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

Research output: Contribution to journalArticlepeer-review

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 languageEnglish
Pages (from-to)2929-2936
Number of pages8
JournalJournal of Proteome Research
Volume9
Issue number6
DOIs
Publication statusPublished - Jun 4 2010

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

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