| pubmed-article:1608449 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1608449 | lifeskim:mentions | umls-concept:C0024369 | lld:lifeskim |
| pubmed-article:1608449 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1608449 | lifeskim:mentions | umls-concept:C0486805 | lld:lifeskim |
| pubmed-article:1608449 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
| pubmed-article:1608449 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:1608449 | lifeskim:mentions | umls-concept:C1523987 | lld:lifeskim |
| pubmed-article:1608449 | lifeskim:mentions | umls-concept:C1709634 | lld:lifeskim |
| pubmed-article:1608449 | lifeskim:mentions | umls-concept:C2353566 | lld:lifeskim |
| pubmed-article:1608449 | pubmed:issue | 6378 | lld:pubmed |
| pubmed-article:1608449 | pubmed:dateCreated | 1992-7-21 | lld:pubmed |
| pubmed-article:1608449 | pubmed:abstractText | Progressive cerebral deposition of the amyloid beta-peptide is an early and invariant feature of Alzheimer's disease. The beta-peptide is released by proteolytic cleavages from the beta-amyloid precursor protein (beta APP), a membrane-spanning glycoprotein expressed in most mammalian cells. Normal secretion of beta APP involves a cleavage in the beta-peptide region, releasing the soluble extramembranous portion and retaining a 10K C-terminal fragment in the membrane. Because this secretory pathway precludes beta-amyloid formation, we searched for an alternative proteolytic processing pathway that can generate beta-peptide-bearing fragments from full-length beta APP. Incubation of living human endothelial cells with a beta APP antibody revealed reinternalization of mature beta APP from the cell surface and its targeting to endosomes/lysosomes. After cell-surface biotinylation, full-length biotinylated beta APP was recovered inside the cells. Purification of lysosomes directly demonstrated the presence of mature beta APP and an extensive array of beta-peptide-containing proteolytic products. Our results define a second processing pathway for beta APP and suggest that it may be responsible for generating amyloid-bearing fragments in Alzheimer's disease. | lld:pubmed |
| pubmed-article:1608449 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1608449 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1608449 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1608449 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1608449 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1608449 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1608449 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1608449 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1608449 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1608449 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:1608449 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:1608449 | pubmed:author | pubmed-author:SelkoeD JDJ | lld:pubmed |
| pubmed-article:1608449 | pubmed:author | pubmed-author:MellonAA | lld:pubmed |
| pubmed-article:1608449 | pubmed:author | pubmed-author:KooE HEH | lld:pubmed |
| pubmed-article:1608449 | pubmed:author | pubmed-author:HaassCC | lld:pubmed |
| pubmed-article:1608449 | pubmed:author | pubmed-author:HuntA NAN | lld:pubmed |
| pubmed-article:1608449 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1608449 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:1608449 | pubmed:volume | 357 | lld:pubmed |
| pubmed-article:1608449 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1608449 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1608449 | pubmed:pagination | 500-3 | lld:pubmed |
| pubmed-article:1608449 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:1608449 | pubmed:meshHeading | pubmed-meshheading:1608449-... | lld:pubmed |
| pubmed-article:1608449 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1608449 | pubmed:articleTitle | Targeting of cell-surface beta-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. | lld:pubmed |
| pubmed-article:1608449 | pubmed:affiliation | Department of Neurology, Harvard Medical School, Brigham and Women's Hospital, Boston, Massachusetts 02115. | lld:pubmed |
| pubmed-article:1608449 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1608449 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1608449 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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