Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:16164418rdf:typepubmed:Citationlld:pubmed
pubmed-article:16164418lifeskim:mentionsumls-concept:C0002395lld:lifeskim
pubmed-article:16164418lifeskim:mentionsumls-concept:C0376604lld:lifeskim
pubmed-article:16164418lifeskim:mentionsumls-concept:C0699919lld:lifeskim
pubmed-article:16164418lifeskim:mentionsumls-concept:C0521390lld:lifeskim
pubmed-article:16164418lifeskim:mentionsumls-concept:C0886515lld:lifeskim
pubmed-article:16164418lifeskim:mentionsumls-concept:C0021467lld:lifeskim
pubmed-article:16164418lifeskim:mentionsumls-concept:C1454853lld:lifeskim
pubmed-article:16164418lifeskim:mentionsumls-concept:C0392756lld:lifeskim
pubmed-article:16164418lifeskim:mentionsumls-concept:C0021469lld:lifeskim
pubmed-article:16164418lifeskim:mentionsumls-concept:C0033268lld:lifeskim
pubmed-article:16164418lifeskim:mentionsumls-concept:C0851285lld:lifeskim
pubmed-article:16164418lifeskim:mentionsumls-concept:C0332120lld:lifeskim
pubmed-article:16164418lifeskim:mentionsumls-concept:C2353566lld:lifeskim
pubmed-article:16164418pubmed:issue9lld:pubmed
pubmed-article:16164418pubmed:dateCreated2005-9-16lld:pubmed
pubmed-article:16164418pubmed:abstractTextThe regulated secretory pathway of neurons is the major source of extracellular A beta that accumulates in Alzheimer's disease (AD). Extracellular A beta secreted from that pathway is generated by beta-secretase processing of amyloid precursor protein (APP). Previously, cysteine protease activity was demonstrated as the major beta-secretase activity in regulated secretory vesicles of neuronal chromaffin cells. In this study, the representative cysteine protease activity in these secretory vesicles was purified and identified as cathepsin B by peptide sequencing. Immunoelectron microscopy demonstrated colocalization of cathepsin B with A beta in these vesicles. The selective cathepsin B inhibitor, CA074, blocked the conversion of endogenous APP to A beta in isolated regulated secretory vesicles. In chromaffin cells, CA074Me (a cell permeable form of CA074) reduced by about 50% the extracellular A beta released by the regulated secretory pathway, but CA074Me had no effect on A beta released by the constitutive pathway. Furthermore, CA074Me inhibited processing of APP into the COOH-terminal beta-secretase-like cleavage product. These results provide evidence for cathepsin B as a candidate beta-secretase in regulated secretory vesicles of neuronal chromaffin cells. These findings implicate cathepsin B as beta-secretase in the regulated secretory pathway of brain neurons, suggesting that inhibitors of cathepsin B may be considered as therapeutic agents to reduce A beta in AD.lld:pubmed
pubmed-article:16164418pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16164418pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16164418pubmed:languageenglld:pubmed
pubmed-article:16164418pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16164418pubmed:citationSubsetIMlld:pubmed
pubmed-article:16164418pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16164418pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16164418pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16164418pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16164418pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16164418pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16164418pubmed:statusMEDLINElld:pubmed
pubmed-article:16164418pubmed:monthSeplld:pubmed
pubmed-article:16164418pubmed:issn1431-6730lld:pubmed
pubmed-article:16164418pubmed:authorpubmed-author:BogyoMatthewMlld:pubmed
pubmed-article:16164418pubmed:authorpubmed-author:Medzihradszky...lld:pubmed
pubmed-article:16164418pubmed:authorpubmed-author:ToneffThomasTlld:pubmed
pubmed-article:16164418pubmed:authorpubmed-author:ReisineTerryTlld:pubmed
pubmed-article:16164418pubmed:authorpubmed-author:HookVivianVlld:pubmed
pubmed-article:16164418pubmed:authorpubmed-author:GreenbaumDoro...lld:pubmed
pubmed-article:16164418pubmed:authorpubmed-author:LaneWilliamWlld:pubmed
pubmed-article:16164418pubmed:authorpubmed-author:NeveuJohnJlld:pubmed
pubmed-article:16164418pubmed:authorpubmed-author:HookGregoryGlld:pubmed
pubmed-article:16164418pubmed:issnTypePrintlld:pubmed
pubmed-article:16164418pubmed:volume386lld:pubmed
pubmed-article:16164418pubmed:ownerNLMlld:pubmed
pubmed-article:16164418pubmed:authorsCompleteYlld:pubmed
pubmed-article:16164418pubmed:pagination931-40lld:pubmed
pubmed-article:16164418pubmed:dateRevised2010-11-18lld:pubmed
pubmed-article:16164418pubmed:meshHeadingpubmed-meshheading:16164418...lld:pubmed
pubmed-article:16164418pubmed:meshHeadingpubmed-meshheading:16164418...lld:pubmed
pubmed-article:16164418pubmed:meshHeadingpubmed-meshheading:16164418...lld:pubmed
pubmed-article:16164418pubmed:meshHeadingpubmed-meshheading:16164418...lld:pubmed
pubmed-article:16164418pubmed:meshHeadingpubmed-meshheading:16164418...lld:pubmed
pubmed-article:16164418pubmed:meshHeadingpubmed-meshheading:16164418...lld:pubmed
pubmed-article:16164418pubmed:meshHeadingpubmed-meshheading:16164418...lld:pubmed
pubmed-article:16164418pubmed:meshHeadingpubmed-meshheading:16164418...lld:pubmed
pubmed-article:16164418pubmed:meshHeadingpubmed-meshheading:16164418...lld:pubmed
pubmed-article:16164418pubmed:meshHeadingpubmed-meshheading:16164418...lld:pubmed
pubmed-article:16164418pubmed:meshHeadingpubmed-meshheading:16164418...lld:pubmed
pubmed-article:16164418pubmed:meshHeadingpubmed-meshheading:16164418...lld:pubmed
pubmed-article:16164418pubmed:meshHeadingpubmed-meshheading:16164418...lld:pubmed
pubmed-article:16164418pubmed:meshHeadingpubmed-meshheading:16164418...lld:pubmed
pubmed-article:16164418pubmed:year2005lld:pubmed
pubmed-article:16164418pubmed:articleTitleInhibition of cathepsin B reduces beta-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate beta-secretase of Alzheimer's disease.lld:pubmed
pubmed-article:16164418pubmed:affiliationDepartment of Pharmacology, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego, La Jolla, CA 92093, USA. vhook@ucsd.edulld:pubmed
pubmed-article:16164418pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:16164418pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:16164418pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:16164418lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:16164418lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:16164418lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:16164418lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:16164418lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:16164418lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:16164418lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:16164418lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:16164418lld:pubmed