Sialylation of the brain cortex and hippocampus tissues and their total proteins from normal mouse (SamR1) and Alzheimer model mouse (SamP8) were comparatively analyzed by a combination of SDS-PAGE, Emerald Pro-Q dye staining, lectin histochemistry and lectin blotting. Lectin histochemistry using TRITC-labeled SNA-I, specific for α-2,6-linked sialic acid, and FITC-labeled MAA, specific for α-2,3-linked sialic acid, showed that both α2,3-and α2,6-linked sialic acid residues are usually expressed with no significant variations in cortex and hippocampus tissues of normal and Alzheimer model mouse brain. SDS-PAGE and Emerald Pro-Q dye staining of the total proteins from each tissue also showed that glycosylation of the most major proteins of both mouse brain tissues are not significantly changed. However, lectin blotting of total proteins showed significant variation in sialylation of most major glycoproteins; especially, significant decreased expression of α 2,3-linked sialic acid residues in proteins with 110, 90, 68, 49, 43 and 36 kDa of both tissues of Alzheimer mouse brain was observed. The specific roles of these glycoproteins showing significant degree of alterations in sialylation in AD mouse remain to be elucidated
저자
Yoon Hee Lee [ Department of Biotechnology and Biomaterial Engineering Center, The Catholic University of Korea ]
Sung Min Kim [ Department of Biotechnology and Biomaterial Engineering Center, The Catholic University of Korea ]
Yong-Il Park [ Department of Biotechnology and Biomaterial Engineering Center, The Catholic University of Korea ]
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.