rdf:type |
|
lifeskim:mentions |
umls-concept:C0001721,
umls-concept:C0026882,
umls-concept:C0036537,
umls-concept:C0205177,
umls-concept:C0962722,
umls-concept:C1514559,
umls-concept:C1710263,
umls-concept:C1723136,
umls-concept:C1869507,
umls-concept:C2354310,
umls-concept:C2936239
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pubmed:issue |
3
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pubmed:dateCreated |
2000-10-19
|
pubmed:abstractText |
Presenilins 1 and 2 are two homologous proteins which, when mutated, appear responsible for most of the early-onset familial forms of Alzheimer's disease. Among various functional aspects, presenilins appear to behave as chaperoning partners of a series of proteins including the beta-amyloid precursor protein. Recently, presenilins were shown to interact with Rab11, a GTPase involved in intracellular transport. This suggested that Rab11-presenilin interaction could influence the routing of betaAPP and thereby modulate its maturation. In this context, we examined whether overexpression of Rab11 or its constitutively active mutant Rab11Q70L could affect betaAPP maturation in human HEK293 cells. We show here that the overexpression of both Rab11-related proteins does not modify the recovery of secreted sAPPalpha or Abeta in HEK293 cells expressing wild-type betaAPP or betaAPP harboring the Swedish double mutation. These data indicate that Rab11 does not influence betaAPP processing in HEK293 cells. However, it does not preclude the possibility for Rab11 to modulate other presenilin-mediated functions in human cells.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Protein Precursor,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PSEN1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PSEN2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Presenilin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Presenilin-2,
http://linkedlifedata.com/resource/pubmed/chemical/rab GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rab11 protein
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
|
pubmed:issn |
0006-291X
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pubmed:author |
|
pubmed:copyrightInfo |
Copyright 2000 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
910-5
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:10973821-Alzheimer Disease,
pubmed-meshheading:10973821-Amino Acid Substitution,
pubmed-meshheading:10973821-Amyloid beta-Peptides,
pubmed-meshheading:10973821-Amyloid beta-Protein Precursor,
pubmed-meshheading:10973821-Cell Line,
pubmed-meshheading:10973821-Gene Expression,
pubmed-meshheading:10973821-Humans,
pubmed-meshheading:10973821-Membrane Proteins,
pubmed-meshheading:10973821-Mutation,
pubmed-meshheading:10973821-Presenilin-1,
pubmed-meshheading:10973821-Presenilin-2,
pubmed-meshheading:10973821-Protein Binding,
pubmed-meshheading:10973821-Protein Processing, Post-Translational,
pubmed-meshheading:10973821-Transfection,
pubmed-meshheading:10973821-rab GTP-Binding Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
Overexpression of Rab11 or constitutively active Rab11 does not affect sAPPalpha and Abeta secretions by wild-type and Swedish mutated betaAPP-expressing HEK293 cells.
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pubmed:affiliation |
IPMC du CNRS, UPR411, 660 Route des Lucioles, Valbonne, 06560, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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