2007年11月
beta-galactoside alpha 2,6-sialyltransferase I cleavage by BACE1 enhances the sialylation of soluble glycoproteins - A novel regulatory mechanism for alpha 2,6-sialylation
JOURNAL OF BIOLOGICAL CHEMISTRY
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- 巻
- 282
- 号
- 48
- 開始ページ
- 34896
- 終了ページ
- 34903
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1074/jbc.M704766200
- 出版者・発行元
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
BACE1((beta) under bar -site (a) under bar myloid precursor protein-(c) under bar leaving (e) under bar nzyme-(1) under bar) is a membrane-bound aspartic protease that cleaves amyloid precursor protein to produce a neurotoxic peptide, amyloid beta-peptide, and has been implicated in triggering the pathogenesis of Alzheimer disease. We showed previously that BACE1 cleaves beta-galactoside alpha 2,6-sialyltransferase I (ST6Gal I) to initiate its secretion, but it remained unclear how BACE1 affects the cellular level of alpha 2,6-sialylation. Here, we found that BACE1 overexpression in Hep3B cells increased the sialylation of soluble secreted glycoproteins, but did not affect cell-surface sialylation. The sialylation of soluble glycoproteins was not increased by ST6Gal I overexpression alone, but was increased by co-overexpression of ST6Gal I and BACE1 or by expression of the soluble form of ST6Gal I, suggesting that soluble ST6Gal I produced by BACE1 plays, at least in part, a role in the sialylation of soluble glycoproteins. We also found that plasma glycoproteins from BACE1-deficient mice exhibited reduced levels of alpha 2,6-sialylation compared with those from wild-type mice. We propose a novel regulatory mechanism in which cleavage and secretion of ST6Gal I enhance the sialylation of soluble glycoprotein substrates.
- リンク情報
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- DOI
- https://doi.org/10.1074/jbc.M704766200
- CiNii Articles
- http://ci.nii.ac.jp/naid/80018066572
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/17897958
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000251155200032&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1074/jbc.M704766200
- ISSN : 0021-9258
- eISSN : 1083-351X
- CiNii Articles ID : 80018066572
- PubMed ID : 17897958
- Web of Science ID : WOS:000251155200032