The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Presenilin clinical mutations can affect γ‐secretase activity by different mechanisms
Open accessAbstract
Mutations in human presenilin (PS) genes cause aggressive forms of familial Alzheimer's disease. Presenilins are polytopic proteins that harbour the catalytic site of the γ‐secretase complex and cleave many type I transmembrane proteins including β‐amyloid precursor protein (APP), Notch and syndecan 3. Contradictory results have been published concerning whether PS mutations cause ‘abnormal’ gain or (partial) loss of function of γ‐secretase. To avoid the possibility that wild‐type PS confounds the interpretation of the results, we used presenilin‐deficient cells to analyse the effects of different clinical mutations on APP, Notch, syndecan 3 and N‐cadherin substrate processing, and on γ‐secretase complex formation. A loss in APP and Notch substrate processing at ɛ and S3 cleavage sites was observed with all presenilin mutants, whereas APP processing at the γ site was affected in variable ways. PS1‐Δ9 and PS1‐L166P mutations caused a reduction in β‐amyloid peptide (Aβ)40 production whereas PS1‐G384A mutant significantly increased Aβ 42. Interestingly PS2, a close homologue of PS1, appeared to be a less efficient producer of Aβ than PS1. Finally, subtle differences in γ‐secretase complex assembly were observed. Overall, our results indicate that the different mutations in PS affect γ‐secretase structure or function in multiple ways.
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Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
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Aph-1, Pen-2, and Nicastrin with Presenilin Generate an Active γ-Secretase Complex
De Strooper, B. (2003) · Neuron · doi:10.1016/s0896-6273(03)00205-8 · Cited by 965
Qi-Takahara, Y., Morishima-Kawashima, M., Tanimura, Y., Dolios, G., Hirotani, N., Horikoshi, Y., Kametani, F., Maeda, M., Saido, T. C., Wang, R., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1575-04.2005 · Cited by 391
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Karran, E., Mercken, M., & Strooper, B. D. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3505 · Cited by 2,188
Self-citationThe Amyloid-β Pathway in Alzheimer’s Disease
Hampel, H., Hardy, J., Blennow, K., Chen, C., Perry, G., Kim, S. H., Villemagne, V. L., Aisen, P., Vendruscolo, M., Iwatsubo, T., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01249-0 · Cited by 1,952
Aβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938
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Metadata
- Authors
- Bentahir, M., Nyabi, O., Verhamme, J., Tolia, A., Horré, K., Wiltfang, J., Esselmann, H., & De Strooper, B.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2006-01-09
- Volume
- 96
- Issue
- 3
- Pages
- 732-742
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2048111211
- Cited by
- 415
- References
- 7
- FWCI
- 22.74
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Bentahir, M., Nyabi, O., Verhamme, J., Tolia, A., Horré, K., Wiltfang, J., Esselmann, H., & De Strooper, B. (2006). Presenilin clinical mutations can affect γ‐secretase activity by different mechanisms. Journal of Neurochemistry. https://doi.org/10.1111/j.1471-4159.2005.03578.x
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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