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제105회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Posttranslational Arginine-Methylation of Lamin A/C during Myoblast Fusion

등록일
2010년 2월 24일 18시 39분 08초
접수번호
1349
발표코드
35P97포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 <발표Ⅳ>
발표형식
포스터
발표분야
분석화학
저자 및
공동저자
김수진, 이상원
고려대학교 화학과, Korea
Protein arginine methylation is one of the major posttranslational modifications regulating a various cellular functions such as RNA processing and DNA repair. Recent report showed the involvement of protein arginine methyltransferase (PRMT) 4 in the chromatin remodeling and gene expression during muscle differentiation in C2C12 cells. As 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. Interestingly, ω-NG, NG-asymmetric dimethylarginines (aDMA), and ω-NG, NG-symmetric dimethylarginines (sDMA) were found to be consistent during myoblast fusion. However, PRMT1 showed the highest activity during myoblast fusion and maintained thereafter, and PRMT5 reached the highest activity only after myoblast fusion. To identify the proteins modified by such PRMTs 2-DE gel was constructed by the total proteins before and after myoblast fusion, and protein spots on 2-DE with immunoreactive signals against aDMA (Asy 24) and sDMA (Sym 10) were identified by mass analysis. Among the proteins identified, lamin C2 was clarified as a protein to be dimethylated, and we discuss a role of posttranslational arginine methylation for myoblast fusion.

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