| pubmed-article:7970175 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7970175 | lifeskim:mentions | umls-concept:C1710263 | lld:lifeskim |
| pubmed-article:7970175 | lifeskim:mentions | umls-concept:C0007635 | lld:lifeskim |
| pubmed-article:7970175 | lifeskim:mentions | umls-concept:C0031437 | lld:lifeskim |
| pubmed-article:7970175 | lifeskim:mentions | umls-concept:C0276496 | lld:lifeskim |
| pubmed-article:7970175 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:7970175 | lifeskim:mentions | umls-concept:C0031584 | lld:lifeskim |
| pubmed-article:7970175 | lifeskim:mentions | umls-concept:C0332293 | lld:lifeskim |
| pubmed-article:7970175 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:7970175 | pubmed:dateCreated | 1994-12-29 | lld:pubmed |
| pubmed-article:7970175 | pubmed:abstractText | Protein phosphorylation mediated by phorbol ester stimulates secretion of the beta-amyloid precursor protein (beta-APP) in the cell culture. This increase in secretion is produced by a transient increase in cleavage to produce non-amyloidogenic protease nexin II products mediated by the alpha-secretase activity, and a concomitant decrease in beta-protein production. Cells expressing the Swedish familial Alzheimer's disease (FAD) variant of beta-APP produce more beta-protein and potentially amyloidogenic fragments than cells expressing wild-type protein; furthermore, cleavage shifts from the alpha- to the beta-secretase cleavage site of the precursor. We show that treatment with phorbol 12,13-dibutyrate (PDBu) of cells expressing the Swedish FAD reverses the mutant phenotype to wild-type. The alpha-secretase cleavage increases with a concomitant loss of beta-protein and other beta-secretase cleaved products. These results show that modulating beta-secretase cleavage directly affects beta-protein production. It suggests that activating protein kinase C through, for example, muscarinic receptor agonists could reduce amyloidosis by modulating the level of beta-protein produced. | lld:pubmed |
| pubmed-article:7970175 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7970175 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7970175 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7970175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7970175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7970175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7970175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7970175 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7970175 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:7970175 | pubmed:issn | 0304-3940 | lld:pubmed |
| pubmed-article:7970175 | pubmed:author | pubmed-author:RobertsS BSB | lld:pubmed |
| pubmed-article:7970175 | pubmed:author | pubmed-author:WarshawskyLL | lld:pubmed |
| pubmed-article:7970175 | pubmed:author | pubmed-author:HunihanL WLW | lld:pubmed |
| pubmed-article:7970175 | pubmed:author | pubmed-author:IngallsK MKM | lld:pubmed |
| pubmed-article:7970175 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7970175 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:7970175 | pubmed:volume | 174 | lld:pubmed |
| pubmed-article:7970175 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7970175 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7970175 | pubmed:pagination | 173-6 | lld:pubmed |
| pubmed-article:7970175 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:7970175 | pubmed:meshHeading | pubmed-meshheading:7970175-... | lld:pubmed |
| pubmed-article:7970175 | pubmed:meshHeading | pubmed-meshheading:7970175-... | lld:pubmed |
| pubmed-article:7970175 | pubmed:meshHeading | pubmed-meshheading:7970175-... | lld:pubmed |
| pubmed-article:7970175 | pubmed:meshHeading | pubmed-meshheading:7970175-... | lld:pubmed |
| pubmed-article:7970175 | pubmed:meshHeading | pubmed-meshheading:7970175-... | lld:pubmed |
| pubmed-article:7970175 | pubmed:meshHeading | pubmed-meshheading:7970175-... | lld:pubmed |
| pubmed-article:7970175 | pubmed:meshHeading | pubmed-meshheading:7970175-... | lld:pubmed |
| pubmed-article:7970175 | pubmed:meshHeading | pubmed-meshheading:7970175-... | lld:pubmed |
| pubmed-article:7970175 | pubmed:meshHeading | pubmed-meshheading:7970175-... | lld:pubmed |
| pubmed-article:7970175 | pubmed:meshHeading | pubmed-meshheading:7970175-... | lld:pubmed |
| pubmed-article:7970175 | pubmed:meshHeading | pubmed-meshheading:7970175-... | lld:pubmed |
| pubmed-article:7970175 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7970175 | pubmed:articleTitle | Reversal of the Swedish familial Alzheimer's disease mutant phenotype in cultured cells treated with phorbol 12,13-dibutyrate. | lld:pubmed |
| pubmed-article:7970175 | pubmed:affiliation | CNS - Department of Biophysics and Molecular Biology, Bristol-Myers Squibb Pharmaceutical Research Institute, Wallingford, CT 06492. | lld:pubmed |
| pubmed-article:7970175 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7970175 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7970175 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7970175 | lld:pubmed |
