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Rodent Aβ Modulates the Solubility and Distribution of Amyloid Deposits in Transgenic Mice
Open accessAbstract
The amino acid sequence of amyloid precursor protein (APP) is highly conserved, and age-related A beta aggregates have been described in a variety of vertebrate animals, with the notable exception of mice and rats. Three amino acid substitutions distinguish mouse and human A beta that might contribute to their differing properties in vivo. To examine the amyloidogenic potential of mouse A beta, we studied several lines of transgenic mice overexpressing wild-type mouse amyloid precursor protein (moAPP) either alone or in conjunction with mutant PS1 (PS1dE9). Neither overexpression of moAPP alone nor co-expression with PS1dE9 caused mice to develop Alzheimer-type amyloid pathology by 24 months of age. We further tested whether mouse A beta could accelerate the deposition of human A beta by crossing the moAPP transgenic mice to a bigenic line expressing human APPswe with PS1dE9. The triple transgenic animals (moAPP x APPswe/PS1dE9) produced 20% more A beta but formed amyloid deposits no faster and to no greater extent than APPswe/PS1dE9 siblings. Instead, the additional mouse A beta increased the detergent solubility of accumulated amyloid and exacerbated amyloid deposition in the vasculature. These findings suggest that, although mouse A beta does not influence the rate of amyloid formation, the incorporation of A beta peptides with differing sequences alters the solubility and localization of the resulting aggregates.
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“For example, multiple reports indicate that there are endogenous differences in rodent and human APP (136), which could significantly alter the production on Aβ after TBI.”
From The Inflammatory Continuum of Traumatic Brain Injury and Alzheimer’s Disease (2018) · cites this paper as [136]
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Mouse models of Alzheimer's disease
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MethodInfluentialSelf-citationThe Inflammatory Continuum of Traumatic Brain Injury and Alzheimer’s Disease
Kokiko-Cochran, O. N., & Godbout, J. P. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00672 · Cited by 128
“For example, multiple reports indicate that there are endogenous differences in rodent and human APP (136), which could significantly alter the production on Aβ after TBI.”
BackgroundDarvesh, S., Cash, M. K., Reid, G. A., Martin, E. V., Mitnitski, A., & Geula, C. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31823cc7a6 · Cited by 153
“1% Triton X-100, normal goat serum (1:100), and a polyclonal rabbit antiYamyloid antibody (1:400; 71-5800, Invitrogen, Camarillo, CA), specific for the 4- to 5-kDa amyloid peptide derived by cleavage from the amyloid precursor protein (38) for approximately 16 hours at room temperature.”
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“Hemi-forebrain samples were prepared for analysis of A levels by twostep sequential extraction using 2% SDS followed by 70% formic acid (FA) as previously described (Jankowsky et al., 2007).”
MethodInfluentialSelf-citationA Novel Neurotrophic Drug for Cognitive Enhancement and Alzheimer's Disease
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Modeling human neurodegenerative diseases in transgenic systems
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Transgenic Mouse Models of Alzheimer’s Disease: An Integrative Analysis
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“It is important to note that rodent Aβ differs in three amino acids with respect to the human protein [17], making it difficult to aggregate in the form of plaques.”
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Selecting a Mouse Model of Alzheimer’s Disease
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“Seed-free Aβ (1-40) peptide was prepared in 10 mM NaOH and filtered through a 30-kDa cutoff filter.”
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Ubiquilin-1 Is a Molecular Chaperone for the Amyloid Precursor Protein
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Bundy, J. L., Vied, C., Badger, C., & Nowakowski, R. S. (2019) · Journal of Comparative Neurology · doi:10.1002/cne.24551 · Cited by 90
“This is unsurprising, as canonical human and mouse APP sequences are homologous with exception to only 17 amino acids (Jankowsky et al., 2007), and peptide assignment issues are well-documented in bottom-up LC–MS/MS for proteins with high sequence homology (Huang, Wang, Yu, & He, 2012).”
