质谱分析揭示胰腺癌细胞中丙酮酸激酶的 O-甲基化。
Mass spectrometric analysis reveals O-methylation of pyruvate kinase from pancreatic cancer cells.
机构信息
Center for Applied Proteomics and Molecular Medicine, George Mason University, Manassas, VA 20110, USA.
出版信息
Anal Bioanal Chem. 2013 May;405(14):4937-43. doi: 10.1007/s00216-013-6880-7. Epub 2013 Mar 19.
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.
摘要
丙酮酸激酶（PK）是一种重要的糖酵解酶，可催化磷酸烯醇丙酮酸去磷酸化生成丙酮酸。M1 同工酶的剪接变体 M2 型丙酮酸激酶（PKM2）在许多癌细胞中过度表达，PKM2 已被作为诊断检测的潜在肿瘤标志物以及癌症治疗的靶点进行研究。为了促进对 PK 的鉴定和表征，我们通过电泳和质谱法研究了来自胰腺癌细胞和正常胰腺导管细胞的酶，并从 PK 中鉴定出多个 O-甲基化残基。这些发现增进了我们对 PK 的生化特性的了解，对于理解其在细胞中的生物学功能将非常重要。
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