normal pancreatic duct cells by mass spectrometry using LTQ-Orbitrap and identified multiple post-translational modifications of R-enolase, such as phosphorylation, acetylation, and methylation. The result showed that more acetylated lysines, methylated aspartic acids, and glutamic acids were found in PDAC cells than that of normal pancreatic duct cells.

KW - LTQ-Orbitrap

KW - acetylation

KW - enolase

KW - mass spectrometry

KW - methylation

KW - pancreatic ductal adenocarcinoma

KW - phosphorylation

KW - post-translational modification

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JO - Journal of Proteome Research

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Mass spectrometry analysis of the post-translational modifications of r-enolase from pancreatic ductal adenocarcinoma cells

Abstract

Keywords

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