期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1814, 期 2, 页码 308-317出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2010.11.006
关键词
Skeletal muscle differentiation; Lamin A/C; Mass spectrometry; Protein arginine methylation
资金
- 21C Frontier Functional Proteomics Project [FPR08A1-010]
- Converging Research Center for Mass Spectrometric Diagnosis [2010K001300]
- Korean Ministry of Education Science Technology [NRF20100020209]
- Korea University
- Korean National Cancer Center [1010050]
- Korea Health Promotion Institute [1010050] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Protein arginine methylation is a major posttranslational modification that regulates various cellular functions, such as RNA processing and DNA repair. A recent report showed the involvement of protein arginine methyltransferase (PRMT) 4 in chromatin remodeling and gene expression during muscle differentiation in C2C12 cells. Because the fusion of myoblasts is a unique phenomenon observed in skeletal muscle differentiation, the present study focused on the expression and activities of PRMTs during myoblast fusion in primary rat skeletal muscle. N-G. N-G-asymmetric dimethylarginines (aDMA) and N-G, N-,N-G-symmetric dimethylarginines (sDMA) were both found consistently throughout myoblast fusion. However, PRMT1 exhibited the highest activity during myoblast fusion and maintained the elevated activity thereafter, whereas PRMT5 reached its highest activity only after myoblast fusion. To identify the proteins modified by such PRMTs, we conducted 2-dimensional electrophoresis (2-DE) of total proteins before and after myoblast fusion, and protein spots on the 2-DE gel immunoreactive for aDMA and sDMA were identified by mass spectrometric analysis. Among the proteins identified, lamin C2 was in particular observed to be dimethylated. Arginine methylation of lamin may therefore be important for muscle development and maintenance. (C) 2010 Elsevier B.V. All rights reserved.
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