Processing of Glycosyltransferases by Alzheimer’s β-secretase (BACE1)
Majority of glycosyltransferases for oligosaccharide biosynthesis are retained in endoplasmic reticulum or the Golgi apparatus. Some of the glycosyltransferases are subsequently cleaved by proteases, and then secreted out of the cell. Indeed, many glycosyltransferases exist as soluble forms in bodily fluids. We previously reported that Alzheimer’s β-secretase (BACE1) is involved in the cleavage and secretion of ST6Gal I, representing the first identification of a protease that plays a role in the secretion of glycosyltransferases (Kitazume et al. 2001). With the expectation that other sialyltransferases and glycosyltransferases might also be BACE1 substrates, we started on screening a series of sialyltransferases for possible BACE1 substrates. BACE1 was overexpressed in cultured cells and its effect on secretion of sialyltransferases was examined (Kitazume et al. 2006).
KeywordsGolgi Apparatus Heparan Sulfate BACE1 Substrate Control pcDNA Vector Oligosaccharide Biosynthesis
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