期刊
ELECTROPHORESIS
卷 33, 期 12, 页码 1850-1854出版社
WILEY
DOI: 10.1002/elps.201200017
关键词
L-lactate dehydrogenase; Mass spectrometry; Metabolism; Methylation; Pancreatic ductal adenocarcinoma
资金
- Associazione Italiana Ricerca sul Cancro (AIRC) [5548]
- Fondazione San Paolo (Special Project Oncology)
- Ministero della Salute: Progetto integrato Oncologia
- Regione Piemonte: Ricerca Industriale e Sviluppo recompetitivo (BIOPRO)
- Regione Piemonte: Ricerca Industriale e Sviluppo recompetitivo (ONCOPROT)
- Ricerca Industriale Converging Technologies (BIOTHER)
- Progetti strategici su tematiche di interesse regionale o sovra regionale (IMMONC)
- Ricerca Sanitaria Finalizzata
- Ricerca Sanitaria Applicata
- European Pancreatic Cancer-Tumor-Microenvironment Network (EPC-TM-Net) [256974]
- Ministero dell'Istruzione e della Ricerca
- Progetti di Rilevante Interesse Nazionale (MIUR PRIN)
- College of Science at George Mason University
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据