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Translation of the Alzheimer Amyloid Precursor Protein mRNA Is Up-regulated by Interleukin-1 through 5′-Untranslated Region Sequences
Open accessAbstract
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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“Because inflammatory proteins (e.g., interleukin-1β, tumor necrosis factor–α, and interferon-γ) can alter APP expression, APP processing, or Aβ transport (47–50), the inflammatory changes caused by the deletion of Abi3 locus may have contributed to the increase in APP protein level and subsequently Aβ accumulation.”
From Deletion of Abi3 gene locus exacerbates neuropathological features of Alzheimer’s disease in a mouse model of Aβ amyloidosis (2021) · cites this paper as [49]
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Cites
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
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
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
Amyloid β Protein Gene: cDNA, mRNA Distribution, and Genetic Linkage Near the Alzheimer Locus
Tanzi, R. E., Gusella, J. F., Watkins, P. C., Bruns, G. A. P., St George-Hyslop, P., Van Keuren, M. L., Patterson, D., Pagan, S., Kurnit, D. M., & Neve, R. L. (1987) · Science · doi:10.1126/science.2949367 · Cited by 1,611
Occurrence of neuropathological changes and dementia of Alzheimer’s disease in Down’s syndrome
Wisniewski, K. E., Wisniewski, H. M., & Wen, G. Y. (1985) · Annals of Neurology · doi:10.1002/ana.410170310 · Cited by 1,159
Abraham, C. R., Selkoe, D. J., & Potter, H. (1988) · Cell · doi:10.1016/0092-8674(88)90462-x · Cited by 900
Self-citationGingras, A., Kennedy, S. G., O'Leary, M., Sonenberg, N., & Hay, N. (1998) · Genes & Development · doi:10.1101/gad.12.4.502 · Cited by 885
Ma, J., Yee, A., Brewer, H. B., Das, S., & Potter, H. (1994) · Nature · doi:10.1038/372092a0 · Cited by 871
Self-citationInterleukin-1 Stimulation of Astroglial Proliferation After Brain Injury
Giulian, D., & Lachman, L. B. (1985) · Science · doi:10.1126/science.3872478 · Cited by 847
Lack of apolipoprotein E dramatically reduces amyloid β-peptide deposition
Bales, K. R., Verina, T., Dodel, R. C., Du, Y., Altstiel, L., Bender, M., Hyslop, P., Johnstone, E. M., Little, S. P., Cummins, D. J., et al. (1997) · Nature Genetics · doi:10.1038/ng1197-263 · Cited by 830
Complement activation by beta-amyloid in Alzheimer disease.
Rogers, J., Cooper, N. R., Webster, S., Schultz, J., McGeer, P. L., Styren, S. D., Civin, W. H., Brachova, L., Bradt, B., & Ward, P. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.21.10016 · Cited by 817
Self-citationScavenger receptor-mediated adhesion of microglia to β-amyloid fibrils
Khoury, J. E., Hickman, S. E., Thomas, C. A., Cao, L., Silverstein, S. C., & Loike, J. D. (1996) · Nature · doi:10.1038/382716a0 · Cited by 727
β-Amyloid-mediated vasoactivity and vascular endothelial damage
Thomas, T., Thomas, G., McLendon, C., Sutton, T., & Mullan, M. (1996) · Nature · doi:10.1038/380168a0 · Cited by 703
The 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. T. (1996) · Science · doi:10.1126/science.271.5254.1406 · Cited by 680
Interleukin 1 regulates synthesis of amyloid beta-protein precursor mRNA in human endothelial cells.
Goldgaber, D., Harris, H. W., Hla, T., Maciag, T., DONNELLY, R. J., Jacobsen, J. S., Vitek, M. P., & Gajdusek, D. C. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.19.7606 · Cited by 597
Selkoe, D. J., Podlisny, M. B., Joachim, C. L., Vickers, E., Lee, G. S., Fritz, L. C., & Oltersdorf, T. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.19.7341 · Cited by 579
Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells.
Busciglio, J., Gabuzda, D. H., Matsudaira, P., & Yankner, B. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.2092 · Cited by 569
Buxbaum, J. D., Oishi, M., Chen, H. I., Pinkas‐Kramarski, R., JAFFE, E. A., Gandy, S., & Greengard, P. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.21.10075 · Cited by 563
Enhanced expression of a glyceraldehyde-3-phosphate dehydrogenase gene in human lung cancers.