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“The APP/PS1 transgenic mouse model used in this study (APPswe/PS1dE9-Line 85) co-expresses a chimeric mouse/ human amyloid precursor protein (APP) 695 harboring the Swedish K670M/N671L mutations (Mo/HuAPPswe) and human presenilin 1 (PS1) with the exon-9 deletion mutation (PS1dE9) under control of the mouse prion prote…”
BackgroundMethodEarly Detection of Cerebral Glucose Uptake Changes in the 5XFAD Mouse
Macdonald, I. R., DeBay, D. R., Reid, G. A., O’Leary, T. P., Jollymore, C. T., Mawko, G., Burrell, S., Martin, E., Bowen, C. V., Brown, R. E., et al. (2014) · Current Alzheimer Research · doi:10.2174/1567205011666140505111354 · Cited by 79
“1% Triton X-100, normal goat serum (1:100), and a polyclonal rabbit anti-A antibody (1:400; 71-5800, Invitrogen, Camarillo, CA), specific for the 4- to 5-kDa amyloid peptide [29], for approximately 16 h at room temperature.”
BackgroundPresenilin transgenic mice as models of Alzheimer’s disease
Elder, G. A., Sosa, M. A. G., Gasperi, R. D., Dickstein, D. L., & Hof, P. R. (2009) · Brain Structure and Function · doi:10.1007/s00429-009-0227-3 · Cited by 76
“Mouse Ab differs from human Ab in its aggregation properties (Jankowsky et al. 2007), specifically in its tendency not to form fibrillar aggregates and these differences may underlie some of the apparent lack of pathology seen in PS FAD mutant transgenic mice.”
Rodgers, S. P., Born, H. A., Das, P., & Jankowsky, J. L. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-28 · Cited by 69
“Hemi-forebrain samples were prepared for analysis of Aβ levels by two-step sequential extraction using 2% SDS followed by 70% formic acid (FA) as previously described [57].”
MethodSelf-citationBeta‐amyloid protein (25–35) disrupts hippocampal network activity: Role of Fyn‐kinase
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Modulation of 5-Lipoxygenase in Proteotoxicity and Alzheimer's Disease
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Murine Aβ over-production produces diffuse and compact Alzheimer-type amyloid deposits
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“Mice expressing 5-fold excess of wild-type mouse APP also fail to produce amyloid deposits when mated to mice expressing human PS1dE9 despite raising the levels of MoAβ42 by more than 2 fold [21].”
BackgroundSelf-citationAPP Regulates Microglial Phenotype in a Mouse Model of Alzheimer's Disease
Manocha, G. D., Floden, A. M., Rausch, K., Kulas, J. A., McGregor, B. A., Rojanathammanee, L., Puig, K. L., Puig, K. L., Karki, S., Nichols, M. R., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.4654-15.2016 · Cited by 67
“Indeed, although increased rodent A production does not appear to promote plaque deposition or gliosis, it has been reported to alter human A solubility and localization in transgenic mice (Jankowsky et al., 2007).”
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“The equivalent mouse A peptides, in contrast, contain three amino acid residue substitutions that prevent the formation of plaques, possibly by altering the -secretase cleavage site (Jankowsky et al., 2007).”
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“First, endogenous murine amyloid peptides lack the aggregationprone amino acids that are present in human Ab, and their expression is lower compared with humans.(47,48) One way to reexamine the proposed hypothesis would be to evaluate whether arterial stiffness is capable of exacerbating Ab pathology in transgenic mur…”
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“Adjacent brain tissue sections from all brains (5 sections/stain/region of interest) were stained using histochemical techniques for BChE activity, thioflavin-S histofluorescence that stains fibrillar -sheets, or A immunohistochemistry using an antibody specific for 4 to 5-kDa amyloid peptide [44].”
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Alzheimers Disease: Pathological Mechanisms and Recent Insights
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“As a consequence, in many models, the A produced is present alongside a small amount of endogenous rodent A , which may have some affect on the development of pathology [77-79].”
