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A study on the effect of myogenin transcription factor modification by O-GlcNAc during differentiation from myoblast to myocyte

첫 페이지 보기
  • 발행기관
    한국당과학회 바로가기
  • 간행물
    한국당과학회 학술대회 바로가기
  • 통권
    2013 한국당과학회 하계학술대회 (2013.08)바로가기
  • 페이지
    pp.87-87
  • 저자
    Hanbyeol Kim, HoJung Seo, SangYoon Park, Jin Won Cho
  • 언어
    영어(ENG)
  • URL
    https://www.earticle.net/Article/A212769

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원문정보

초록

영어
β-O-linked N-acetylglucosamine(O-GlcNAc) is dynamic post-translational modification in nucleus and cytosol and it is regulated by O-GlcNAc transferase(OGT) and O-GlcNAcase. Many proteins, such as transcription factors, enzymes, cytoskeletal proteins, ribosomal proteins and chaperones have been identified to be modified with O-GlcNAc. O-GlcNAc modification modifies at their Ser/Thr residues and affects their functions. The hexosamine biosynthesis pathway takes about 5% of glucose in total glucose flux, and it’s final product is UDP-GlcNAc, which is source of O-GlcNAc modification. O-GlcNAc modification is reported to involve in skeletal muscle metabolism and development process. We studied whether O-GlcNAc modification is involved in differentiation in myoblast C2C12 cell. We observed that total O-GlcNAc modification level was dynamically changed during myogenesis. After treatment NButGT, we observed that myogenin expression level decreased. Using RT PCR, we found that mRNA level of myogenin decrease after treatment NButGT. And we found that the promoter activity of myogenin decreases after NButGT using reporter gene assay. For finding the promoter region affected O-GlcNAc , we did reporter gene assay using shorter length promoter and found at least 169 base pair upstream region of myogenin is affected by O-GlcNAc. And using this region, we found that Mef2c protein can be important transcription factor regulated by O-GlcNAc using avidin-biotin complex DNA binding assay. We confirm that Mef2c is O-GlcNAcylated using immunoprecipitation and we found several O-GlcNAcylated sites on Mef2c using mass spectrometry. Based on the result, we made the Mef2c point mutants converted from Serine, Threonine of O-GlcNAcylated sites to Alanine. Additionally, we found O-GlcNAc modification could regulate DNA binding affinity and transcriptional complex formation.

저자

  • Hanbyeol Kim [ Department of Integrated OMICS for Biomedical Sciences, Graduate School, Yonsei University ]
  • HoJung Seo [ Department of Integrated OMICS for Biomedical Sciences, Graduate School, Yonsei University ]
  • SangYoon Park [ Department of Integrated OMICS for Biomedical Sciences, Graduate School, Yonsei University ]
  • Jin Won Cho [ Department of Integrated OMICS for Biomedical Sciences, Graduate School, Yonsei University, Department of Biology, Yonsei University, Seoul 120-749, Korea ]

참고문헌

자료제공 : 네이버학술정보

간행물 정보

발행기관

  • 발행기관명
    한국당과학회 [Korean Society for Glycoscience]
  • 설립연도
    2006
  • 분야
    의약학>약학
  • 소개
    본 학회는 화학, 생화학, 분자생물학, 미생물학, 식품공학, 의학, 약학, 유전공학 및 생물공학, 환경 및 기타 공업 등 전 분야의 탄수화물관련 이론과 기술을 연구 발전시키고 산학협동을 통해 이를 보급하여 국내 관련 산업의 발전 및 국민생활의 과학화에 기여하고자 하며, 이러한 목표와 비젼의 실현을 위해 회원들이 적극적인 참여와 활동을 전개하고자 한다.

간행물

  • 간행물명
    한국당과학회 학술대회
  • 간기
    연간
  • 수록기간
    2006~2022
  • 십진분류
    KDC 517 DDC 614

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