Response to: Pardossi-Piquard et al., "Presenilin-Dependent Transcriptional Control of the A[beta]-Degrading Enzyme Neprilysin by Intracellular Domains of [beta]APP and APLP." Neuron 46, 541-554

Consistent with the above results in the PS-deficient BD8 cells, neprilysin levels were unchanged upon transfection with C60, Fe65, and Tip60 in both PBD8 (Figure 3B) and 293T cells (Figure 3C).\n Neprilysin levels in wt mouse embryonic stem cells, fibroblasts, and HEK293T cells were unchanged by...

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Bibliographic Details
Published in:Neuron (Cambridge, Mass.) Mass.), 2007-02, Vol.53 (4), p.479
Main Authors: Chen, Allen C, Selkoe, Dennis J
Format: Article
Language:English
Subjects:
Evacuations & rescues
Kinases
Proteins
Rodents
Stem cells
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Summary:Consistent with the above results in the PS-deficient BD8 cells, neprilysin levels were unchanged upon transfection with C60, Fe65, and Tip60 in both PBD8 (Figure 3B) and 293T cells (Figure 3C).\n Neprilysin levels in wt mouse embryonic stem cells, fibroblasts, and HEK293T cells were unchanged by a γ-secretase inhibitor. [...]transfection of wt mouse embryonic stem cells or 293T cells with AICD alone; Fe65 plus Tip60 alone; or AICD, Fe65, and Tip 60 together produced no change in cellular neprilysin levels. [...]most mammals (e.g., mice and rats) show no detectable accumulation of Aβ throughout life, making it unlikely that there would have been evolutionary pressure for a specific mechanism to upregulate the neprilysin cleavage of Aβ. These various concerns about biological plausibility, together with the lack of experimental support from our study, make this mechanism untenable at present.
ISSN:0896-6273
1097-4199
DOI:10.1016/j.neuron.2007.01.023