pubmed-article:12857759 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12857759 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
pubmed-article:12857759 | lifeskim:mentions | umls-concept:C0002716 | lld:lifeskim |
pubmed-article:12857759 | lifeskim:mentions | umls-concept:C1412727 | lld:lifeskim |
pubmed-article:12857759 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:12857759 | lifeskim:mentions | umls-concept:C1709634 | lld:lifeskim |
pubmed-article:12857759 | pubmed:issue | 38 | lld:pubmed |
pubmed-article:12857759 | pubmed:dateCreated | 2003-9-15 | lld:pubmed |
pubmed-article:12857759 | pubmed:abstractText | Generation of the amyloid peptide through proteolytic processing of the amyloid precursor protein by beta- and gamma-secretases is central to the etiology of Alzheimer's disease. beta-secretase, known more widely as the beta-site amyloid precursor protein cleaving enzyme 1 (BACE1), has been identified as a transmembrane aspartic proteinase, and its ectodomain has been reported to be cleaved and secreted from cells in a soluble form. The extracellular domains of many diverse proteins are known to be cleaved and secreted from cells by a process known as ectodomain shedding. Here we confirm that the ectodomain of BACE1 is secreted from cells and that this processing is up-regulated by agents that activate protein kinase C. A metalloproteinase is involved in the cleavage of BACE1 as hydroxamic acid-based metalloproteinase inhibitors abolish the release of shed BACE1. Using potent and selective inhibitors, we demonstrate that ADAM10 is a strong candidate for the BACE1 sheddase. In addition, we show that the BACE1 sheddase is distinct from alpha-secretase and, importantly, that inhibition of BACE1 shedding does not influence amyloid precursor protein processing at the beta-site. | lld:pubmed |
pubmed-article:12857759 | pubmed:language | eng | lld:pubmed |
pubmed-article:12857759 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12857759 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12857759 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12857759 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12857759 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12857759 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12857759 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12857759 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12857759 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12857759 | pubmed:month | Sep | lld:pubmed |
pubmed-article:12857759 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:12857759 | pubmed:author | pubmed-author:DingwallColin... | lld:pubmed |
pubmed-article:12857759 | pubmed:author | pubmed-author:FallerAndrewA | lld:pubmed |
pubmed-article:12857759 | pubmed:author | pubmed-author:RiddellDavid... | lld:pubmed |
pubmed-article:12857759 | pubmed:author | pubmed-author:HussainIshrut... | lld:pubmed |
pubmed-article:12857759 | pubmed:author | pubmed-author:HawkinsJulieJ | lld:pubmed |
pubmed-article:12857759 | pubmed:author | pubmed-author:ShikotraAarti... | lld:pubmed |
pubmed-article:12857759 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12857759 | pubmed:day | 19 | lld:pubmed |
pubmed-article:12857759 | pubmed:volume | 278 | lld:pubmed |
pubmed-article:12857759 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12857759 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12857759 | pubmed:pagination | 36264-8 | lld:pubmed |
pubmed-article:12857759 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:12857759 | pubmed:meshHeading | pubmed-meshheading:12857759... | lld:pubmed |
pubmed-article:12857759 | pubmed:meshHeading | pubmed-meshheading:12857759... | lld:pubmed |
pubmed-article:12857759 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12857759 | pubmed:articleTitle | Characterization of the ectodomain shedding of the beta-site amyloid precursor protein-cleaving enzyme 1 (BACE1). | lld:pubmed |
pubmed-article:12857759 | pubmed:affiliation | Neurology and Gastrointestinal Centre of Excellence for Drug Discovery, GlaxoSmithKline Research & Development Limited, New Frontiers Science Park, Third Avenue, Harlow, Essex, CM19 5AW, United Kingdom. Ishrut_2_Hussain@gsk.com | lld:pubmed |
pubmed-article:12857759 | pubmed:publicationType | Journal Article | lld:pubmed |
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