Tokunaga, K., Nakamura, Y., Sakata, K., Fujimori, K., Ohkubo, M., Sawada, K., & Sakiyama, S. (1987) · PubMed · Cited by 537
(1997) · doi:10.1073/pnas.94.4.1550 · Cited by 535
Ameboid microglia as effectors of inflammation in the central nervous system
Giulian, D. (1987) · Journal of Neuroscience Research · doi:10.1002/jnr.490180123 · Cited by 482
Nonsteroidal anti-inflammatory drugs in Alzheimer's disease
Rich, J. B., Rasmusson, D. X., Folstein, M. F., Carson, K. A., Kawas, C., & Brandt, J. (1995) · Neurology · doi:10.1212/wnl.45.1.51 · Cited by 446
Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro.
(1994) · PubMed Central · Cited by 441
βA4 amyloid protein deposition in brain after head trauma
Roberts, G., Gentleman, S., Lynch, A., & Graham, D. I. (1991) · The Lancet · doi:10.1016/0140-6736(91)92724-g · Cited by 440
Formation of β-amyloid protein deposits in brains of transgenic mice
Quon, D. H., Wang, Y., Catalano, R., Scardina, J. M., Murakami, K., & Cordell, B. (1991) · Nature · doi:10.1038/352239a0 · Cited by 405
Sanan, D. A., Weisgraber, K. H., Russell, S. J., Mahley, R. W., Huang, D., Saunders, A., Schmechel, D., Wisniewski, T., Frangione, B., & Roses, A. D. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117407 · Cited by 404
Expression of β-amyloid precursor protein in reactive astrocytes following neuronal damage
Siman, R. G., Card, J. P., Nelson, R. B., & Davis, L. G. (1989) · Neuron · doi:10.1016/0896-6273(89)90252-3 · Cited by 344
Evans, K. C., Berger, E. P., Cho, C. G., Weisgraber, K. H., & Lansbury, P. T. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.3.763 · Cited by 333
Rouault, T. A., Stout, C. D., Kaptain, S., Harford, J. B., & Klausner, R. D. (1991) · Cell · doi:10.1016/0092-8674(91)90312-m · Cited by 296
Do nonsteroidal anti-inflammatory drugs decrease the risk for Alzheimer's disease?
Andersen, K., Launer, L. J., Ott, A., Hoes, A. W., Breteler, M. M. B., & Albert Hofman, D. (1995) · Neurology · doi:10.1212/wnl.45.8.1441 · Cited by 284
Sheng, J. G., Ito, K., Skinner, R. D., Mrak, R. E., Rovnaghi, C. R., van Eldik, L. J., & Griffin, W. S. T. (1996) · Neurobiology of Aging · doi:10.1016/0197-4580(96)00104-2 · Cited by 269
Rogers, J. T., Bridges, K. R., Durmowicz, G. P., Glass, J., Auron, P. E., & Munro, H. N. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77341-9 · Cited by 260
Self-citationForloni, G., Demicheli, F., Giorgi, S., Bendotti, C., & Angeretti, N. (1992) · Molecular Brain Research · doi:10.1016/0169-328x(92)90202-m · Cited by 257
Ferritin Synthesis in Inflammation: I. PATHOGENESIS OF IMPAIRED IRON RELEASE
Konijn, A. M., & Hershko, C. (1977) · British Journal of Haematology · doi:10.1111/j.1365-2141.1977.tb08806.x · Cited by 247
Chandra, T., Stackhouse, R., Kidd, V. J., Robson, K., & Woo, S. L. C. (1983) · Biochemistry · doi:10.1021/bi00291a001 · Cited by 198
Cohen, M. L., Golde, T. E., Usiak, M., Younkin, L. H., & Younkin, S. G. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.4.1227 · Cited by 186
Interleukin‐1‐like activity in rat brain: Sources, targets, and effects of injury
Nieto‐Sampedro, M., & Berman, M. A. (1987) · Journal of Neuroscience Research · doi:10.1002/jnr.490170303 · Cited by 177
Das, S., & Potter, H. (1995) · Neuron · doi:10.1016/0896-6273(95)90300-3 · Cited by 167
Self-citationPantopoulos, K., Mueller, S., Atzberger, A., Ansorge, W. J., Stremmel, W., & Hentze, M. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.15.9802 · Cited by 163
Leedman, P. J., Stein, A. R., Chin, W. W., & Rogers, J. T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.20.12017 · Cited by 154
Self-citationRogers, J. (1996) · Blood · doi:10.1182/blood.v87.6.2525.bloodjournal8762525 · Cited by 154
Self-citationPhosphorylation and Activation of both Iron Regulatory Proteins 1 and 2 in HL-60 Cells
Schalinske, K. L., & Eisenstein, R. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.12.7168 · Cited by 125
Gray, C. W., & Patel, A. J. (1993) · Molecular Brain Research · doi:10.1016/0169-328x(93)90037-p · Cited by 117
Zaidi, S. H. E., & Malter, J. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.29.17292 · Cited by 110
Moir, R. D., Lynch, T., Bush, A. I., Whyte, S., Henry, A., Portbury, S. D., Multhaup, G., Small, D. H., Tanzi, R. E., Beyreuther, K. T., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.5013 · Cited by 103
Interleukin-1: a gene expression system regulated at multiple levels.
