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Processing of Glycosyltransferases by Alzheimer’s β-secretase (BACE1)

  • Shinobu Kitazume
  • Shou Takashima
  • Yasuhiro Hashimoto

Abstract

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).

Keywords

Golgi Apparatus Heparan Sulfate BACE1 Substrate Control pcDNA Vector Oligosaccharide Biosynthesis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Kitazume S, Tachida Y, Oka R, Shirotani K, Saido TC, Hashimoto Y (2001) Alzheimer’s β-secretase, β-site amyliod precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase. Proc Natl Acad Sci USA 98:13554–13559PubMedCrossRefGoogle Scholar
  2. Kitazume S, Nakagawa K, Oka R, Tachida Y, Ogawa K, Luo Y, Citron M, Shitara H, Taya C, Yonekawa H, Pulson JC, Miyoshi E, Taniguchi N, Hashimoto Y (2005) In vivo cleavage of α2,6-sialyltransferase by Alzheimer’s β-secretase. J Biol Chem 280:8589–8595PubMedCrossRefGoogle Scholar
  3. Kitazume S, Tachida Y, Oka R, Nakagawa K, Takashima S, Lee YC, Hashimoto Y (2006) Screening a series of sialyltransferases for possible BACE1 substrates Glycoconjugate J 23:437–441CrossRefGoogle Scholar
  4. Nagai N, Habuchi H, Kitazume S, Toyoda H, Hashimoto Y, Kimata K (2007) Regulation of heparan sulfate 6-O-sulfation by β-secretase activity. J Biol Chem M610691200; 282:14942–14951PubMedCrossRefGoogle Scholar

Copyright information

© Springer 2008

Authors and Affiliations

  • Shinobu Kitazume
    • 1
    • 2
  • Shou Takashima
    • 1
    • 2
  • Yasuhiro Hashimoto
    • 1
    • 2
    • 3
  1. 1.Glyco-chain Functions Laboratory, Supra-biomolecular System GroupFrontier Research System, RIKENWako, SaitamaJapan
  2. 2.CRESTKawaguchi, SaitamaJapan
  3. 3.Department of Biochemistry, School of MedicineFukushima Medical UniversityFukushimaJapan

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