BackgroundCholinergic Surveillance over Hippocampal RNA Metabolism and Alzheimer's-Like Pathology
Kolisnyk, B., Al‐Onaizi, M., Soreq, L., Barbash, S., Bekenstein, U., Haberman, N., Hanin, G., Kish, M. T., da Silva, J. S., Fahnestock, M. L., et al. (2016) · Cerebral Cortex · doi:10.1093/cercor/bhw177 · Cited by 56
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“Even overexpression of murine APP did not alter the extent of parenchymal A deposition in APPSwe and PS1dE9 mice (line 85), but did increase the solubility of A wt42 and led to more cerebral amyloid angiopathy.(38) Nonetheless,”
BackgroundModeling an Anti-Amyloid Combination Therapy for Alzheimer’s Disease
Chow, V. W., Savonenko, A. V., Melnikova, T., Kim, H., Price, D. L., Li, T., & Wong, P. C. (2010) · Science Translational Medicine · doi:10.1126/scitranslmed.3000337 · Cited by 53
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“In transgenic mice based on the human FAD PS mutation, Ab-dependent effects usually result from overproduction of mousesourced Ab, which has different aggregation properties than human Ab [38], specifically its tendency not to form fibrillar”
BackgroundInhibition of formyl peptide receptors improves the outcome in a mouse model of Alzheimer disease
Schröder, N., Schaffrath, A., Welter, J. A., Putzka, T., Griep, A., Ziegler, P., Brandt, E., Samer, S., Heneka, M. T., Kaddatz, H., et al. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01816-2 · Cited by 43
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“Lower A molecular weight forms were not detected using anti-A (6E10), as reported previously (41).”
BackgroundA Potent Multi-functional Neuroprotective Derivative of Tetramethylpyrazine
Chen, H.-Y., Xu, D., Tan, G.-L., Cai, W., Zhang, G.-X., Cui, W., Wang, J.-Z., Long, C., Sun, Y.-W., Yu, P., et al. (2015) · Journal of Molecular Neuroscience · doi:10.1007/s12031-015-0566-x · Cited by 39
“Previous studies have shown that there is a clear pathological change along with the deficits in Y maze test at 5–6 months in APP/PS1 transgenic mice (Jankowsky et al. 2007; Chen et al. 2011).”
BackgroundMorales‐Corraliza, J., Schmidt, S. D., Mazzella, M. J., Berger, J. D., Wilson, D. A., Wesson, D. W., Jucker, M., Levy, E., Nixon, R. A., & Mathews, P. M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.04.007 · Cited by 34
On the Role of Platelet-Generated Amyloid Beta Peptides in Certain Amyloidosis Health Complications
Inyushin, M. Y., Zayas‐Santiago, A., Rojas, L. V., & Kucheryavykh, L. Y. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.571083 · Cited by 43
Isoflurane anesthesia in aged mice and effects of A1 adenosine receptors on cognitive impairment
Zuo, C., Wang, C., Liu, J., Shen, T., Zhou, J., Hao, X., Pan, Y., Liu, H., Lian, Q., & Lin, H. (2018) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12794 · Cited by 34
An Anti-β-Amyloid Vaccine for Treating Cognitive Deficits in a Mouse Model of Down Syndrome
Belichenko, P., Madani, R., Rey-Bellet, L., Pihlgren, M., Becker, A., Plassard, A., Vuillermot, S., Giriens, V., Nosheny, R., Kleschevnikov, A., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152471 · Cited by 35
“Brain tissue was homogenized as described [38] and immunoblottings, using 4–12% Bis-Tris Plus Gels or Novex 10–20% Tricine Protein Gels, were performed under reducing conditions according to manufacturer’s instructions (Invitrogen, Illkirch, France).”
MethodD’Acunzo, P., Argyrousi, E. K., Ungania, J. M., Kim, Y., DeRosa, S., Pawlik, M., Goulbourne, C. N., Arancio, O., & Levy, E. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00721-z · Cited by 44
“…fail to produce Aβ deposits at any age unless the human App gene is exogenously overexpressed, and therefore Aβ fibrils and oligomers are absent in murine lines in which only the rodent gene is upregulated, such as DS murine models and when the App rodent gene is upregulated by 5-fold [53–55].”
BackgroundAnimal models of Alzheimer’s disease: preclinical insights and challenges
Xu, Q., Yang, W., Zhong, M., Lin, Z., Gray, N. E., & Xian, Y. (2023) · Acta Materia Medica · doi:10.15212/amm-2023-0001 · Cited by 30
“These models generally do not exhibit pronounced AD-like pathologies because the models have a lower Aβ42 level than APP transgenic mice [136, 140].”
