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A novel zinc(II) binding site modulates the function of the beta A4 amyloid protein precursor of Alzheimer's disease
Open accessAbstract
Abnormalities of zinc metabolism occur in Alzheimer's disease (AD), a condition where pathological catabolism of the amyloid protein precursor (APP) causes cerebral beta A4 amyloidosis. An association between zinc and APP metabolism was sought by studying the binding of 65Zn2+ to APP. 65Zn2+ bound in a rapid, saturable, and specific manner (KD = 764 nM). A novel zinc binding motif, strongly conserved between members of the APP family, was located between the cysteine-rich and negatively charged domains of the protein. Zinc increased binding of APP to heparin and has been shown to potentiate the inhibition of coagulation factor XIa by an APP isoform containing a Kunitz-type inhibitory domain (Komiyama, Y., Murakami, T., Egawa, H., Okubo, S., Yasunaga, K., and Murata, K. (1992) Thromb. Res. 66, 397-408) situated near the zinc binding region. Zinc is a factor that modulates the functional properties of the substrate for beta A4 amyloidogenesis.
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Citations
Cited by
Copper, iron and zinc in Alzheimer's disease senile plaques
Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120
The metallobiology of Alzheimer's disease
Bush, A. I. (2003) · Trends in Neurosciences · doi:10.1016/s0166-2236(03)00067-5 · Cited by 1,315
Self-citationMolecular pathways to neurodegeneration
Bossy-Wetzel, E., Schwarzenbacher, R., & Lipton, S. A. (2004) · Nature Medicine · doi:10.1038/nm1067 · Cited by 740
Bush, A. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)00073-3 · Cited by 731
Self-citationThe Amyloid Precursor Protein of Alzheimer's Disease in the Reduction of Copper(II) to Copper(I)
Multhaup, G., Schlicksupp, A., Hesse, L., Beher, D., Ruppert, T., Masters, C. L., & Beyreuther, K. (1996) · Science · doi:10.1126/science.271.5254.1406 · Cited by 678
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Metadata
- Authors
- Bush, A. I., Multhaup, G., Moir, R. D., Williamson, T. G., Small, D. H., Rumble, B., Pollwein, P., Beyreuther, K., & Masters, C. L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-08
- Volume
- 268
- Issue
- 22
- Pages
- 16109-16112
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1600007560
- Cited by
- 286
- References
- 0
- FWCI
- 5.62
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: A novel zinc(II) binding site modulates the function of the beta A4 amyloid protein precursor of Alzheimer's disease. https://app.cochat.ai/papers/10.1016/s0021-9258(19)85394-2
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- Bush, A. I., Multhaup, G., Moir, R. D., Williamson, T. G., Small, D. H., Rumble, B., Pollwein, P., Beyreuther, K., & Masters, C. L. (1993). A novel zinc(II) binding site modulates the function of the beta A4 amyloid protein precursor of Alzheimer's disease. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)85394-2
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
