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

Zhou, Weidong; Capello, Michela; Fredolini, Claudia; Racanicchi, Leda; Dugnani, Erica; Piemonti, Lorenzo; Liotta, Lance; Novelli, Francesco; Petricoin, Emanuel

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. [Figure not available: see fulltext.]

PYRUVATE kinase; MASS spectrometry; PANCREATIC cancer; CANCER cells; METHYLATION

Analytical & Bioanalytical Chemistry, 2013, Vol 405, Issue 14, p4937

1618-2642

Academic Journal

10.1007/s00216-013-6880-7