| pubmed-article:16412100 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16412100 | lifeskim:mentions | umls-concept:C0036536 | lld:lifeskim |
| pubmed-article:16412100 | lifeskim:mentions | umls-concept:C0036537 | lld:lifeskim |
| pubmed-article:16412100 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:16412100 | lifeskim:mentions | umls-concept:C0872366 | lld:lifeskim |
| pubmed-article:16412100 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:16412100 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:16412100 | pubmed:dateCreated | 2006-1-31 | lld:pubmed |
| pubmed-article:16412100 | pubmed:abstractText | Alzheimer's disease (AD) is characterized by amyloid-beta peptide (Abeta) deposition in the brain. Abeta is produced by sequential cleavage of amyloid precursor protein (APP) by beta-secretase (BACE1: beta-site APP-cleaving enzyme 1) and gamma-secretase. Previously, we demonstrated that BACE1 also cleaves beta-galactoside alpha2,6-sialyltransferase (ST6Gal-I) and down-regulates its transferase activity. Here, we report that overexpression of ST6Gal-I in Neuro2a cells enhanced alpha2,6-sialylation of endogenous APP and increased the extracellular levels of its metabolites [Abeta by two-fold, soluble APPbeta (sAPPbeta) by three-fold and sAPPalpha by 2.5-fold). Sialylation-deficient mutant (Lec-2) cells secreted half as much Abeta as wild-type Chinese hamster ovary (CHO) cells. Furthermore, wild-type CHO cells showed enhanced secretion of the APP metabolites upon ST6Gal-I overexpression, whereas Lec-2 cells did not, indicating that the secretion enhancement requires sialylation of cellular protein(s). Secretion of metabolites from a mutant APP (APP-Asn467,496Ala) that lacked N-glycosylation sites was not enhanced upon ST6Gal-I overexpression, suggesting that the N-glycans on APP itself are required for the enhanced secretion. In the mouse brain, the amount of alpha2,6-sialylated APP appeared to be correlated with the sAPPbeta level. These results suggest that sialylation of APP promotes its metabolic turnover and could affect the pathology of AD. | lld:pubmed |
| pubmed-article:16412100 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16412100 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412100 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16412100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16412100 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16412100 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:16412100 | pubmed:issn | 0022-3042 | lld:pubmed |
| pubmed-article:16412100 | pubmed:author | pubmed-author:HashimotoYasu... | lld:pubmed |
| pubmed-article:16412100 | pubmed:author | pubmed-author:EndoTamaoT | lld:pubmed |
| pubmed-article:16412100 | pubmed:author | pubmed-author:MaruyamaKeiK | lld:pubmed |
| pubmed-article:16412100 | pubmed:author | pubmed-author:SaidoTakaomi... | lld:pubmed |
| pubmed-article:16412100 | pubmed:author | pubmed-author:SatoYujiY | lld:pubmed |
| pubmed-article:16412100 | pubmed:author | pubmed-author:KitazumeShino... | lld:pubmed |
| pubmed-article:16412100 | pubmed:author | pubmed-author:OkaRitsukoR | lld:pubmed |
| pubmed-article:16412100 | pubmed:author | pubmed-author:NakagawaKazuh... | lld:pubmed |
| pubmed-article:16412100 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16412100 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:16412100 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16412100 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16412100 | pubmed:pagination | 924-33 | lld:pubmed |
| pubmed-article:16412100 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:16412100 | pubmed:meshHeading | pubmed-meshheading:16412100... | lld:pubmed |
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| pubmed-article:16412100 | pubmed:meshHeading | pubmed-meshheading:16412100... | lld:pubmed |
| pubmed-article:16412100 | pubmed:meshHeading | pubmed-meshheading:16412100... | lld:pubmed |
| pubmed-article:16412100 | pubmed:meshHeading | pubmed-meshheading:16412100... | lld:pubmed |
| pubmed-article:16412100 | pubmed:meshHeading | pubmed-meshheading:16412100... | lld:pubmed |
| pubmed-article:16412100 | pubmed:meshHeading | pubmed-meshheading:16412100... | lld:pubmed |
| pubmed-article:16412100 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16412100 | pubmed:articleTitle | Sialylation enhances the secretion of neurotoxic amyloid-beta peptides. | lld:pubmed |
| pubmed-article:16412100 | pubmed:affiliation | Glycochain Functions Laboratory, Suprabiomolecular System Group, Frontier Research System, RIKEN, Wako-shi, Saitama, Japan. | lld:pubmed |
| pubmed-article:16412100 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16412100 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16412100 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16412100 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16412100 | lld:pubmed |
