Cited by 290Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsRNA and protein synthesis mechanisms

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Translation of the Alzheimer Amyloid Precursor Protein mRNA Is Up-regulated by Interleukin-1 through 5′-Untranslated Region Sequences

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Rogers, Jack T., Leiter, Lorene M., McPhee, Jay, Cahill, Catherine M., Zhan, Shan-Shan, Potter, Huntington, Nilsson, Lars N.G.·1999·Journal of Biological Chemistry

DOI 10.1074/jbc.274.10.6421

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Abstract

The amyloid precursor protein (APP) has been associated with Alzheimer's disease (AD) because APP is processed into the beta-peptide that accumulates in amyloid plaques, and APP gene mutations can cause early onset AD. Inflammation is also associated with AD as exemplified by increased expression of interleukin-1 (IL-1) in microglia in affected areas of the AD brain. Here we demonstrate that IL-1alpha and IL-1beta increase APP synthesis by up to 6-fold in primary human astrocytes and by 15-fold in human astrocytoma cells without changing the steady-state levels of APP mRNA. A 90-nucleotide sequence in the APP gene 5'-untranslated region (5'-UTR) conferred translational regulation by IL-1alpha and IL-1beta to a chloramphenicol acetyltransferase (CAT) reporter gene. Steady-state levels of transfected APP(5'-UTR)/CAT mRNAs were unchanged, whereas both base-line and IL-1-dependent CAT protein synthesis were increased. This APP mRNA translational enhancer maps from +55 to +144 nucleotides from the 5'-cap site and is homologous to related translational control elements in the 5'-UTR of the light and and heavy ferritin genes. Enhanced translation of APP mRNA provides a mechanism by which IL-1 influences the pathogenesis of AD.

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Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Biologic basis for interleukin-1 in disease.
Dinarello, C. (1996) · Blood · doi:10.1182/blood.v87.6.2095.bloodjournal8762095 · Cited by 4,344
Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599
Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516
RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
Yan, S. D., Chen, X., Fu, J., Chen, M., Zhu, H., Roher, A., Slattery, T., Zhao, L., Nagashima, M., Morser, J., et al. (1996) · Nature · doi:10.1038/382685a0 · Cited by 2,012
On Finding All Suboptimal Foldings of an RNA Molecule
Zuker, M. (1989) · Science · doi:10.1126/science.2468181 · Cited by 1,998
Amyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921
Brain interleukin 1 and S-100 immunoreactivity are elevated in Down syndrome and Alzheimer disease.
Griffin, W. S., Stanley, L. C., Ling, C., White, L., MacLeod, V, Perrot, L. J., White, C. L., & Araoz, C. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.19.7611 · Cited by 1,777
Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production
Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J. (1992) · Nature · doi:10.1038/360672a0 · Cited by 1,757

Flagged first, then by citations

Show all 66 references

Research works printed but not linked: 5

Wisniewski, 1994, Am. J. Pathol., 145, 1030
Frautschy, 1998, Am. J. Pathol., 152, 3007
Auron, 1994, Eur. Cytokine Netw., 5, 573
Tokunaga, 1987, Cancer Res., 47, 5616
Nilsson, 1998, Front. Biosci., 16, 436

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Authors: Rogers, J. T., Leiter, L. M., McPhee, J., Cahill, C. M., Zhan, S.-S., Potter, H., & Nilsson, L. N. G.
Affiliations: Brigham and Women's Hospital (US)
Massachusetts General Hospital (US)
University of South Florida (US)
Corresponding author: Rogers, Jack T.
ORCID: Rogers, Jack T.
Cahill, Catherine M.
Potter, Huntington
Nilsson, Lars N.G.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1999-03
Volume: 274
Issue: 10
Pages: 6421-6431
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.274.10.6421
OpenAlex: W2149650428
Cited by: 290
References: 66
Citations by year: 2026: 8 · 2025: 5 · 2024: 7 · 2023: 9 · 2022: 2 · 2021: 10 · 2020: 9 · 2019: 10 · 2018: 9 · 2017: 7 · 2016: 10 · 2015: 5 · 2014: 9 · 2013: 7 · 2012: 13
FWCI: 10.62
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7888 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: U.S. Public Health Service (6872302)
National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR29I32717)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords: amyloid precursor protein, Alzheimer's disease, interleukin-1, translational regulation, 5' untranslated region, translational enhancer, astrocytes, astrocytoma cells, IL-1α, IL-1β, inflammation, ferritin gene, mRNA translation
MeSH terms: Alzheimer Disease, Astrocytes, Base Sequence, Cells, Cultured, Humans, Interleukin-1, Molecular Sequence Data, RNA, Messenger, Transfection, Protein Biosynthesis, Up-Regulation, Amyloid beta-Protein Precursor

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Translation of the Alzheimer Amyloid Precursor Protein mRNA Is Up-regulated by Interleukin-1 through 5′-Untranslated Region Sequences

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