earticle

영어

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