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Decrease in α 2,3- and α2,6-Sialylation in Rat Brain Cortex Tissue during Early Post-natal Development Correlates with Increased Sialidase Activity

첫 페이지 보기
  • 발행기관
    한국당과학회 바로가기
  • 간행물
    한국당과학회 학술대회 바로가기
  • 통권
    2008 Eastern Asian Glycoscience Symposium (2008.11)바로가기
  • 페이지
    pp.83-84
  • 저자
    Lee, Yoon-Hee, Sung-Min Kim, Su-Il Do, Young-Kug Choo, Yong-Il Park
  • 언어
    영어(ENG)
  • URL
    https://www.earticle.net/Article/A192368

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원문정보

초록

영어
In this study, alterations in glycan chains, especially in sialylation, of the glycoproteins in brain cortex tissues during early post-natal development of E18 and post-natal rats (1-day, 4-week and 8-week-old) were investigated. The lectin histochemistry using sialic acid specific lectins, SNA and MAA, lectin blotting of total proteins, and total N-glycan structure analysis showed that both α2,3- and α2,6-linked sialic acid residues of the several proteins on the surface of cortex tissues are significantly expressed in cortex tissues of 1-day-old rats and that, as the rats grow up to young adult (8-week-old), their expression is markedly down-regulated. The activity of sialidase, which catalyzes the cleavage of terminal sialic acids of glycan chain of glycoproteins, significantly increased as rats grow up. Interestingly, however, western blotting analysis of sialidase and α2,3- and α2,6-sialyltransferase showed that there was no significant difference in sialidase protein level in between E18 and 8-week-old young adult rat brains, whereas the protein levels of α2,3- and α2,6-sialyltransferases gradually decreased. These results strongly suggest that the decreased level of α2,3- and α2,6- sialylation on N-glycans would correlate with the up-regulation of enzyme activity, not the protein level of the sialidase, and also with the down-regulation of both α2,3- and α2,6-sialyltranferase protein level. The results suggest that the observation on the developmental stage-dependent decrease in α2,3 and α2,6 sialylation on glycoproteins could be attributed to a certain post-translational regulation of sialo-enzymes. Elucidating the mechanism and function of these regulation events would be very important for better understanding the normal development of brain tissues and also to effectively treat neurodegenerative diseases. Furthermore, the specific roles of those glycoproteins, observed in this study, which showed significant degree of age-dependent alterations in glycosylation and sialylation remain to be elucidated and these sialoglycoproteins may provide new, even specific, regulatory molecules in the early post-natal development of rat brain nervous system.

저자

  • Lee, Yoon-Hee [ Department of Biotechnology and The Biomaterial Engineering Research Center, The Catholic University of Korea ]
  • Sung-Min Kim [ Department of Biotechnology and The Biomaterial Engineering Research Center, The Catholic University of Korea ]
  • Su-Il Do [ Department of Biological Science, Ajou University ]
  • Young-Kug Choo [ Department of Biological Science, Wonkwang University ]
  • Yong-Il Park [ Department of Biotechnology and The Biomaterial Engineering Research Center, The Catholic University of 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

이 권호 내 다른 논문 / 한국당과학회 학술대회 2008 Eastern Asian Glycoscience Symposium

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