| Content Provider |
World Health Organization (WHO)-Global Index Medicus |
| Author |
Du, Yipeng Cai, Tanxi Li, Tingting Xue, Peng Zhou, Bo He, Xiaolong Wei, Peng Liu, Pingsheng Yang, Fuquan Wei, Taotao |
| Description |
Author Affiliation: Du Y ( From the National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China); Cai T ( §Laboratory of Protein and Peptide Pharmaceuticals & Laboratory of Proteomics, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China); Li T ( ¶Department of Biomedical Informatics, Peking University Health Science Center, Beijing 100191, China); Xue P ( §Laboratory of Protein and Peptide Pharmaceuticals & Laboratory of Proteomics, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China); Zhou B ( From the National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China); He X ( From the National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China); Wei P ( From the National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China); Liu P ( From the National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China); Yang F ( §Laboratory of Protein and Peptide Pharmaceuticals & Laboratory of Proteomics, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China); Wei T ( From the National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China) |
| Abstract |
Protein lysine malonylation, a newly identified protein post-translational modification (PTM), has been proved to be evolutionarily conserved and is present in both eukaryotic and prokaryotic cells. However, its potential roles associated with human diseases remain largely unknown. In the present study, we observed an elevated lysine malonylation in a screening of seven lysine acylations in liver tissues of db/db mice, which is a typical model of type 2 diabetes. We also detected an elevated lysine malonylation in ob/ob mice, which is another model of type 2 diabetes. We then performed affinity enrichment coupled with proteomic analysis on liver tissues of both wild-type (wt) and db/db mice and identified a total of 573 malonylated lysine sites from 268 proteins. There were more malonylated lysine sites and proteins in db/db than in wt mice. Five proteins with elevated malonylation were verified by immunoprecipitation coupled with Western blot analysis. Bioinformatic analysis of the proteomic results revealed the enrichment of malonylated proteins in metabolic pathways, especially those involved in glucose and fatty acid metabolism. In addition, the biological role of lysine malonylation was validated in an enzyme of the glycolysis pathway. Together, our findings support a potential role of protein lysine malonylation in type 2 diabetes with possible implications for its therapy in the future. |
| File Format |
HTM / HTML |
| ISSN |
15359476 |
| e-ISSN |
15359484 |
| DOI |
10.1074/mcp.M114.041947 |
| Journal |
Molecular & Cellular Proteomics |
| Issue Number |
1 |
| Volume Number |
14 |
| Language |
English |
| Publisher |
American Society for Biochemistry and Molecular Biology |
| Publisher Date |
2015-01-01 |
| Publisher Place |
United States |
| Access Restriction |
Open |
| Subject Keyword |
Discipline Proteomics Diabetes Mellitus, Type 2 Metabolism Lysine Protein Processing, Post-translational Animals Disease Models, Animal Liver Mice, Inbred C57bl Obesity Proteins Research Support, Non-u.s. Gov't |
| Content Type |
Text |
| Resource Type |
Article |
| Subject |
Medicine Analytical Chemistry Molecular Biology Biochemistry |
