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MS analysis reveals O ‐methylation of L ‐lactate dehydrogenase from pancreatic ductal adenocarcinoma cells
Author(s) -
Zhou Weidong,
Capello Michela,
Fredolini Claudia,
Racanicchi Leda,
Piemonti Lorenzo,
Liotta Lance A.,
Novelli Francesco,
Petricoin Emanuel F.
Publication year - 2012
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201200017
Subject(s) - lactate dehydrogenase , methylation , pancreatic cancer , biochemistry , enzyme , chemistry , acetylation , microbiology and biotechnology , biology , cancer , gene , genetics
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 ( PTM s), and it has been reported that LDH was subjected to several PTM s, including phosphorylation, acetylation, and methylation. In this present work, we characterized the PTM s 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.