Auron, P. E., & Webb, A. C. (1995) · PubMed · Cited by 94
Iron Levels Modulate α‐Secretase Cleavage of Amyloid Precursor Protein
Bodovitz, S., Falduto, M. T., Frail, D. E., & Klein, W. L. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64010307.x · Cited by 86
Blom, M. A. A., van Twillert, M. G. H., de Vries, S. C., Engels, F., Finch, C. E., Veerhuis, R., & Eikelenboom, P. (1997) · Brain Research · doi:10.1016/s0006-8993(97)01204-3 · Cited by 79
LeBlanc, A. C., Chen, H. Y., AUTILIO‐GAMBETTI, L., & Gambetti, P. L. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80861-v · Cited by 76
Dysregulation of gene expression in mouse trisomy 16, an animal model of Down syndrome.
Holtzman, D. M., Bayney, R. M., Li, Y. W., Khosrovi, H., Berger, C. N., Epstein, C. J., & Mobley, W. C. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05094.x · Cited by 68
Alternative polyadenylation of the amyloid protein precursor mRNA regulates translation.
de Sauvage, F. J., Kruys, V., Marinx, O., Huez, G. A., & Octave, J. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05382.x · Cited by 57
Rogers, J. T., Andriotakis, J., Lacroix, L., Durmowicz, G. P., Kasschau, K., & Bridges, K. R. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.13.2678 · Cited by 55
Self-citationThe predominant form of the amyloid beta-protein precursor in human brain is protease nexin 2.
Nostrand, W. E. V., Farrow, J. S., Wagner, S. L., Bhasin, R., Goldgaber, D., Cotman, C. W., & Cunningham, D. D. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.22.10302 · Cited by 52
A specific structural interaction of Alzheimer's peptide Aβ1–42 with α1-antichymotrypsin
Janciauskiene, S. M., Eriksson, S., & Wright, H. T. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0896-668 · Cited by 51
HB-GAM is a cytokine present in Alzheimerʼs and Downʼs syndrome lesions
Wısnıewskı, T., Lalowski, M. M., Baumann, M., Rauvala, H., Raulo, E., Nolo, R. M., & Frangione, B. (1996) · Neuroreport · doi:10.1097/00001756-199601310-00068 · Cited by 43
Quantification of APP and APLP2 mRNA in APOE genotyped Alzheimer's disease brains
Johnston, J. A., Norgren, S., Ravid, R., Wasco, W., Winblad, B. G., Lannfelt, L., & Cowburn, R. F. (1996) · Molecular Brain Research · doi:10.1016/s0169-328x(96)00161-1 · Cited by 28
Machein, U., Lieb, K., Hüll, M., & Fiebich, B. L. (1995) · Neuroreport · doi:10.1097/00001756-199511270-00004 · Cited by 27
Neve, R. L., Valletta, J. S., Li, Y., Ventosa-Michelman, M., Holtzman, D. M., & Mobley, W. C. (1996) · Molecular Brain Research · doi:10.1016/0169-328x(96)00007-1 · Cited by 19
A new quantitative solution hybridisation-RNase protection assay for APP and APLP2 mRNA
Johnston, J. A., Norgren, S., Annerén, G., Cowburn, R. F., & Lannfelt, L. (1996) · Molecular Brain Research · doi:10.1016/s0169-328x(96)00160-x · Cited by 13
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
Cited by
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Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514
Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530
“The APP transgene includes the 5 untranslated region, which contains a putative interleukin-1 (IL-1 ) translational enhancer element (Rogers et al., 1999).”
BackgroundLee, J. W., Lee, Y. K., Yuk, D. Y., Choi, D. Y., Ban, S. B., Oh, K. W., & Hong, J. T. (2008) · Journal of Neuroinflammation · doi:10.1186/1742-2094-5-37 · Cited by 772
History and progress of hypotheses and clinical trials for Alzheimer’s disease
Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723
Chin-Chan, M., Navarro-Yepes, J., & Quintanilla‐Vega, B. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00124 · Cited by 746
Metadata
- 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.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-03
- Volume
- 274
- Issue
- 10
- Pages
- 6421-6431
- ISSN
- 0021-9258 (ISSN-L)
- 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
- 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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