BackgroundMüller, L., Guerra, N. P., Stenzel, J., Rühlmann, C., Lindner, T., Krause, B. J., Vollmar, B., Teipel, S. J., & Kuhla, A. (2021) · Nutrients · doi:10.3390/nu13030985 · Cited by 40
“The study was performed in female APPswe/PS1delta9 (tg) mice co-expressing human amyloid-β precursor protein (APP) K594N and M595L mutation, as well as the human presenilin (PS) 1, L166P mutation under the control of the mouse prion protein promotor [19,20].”
BackgroundJacquet, A. D. R., Denis, H. L., Cicchetti, F., & Alpaugh, M. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-00999-7 · Cited by 36
A new take on prions: preventing Alzheimer's disease
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Amyloid Beta Peptides Differentially Affect Hippocampal Theta Rhythms In Vitro
Gutiérrez-Lerma, A. I., Ordaz, B., & Peña‐Ortega, F. (2013) · International Journal of Peptides · doi:10.1155/2013/328140 · Cited by 26
Lifespan profiles of Alzheimer's disease–associated genes and their products in monkeys and mice
Dosunmu, R., Wu, J.-F., Adwan, L., Maloney, B., Basha, M., McPherson, C., Harry, G., Rice, D., Zawia, N., & Lahiri, D. (2009) · Journal of Alzheimer's Disease · doi:10.3233/jad-2009-1138 · Cited by 31
Expression of endogenous mouse APP modulates β-amyloid deposition in hAPP-transgenic mice
Steffen, J., Krohn, M., Schwitlick, C., Brüning, T., Paarmann, K., Pietrzik, C. U., Biverstål, H., Jansone, B., Langer, O., & Pahnke, J. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0448-2 · Cited by 31
“However, this is completely contradictory to in vivo results, showing that deposits of various transgenic mice are by far more unstable than those of AD patients [15, 16, 21].”
InfluentialAhmed, M. M., Wang, A. C., Elos, M. T., Chial, H. J., Sillau, S., Solano, D. A., Coughlan, C. M., Aghili, L., Anton, P. E., Markham, N. E., et al. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105694 · Cited by 31
“Similar to other mouse models of DS, including Ts65Dn, Dp16 mice do not develop AD-related neuropathology, such as amyloid plaques, despite harboring three copies of the mouse APP gene, because the mouse A peptide exhibits little propensity to aggregate into neurotoxic -sheet oligomers and fibrils (51).”
ResultNeuroprotective Effects of the FGF21 Analogue LY2405319
Rühlmann, C., Dannehl, D., Brodtrück, M., Adams, A. C., Stenzel, J., Lindner, T., Krause, B. J., Vollmar, B., & Kuhla, A. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-200837 · Cited by 24
Illouz, T., Nicola, R., Ben-Shushan, L., Madar, R., Biragyn, A., & Okun, E. (2021) · Communications Biology · doi:10.1038/s42003-021-01851-6 · Cited by 21
Huang, X., Chen, Y., Li, W., Cohen, S. N., Liao, F., Liang, L., Xu, H., & Zhang, Y. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq302 · Cited by 20
Role of presenilin1 in structural plasticity of cortical dendritic spines in vivo
Jung, C. K. E., Fuhrmann, M., Honarnejad, K., LEUVEN, F. V., & Herms, J. W. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07503.x · Cited by 21
Wesson, D. W., Morales‐Corraliza, J., Mazzella, M. J., Wilson, D. A., & Mathews, P. M. (2012) · Behavioural Brain Research · doi:10.1016/j.bbr.2012.09.019 · Cited by 18
“In transgenic mouse models of human amyloidosis, the overexpression of hAPP results in the accumulation of hAβ along with the endogenously expressed mAβ [31, 48, 49].”
Salmani, H., Hosseini, M., Baghcheghi, Y., & Noshahr, Z. S. (2020) · Pharmacological Reports · doi:10.1007/s43440-020-00141-y · Cited by 16
Novel Ab-Targeted therapeutic strategies for Alzheimer?s disease
Clionsky, M., & Clionsky, E. (2013) · doi:10.4172/2161-0460.s1.002 · Cited by 16
“The APP/PS1 transgenic mice (line 85) have been previously characterized [83].”
