Mass spectrometric analysis reveals O-methylation of pyruvate kinase from pancreatic cancer cells

Weidong Zhou*, Michela Capello, Claudia Fredolini, Leda Racanicchi, Erica Dugnani, Lorenzo Piemonti, Lance A. Liotta, Francesco Novelli, Emanuel F. Petricoin

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Pyruvate kinase (PK) is an important glycolytic enzyme that catalyzes the dephosphorylation of phosphoenolpyruvate to pyruvate. Human PK isozyme M2 (PKM2), a splice variant of M1, is overexpressed in many cancer cells, and PKM2 has been investigated as a potential tumor marker for diagnostic assays and as a target for cancer therapy. To facilitate identification and characterization of PK, we studied the enzyme from pancreatic cancer cells and normal pancreatic duct cells by electrophoresis and mass spectrometry, and identified multiple O-methylated residues from PK. These findings advance our knowledge of the biochemical properties of PK and will be important in understanding its biological function in cells.

Original languageEnglish
Pages (from-to)4937-4943
Number of pages7
JournalAnalytical and Bioanalytical Chemistry
Volume405
Issue number14
DOIs
StatePublished - May 2013
Externally publishedYes

Keywords

  • Mass spectrometry
  • Metabolism
  • Methylation
  • PKM2
  • Pancreatic cancer

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