The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid beta-protein precursor
Open accessAbstract
Alzheimer's disease (AD) is a progressive neurodegenerative disorder characterized by the extracellular deposition of amyloid beta-protein (A beta), a molecule produced by post-translational processing of the beta-amyloid precursor protein (beta APP). Mutations within the gene encoding beta APP have been linked to early onset forms of AD, but the pathogenetic mechanism(s) producing the phenotype are unknown. We analyzed the effects on beta APP processing in vitro of a naturally occurring Ala-->Gly mutation at position 692 of beta APP770 (A692G) (Hendriks, L., Duijin, C., Cras, P., Cruts, M., van Hul, W., van Harskamp, F., Warren, A., McInnis, M., Antonarakis, S., Martin, J.-J., Hofman, A., and van Broeckhoven, C. (1992) Nature Genet. 1, 218-221), as well as the effects of five genetically engineered mutations at or near this site. Substitution of glycine or proline for Ala692, or for Phe690, produced relative increases in secretion of A beta and relative decreases in secretion of the p3 peptide(s) arising after alpha-secretase generation of soluble APP (APPs). The Phe690-->Pro substitution also resulted in the synthesis of truncated APPs molecules. The structurally conservative substitutions Ala692-->Val and Phe690-->Tyr did not exhibit these effects. Certain of the substitutions also resulted in the production of a minor peptides, previously undescribed in vitro, beginning at Ala2, Lys16, and Phe19 of A beta. These data show that beta APP mutations carboxyl-terminal to alpha-secretase and beta-secretase cleavage sites can exert strong control over beta APP processing. Increased secretion of A beta may accelerate amyloidogenesis by providing more precursors for aggregation. It is also possible that truncated A beta peptides resulting from several of these mutations may accelerate amyloidogenesis through self-aggregation and/or seeding the fibrillogenesis of longer, more abundant A beta species.
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Amyloid β-peptide is produced by cultured cells during normal metabolism
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Self-citationIsolation and quantification of soluble Alzheimer's β-peptide from biological fluids
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Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
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Release of Excess Amyloid β Protein from a Mutant Amyloid β Protein Precursor
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Cells with a familial Alzheimerʼs disease mutation produce authentic β-peptide
Dovey, H. F., Suomensaari-Chrysler, S., Lieberburg, I., Sinha, S., & Keim, P. S. (1993) · NeuroReport · doi:10.1097/00001756-199308000-00011 · Cited by 71
Cited by
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
Self-citationJankowsky, J. L., Fadale, D. J., Anderson, J., Xu, G. M., Gonzales, V., Jenkins, N. A., Copeland, N. G., Lee, M. K., Younkin, L. H., Wagner, S. L., et al. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh019 · Cited by 1,575
Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201750200 · Cited by 1,452
Alzheimer’s Disease: The Challenge of the Second Century
Holtzman, D. M., Morris, J. C., & Goate, A. M. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002369 · Cited by 1,424
Citron, M., Westaway, D., Xia, W., Carlson, G., Diehl, T., Levesque, G., Johnson-wood, K., Lee, M., Seubert, P., Davis, A., et al. (1997) · Nature Medicine · doi:10.1038/nm0197-67 · Cited by 1,271
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Metadata
- Authors
- Haass, C., Hung, A. Y., Selkoe, D. J., & Teplow, D. B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1994-07
- Volume
- 269
- Issue
- 26
- Pages
- 17741-17748
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1539232350
- Cited by
- 317
- References
- 9
- FWCI
- 16.01
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Haass, C., Hung, A. Y., Selkoe, D. J., & Teplow, D. B. (1994). Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid beta-protein precursor. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)32503-6
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