Source:http://linkedlifedata.com/resource/pubmed/id/16375654
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2005-12-26
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pubmed:abstractText |
Programmed cell death (PCD) also called apoptosis, is a normal and genetically controlled event that could play, when mis-regulated, a pivotal role in the development of several neurodegenerative disorders such as Parkinson's disease. Sporadic Alzheimer's disease is one of the most prominent age-related syndromes whose etiology, although still unknown, could be related to biochemical or environmental causes. A few cases of Alzheimer's disease are likely of genetic origin and linked to mutations on the genes coding for the amyloid precursor protein (betaAPP) and presenilins 1 and 2. Although still discussed, the hypothesis of an implication of apoptotic cell death in Alzheimer's disease neuropathology has been recently supported by a growing body of biochemical evidences. Thus, the implication of presenilins in apoptotic processes in vitro has been well documented but the mechanisms underlying this function are still a matter of intense research. The aim of this review is to focus on the mechanisms by which presenilin 2 affects the programmed cell death with special emphasis on the role of the proteolytically derived presenilin fragments generated by both presenilinase- and caspases. The distinct apoptotic phenotypes elicited by the two parent proteins presenilins 1 and 2 and their functional cross talk will be briefly discussed.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PSEN2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Presenilin-2,
http://linkedlifedata.com/resource/pubmed/chemical/presenilinase, human
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1567-2050
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
507-14
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16375654-Alzheimer Disease,
pubmed-meshheading:16375654-Apoptosis,
pubmed-meshheading:16375654-Aspartic Acid Endopeptidases,
pubmed-meshheading:16375654-Caspases,
pubmed-meshheading:16375654-Humans,
pubmed-meshheading:16375654-Membrane Proteins,
pubmed-meshheading:16375654-Phenotype,
pubmed-meshheading:16375654-Presenilin-2
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pubmed:year |
2005
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pubmed:articleTitle |
Recent insights on the pro-apoptotic phenotype elicited by presenilin 2 and its caspase and presenilinase-derived fragments.
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pubmed:affiliation |
Institut de Pharmacologie Moléculaire et Cellulaire of Centre Nationale de la Recherche Scientifique, UMR6097 CNRS/UNSA, Sophia Antipolis, France. acosta@ipmc.cnrs.fr
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pubmed:publicationType |
Journal Article,
Review
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