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Proteomic identification of cytosolic proteins that undergo arginine methylation during rat liver regeneration
Author(s) -
An Sinae,
Yun Miyong,
Park Yun Gyu,
Park Gil Hong
Publication year - 2009
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.200800772
Subject(s) - methylation , arginine , protein methylation , liver regeneration , protein arginine methyltransferase 5 , biology , oxidative stress , biochemistry , microbiology and biotechnology , cytosol , regeneration (biology) , methyltransferase , amino acid , enzyme , gene
Protein arginine methylation plays a crucial role in signal transduction, protein–protein interactions, and transcriptional regulation. Previously, we showed that protein arginine methyltransferase activity increased significantly during rat liver regeneration. In the present study, in vivo arginine methylation during liver regeneration was investigated. The presence of symmetric or asymmetric dimethylarginine in proteins varied significantly at the early stage of regeneration after partial hepatectomy. The nature of the 31 proteins that showed significant variations in arginine methylation were identified using 2‐DE and MS. Many of these proteins were oxidative stress‐related or oxidation‐prone proteins that exhibited significant variations in arginine methylation without changes in their expression levels. The oxidation of some of the oxidation‐prone proteins under oxidative stress such as carbonic anhydrase 3 decreased with increased levels of arginine methylation, whereas normal levels of protein oxidation were recovered as arginine methylation subsided. Taken together, this study demonstrated that time‐dependent methylation events in hepatocytes during the early period of rat liver regeneration may participate in the regulation or protection of protein activities, thus presenting a significant new insight into the biology of proliferating cells at the post‐translational modification level and into a key population of proteins involved in these processes.