Abnormal cleavage of APP impairs its functions in cell adhesion and migration
Abstract
Amyloid precursor protein (APP) is expressed ubiquitously but its wrong cleavage only occurs in central nervous system. In this research, overexpression of wild type human APP695 was found to stimulate the adhesion and migration of N2a cells. In the cells co-transfected by familial Alzheimer's disease (FAD)-linked Swedish mutant of APP695 gene plus big up tri, openE9 deleted presenilin1 gene (N2a/Swe. big up tri, open9), however, this stimulating function was impaired compared to that in the cells co-transfected by Swedish mutant of APP695 gene plus dominant negative mutant of presenilin1 D385A gene (N2a/Swe.385). Furthermore, it was also found that the phosphorylation of FAK Tyr-861 and GSK-3beta Ser-9 was reduced in N2a/Swe.Delta9 cells, which can be possibly taken as a reasonable explanation for the underlying mechanism. Our results suggest that impaired cell adhesion and migration induced by abnormal cleavage of APP could contribute to the pathological effects in FAD brain.
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Modified APP cleavage/degradation may modulate the membranous pool of APP or its metabolic products and impair APP function in cell adhesion and synaptic plasticity.
“In this context, modified APP cleavage/degradation may modulate the membranous pool of APP or its metabolic products (e.g., AICD, APPs-α) and impair APP function in cell adhesion and synaptic plasticity [117].”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [117]
Cites
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Dourlen, P., Kilinc, D., Malmanche, N., Chapuis, J., & Lambert, J.-C. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02004-0 · Cited by 168 · see citing works
Amyloid-β precursor protein promotes cell proliferation and motility of advanced breast cancer
Lim, S., Yoo, B. K., Kim, H.-S., Gilmore, H. L., Lee, Y., Lee, H.-P., Kim, S.-J., Letterio, J., & Lee, H.-G. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-928 · Cited by 100 · see citing works
ADGC, A. D. N. I., Chapuis, J., Flaig, A., Grenier-Boley, B., Eysert, F., Pottiez, V., Deloison, G., Vandeputte, A., Ayral, A.-M., Mendes, T., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-016-1652-z · Cited by 75 · see citing works
- Authors
- Sheng, B., Song, B., Zheng, Z., Zhou, F., Lu, G., Zhao, N., Zhang, X., & Gong, Y.
- Affiliations
- Tsinghua University (CN)
- Corresponding author
- Gong, Yandao
- Venue
- Neuroscience Letters
- Publisher
- Elsevier BV
- Published
- 2009-02
- Volume
- 450
- Issue
- 3
- Pages
- 327-331
- ISSN
- 0304-3940 (ISSN-L)
- OpenAlex
- W2091045813
- Cited by
- 20
- References
- 1
- Citations by year
- 2024: 1 · 2019: 3 · 2018: 2 · 2017: 1 · 2016: 2 · 2014: 6 · 2013: 1 · 2012: 2
- FWCI
- 0.43
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuroscience Letters (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid precursor protein, APP cleavage, familial Alzheimer's disease, presenilin 1, cell adhesion, cell migration, focal adhesion kinase phosphorylation, GSK3β phosphorylation, N2a cells, Alzheimer's disease pathogenesis
- MeSH terms
- Glycogen Synthase Kinase 3 beta, Alzheimer Disease, Animals, Brain, Cell Adhesion, Cell Movement, Humans, Mutation, Nerve Regeneration, Neuronal Plasticity, Neurons, Phosphorylation, Transfection, Amyloid beta-Protein Precursor, Glycogen Synthase Kinase 3, Cell Line, Tumor, Mice, Focal Adhesion Kinase 1, Presenilin-1
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