Emerging and potential therapies for Alzheimer's disease
Jarosz-Griffiths, H., Morten, I. J., & Hooper, N. M. (2008) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.12.6.693 · Cited by 30
“However, it must be noted that increasing levels of murine A β do not result in amyloid plaque deposition [81] .”
BackgroundN‑terminal Domain of Amyloid‑β Impacts Fibrillation and Neurotoxicity
Shi, J., Li, H., Liu, H., Zhu, L., Guo, Y.-B., Pei, J., An, H., Li, Y., Li, S.-D., Zhang, Z., et al. (2022) · ACS Omega · doi:10.1021/acsomega.2c04583 · Cited by 14
Endogenous murine Aβ increases amyloid deposition in APP23 but not in APPPS1 transgenic mice
Mahler, J., Morales‐Corraliza, J., Stolz, J., Skodras, A., Radde, R., Duma, C. C., Eisele, Y. S., Mazzella, M. J., Wong, H. K. A., Klunk, W. E., et al. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.03.011 · Cited by 15
“Nevertheless, overexpression of murine APP/Aβ was so far unable to initiate plaque deposition in mice (e.g. Jankowsky et al., 2007).”
BackgroundInfluentialSun, F.-X., Jiang, F., Zhang, N., Li, H., Tian, W., & Liu, W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.565020 · Cited by 13
“The behavioral test was performed as previously described using the Morris Water Maze (Jankowsky et al., 2007; Liu et al., 2017).”
MethodBasak, J. M., Falk, M., Mitchell, D. N., Coakley, K. A., Quillinan, N., Orfila, J. E., & Herson, P. S. (2023) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x231159597 · Cited by 15
Neuronal Cell Cycle Re-Entry Enhances Neuropathological Features in App NLF Knock-In Mice
Barrett, T., Stangis, K. A., Saito, T., Saido, T. C., & Park, K. H. J. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210091 · Cited by 12
Can Animal Models Inform on the Relationship between Depression and Alzheimer Disease?
Nyarko, J. N. K., Quartey, M. O., Baker, G. B., & Mousseau, D. D. (2018) · The Canadian Journal of Psychiatry · doi:10.1177/0706743718772514 · Cited by 12
Park, K. H. J., & Barrett, T. (2020) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-200170 · Cited by 12
[18F]-florbetaben PET/CT Imaging in the Alzheimer’s Disease Mouse Model APPswe/PS1dE9
Stenzel, J., Rühlmann, C., Lindner, T., Polei, S., Teipel, S. J., Kurth, J., Rominger, A., Krause, B. J., Vollmar, B., & Kuhla, A. (2018) · Current Alzheimer Research · doi:10.2174/1567205015666181022095904 · Cited by 11
Finnie, G. S., Gunnarsson, R. K., Manavis, J., Blumbergs, P. C., Mander, K. A., Edwards, S. R., van den Heuvel, C. J., & Finnie, J. W. (2017) · Journal of Comparative Pathology · doi:10.1016/j.jcpa.2017.03.001 · Cited by 11
Mammalian Models in Alzheimer’s Research: An Update
Sharma, H., Chang, K., Hulme, J., & An, S. S. A. (2023) · Cells · doi:10.3390/cells12202459 · Cited by 12
“This increase in the level of insoluble A β was related to the fact that humans and mice A β have three different amino acids, which result in boosted amyloidogenicity compared to human sequence [145,147].”
BackgroundThe accessible cerebral vascular proteome in a mouse model of cerebral β-amyloidosis
Roesli, C., Fugmann, T., Borgia, B., Schliemann, C., Neri, D., & Jucker, M. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.01.010 · Cited by 10
“deposition of human Aβ templates the co-aggregation and deposition of murine Aβ in particular in the vasculature [13].”
BackgroundEx vivo analysis platforms for monitoring amyloid precursor protein cleavage
Kamikubo, Y., Jin, H., Zhou, Y., Niisato, K., Hashimoto, Y., Takasugi, N., & Sakurai, T. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1068990 · Cited by 11
“Since rodent Aβ is poorly aggregated (Jankowsky et al., 2007), cultured hippocampal slices are not a good platform for analyzing Aβ aggregation and accumulation.”
