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Overexpression of Rab11 or Constitutively Active Rab11 Does Not Affect sAPPα and Aβ Secretions by Wild-Type and Swedish Mutated βAPP-Expressing HEK293 Cells
- Source :
- Biochemical and Biophysical Research Communications. 275:910-915
- Publication Year :
- 2000
- Publisher :
- Elsevier BV, 2000.
-
Abstract
- 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.
- Subjects :
- Mutant
Biophysics
Gene Expression
Context (language use)
Plasma protein binding
Biology
Transfection
Biochemistry
Presenilin
Cell Line
Amyloid beta-Protein Precursor
Alzheimer Disease
Presenilin-2
mental disorders
Presenilin-1
Humans
Molecular Biology
Amyloid beta-Peptides
HEK 293 cells
Wild type
Membrane Proteins
Cell Biology
Cell biology
Amino Acid Substitution
rab GTP-Binding Proteins
Cell culture
Mutation
Protein Processing, Post-Translational
Protein Binding
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 275
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....c9f664f92e3c4740411d53843af54ac7