MS analysis reveals O-methylation of L-lactate dehydrogenase from pancreatic ductal adenocarcinoma cells

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

Research output: Contribution to journalArticlepeer-review

Abstract

L-lactate dehydrogenase (LDH) converts pyruvate to lactate when oxygen is absent or in short supply, and the enzyme plays a crucial role in cancer metabolism. The functions of many mammalian proteins are modulated by posttranslational modifications (PTMs), and it has been reported that LDH was subjected to several PTMs, including phosphorylation, acetylation, and methylation. In this present work, we characterized the PTMs of LDH from pancreatic ductal adenocarcinoma (PDAC) cells by electrophoresis and mass spectrometry, and identified 13 O-methylated residues from the enzyme. In addition, our qualitative analysis revealed differential methylation of LDH from normal duct cells. The preliminary findings from this study provide important biochemical information toward further understanding of the LDH modifications and their functional significance in pathophysiological processes of pancreatic cancer.

Original languageEnglish
Pages (from-to)1850-1854
Number of pages5
JournalElectrophoresis
Volume33
Issue number12
DOIs
Publication statusPublished - Jul 2012

Keywords

  • L-lactate dehydrogenase
  • Mass spectrometry
  • Metabolism
  • Methylation
  • Pancreatic ductal adenocarcinoma

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry

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