Center for Applied Proteomics and Molecular Medicine, George Mason University, Manassas, Virginia 20110, USA.
J Proteome Res. 2010 Jun 4;9(6):2929-36. doi: 10.1021/pr901109w.
Enolase is a key glycolytic enzyme that catalyzes the dehydration of 2-phosphoglycerate to phosphoenolpyruvate. Recently, enolase was revealed as an important protein in pathophysiological processes since it was found on the surface of hematopoietic cells and overexpressed in several tumor cells. Our previous studies demonstrated that alpha-enolase is up-regulated in pancreatic ductal adenocarcinoma (PDAC). In this present work, we further characterized the alpha-enolase from PDAC and normal pancreatic duct cells by mass spectrometry using LTQ-Orbitrap and identified multiple post-translational modifications of alpha-enolase, such as phosphorylation, acetylation, and methylation. The result showed that more acetylated lysines, methylated aspartic acids, and glutamic acids were found in PDAC cells than that of normal pancreatic duct cells.
烯醇化酶是一种关键的糖酵解酶，可催化 2-磷酸甘油酸脱水生成磷酸烯醇丙酮酸。最近，烯醇化酶被发现是一种在生理病理过程中起重要作用的蛋白质，因为它存在于造血细胞表面，并在几种肿瘤细胞中过度表达。我们之前的研究表明，α-烯醇化酶在胰腺导管腺癌（PDAC）中上调。在本工作中，我们进一步使用 LTQ-Orbitrap 通过质谱法对 PDAC 和正常胰腺导管细胞中的α-烯醇化酶进行了表征，并鉴定了α-烯醇化酶的多种翻译后修饰，如磷酸化、乙酰化和甲基化。结果表明，PDAC 细胞中存在更多的乙酰化赖氨酸、甲基天冬氨酸和谷氨酸，而正常胰腺导管细胞中则较少。