BackgroundNgô, S. T., Nguyen, P. H., & Derreumaux, P. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c00030 · Cited by 7
Amyloids as Sensors and Protectors (ASAP) Hypothesis
Chapa, R. P., Emery, M. A., Fawver, J. N., & Murray, I. V. J. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-112015 · Cited by 7
Regulation of Apoptotic Pathways by MicroRNAs: A Therapeutic Strategy for Alzheimer’s Disease
Saadh, M. J., Muhammad, F. A., Alazzawi, T. S., Fahdil, A. A., Athab, Z. H., Tuxtayev, J., Alsaikhan, F., & Farhood, B. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04833-5 · Cited by 5
“Mir-132 is extensively studied for its role in the brain, as it mainly adjusts neuronal adaptability through CREB signaling pathways [225] both in vivo [226] and in vitro [227, 228].”
Distinct impact of glycation towards the aggregation and toxicity of murine and human amyloid-β.
Nam, E., Han, J., Choi, S., & Lim, M. (2021) · Chemical Communications · doi:10.1039/d1cc02695j · Cited by 4
Post, J., Schaffrath, A., Gering, I., Hartwig, S., Lehr, S., Shah, N. J., Langen, K., Willbold, D., Kutzsche, J., & Willuweit, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22137066 · Cited by 4
“SOD1G93A mice only secrete endogenous murine Aβ, which is not capable of forming aggregates [69].”
BackgroundWhite, J. D., Urbano, C. M., Taylor, J. O., Peterman, J. L., Cooksey, M., Eimerbrink, M. J., Eriksson, M. D., Cooper, B. G., Chumley, M. J., & Boehm, G. W. (2019) · Behavioural Brain Research · doi:10.1016/j.bbr.2019.112303 · Cited by 4
Mo, D., Li, X., Raabe, C., Rozhdestvensky, T. S., Skryabin, B. V., & Brosius, J. (2018) · bioRxiv · doi:10.1101/260968 · Cited by 4
Song, W., Creighton, S. D., Michalski, B., Mojgani, J. S., Kapadia, M., Ma, D., Šakić, B., Zovkic, I. B., & Fahnestock, M. L. (2025) · Biology of Sex Differences · doi:10.1186/s13293-025-00790-9 · Cited by 3
“On the other hand, the upregulated m App following GDX in females may also aggravate amyloid pathology, as a study comparing APP/PS1 mice with and without the endogenous mouse App gene indicated that the additional mouse Aβ increased soluble amyloid accumulation [57].”
Deletion of Dcf1 Reduces Amyloid-β Aggregation and Mitigates Memory Deficits
Li, W., Gan, L., Ma, F.-F., Feng, R., Wang, J., Li, Y., Sun, Y., Wang, Y.-J., Diao, X., Qian, F.-Y., et al. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-200619 · Cited by 4
“After sealing the sections with coverslips, the samples were imaged using a 488-nm wavelength laser on a confocal microscope (LSM710, Zeiss, Germany) [34].”
What's New on Alzheimer's Disease? Insights From AD Mouse Models
Rey, C. C., Cattaud, V., Rampon, C., & Verret, L. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.11400-x · Cited by 6
“In fact, murine APP produces lower levels of Aβ and has a lower aggregation capacity even after overexpression of APP (Jankowsky et al., 2007).”
BackgroundAnimal Models of Alzheimer’s Disease
Kiyota, T. (2013) · Springer protocols handbooks/Springer protocols · doi:10.1007/978-1-4614-8794-4_35 · Cited by 3
In Vivo Seeding of Amyloid-β Protein and Implications in Modeling Alzheimer’s Disease Pathology
Liu, Q., Song, S., Liu, L., & Hong, W. (2025) · Biomolecules · doi:10.3390/biom15040571 · Cited by 5
Ahmed, M. M., Wang, A. C.-J., Elos, M. T., Chial, H. J., Sillau, S. H., Solano, D., Coughlan, C. M., Aghili, L., Anton, P., Markham, N., et al. (2021) · bioRxiv · doi:10.1101/2021.07.04.451073 · Cited by 2
“propensity to aggregate into neurotoxic b-sheet oligomers and fibrils (48).”
BackgroundKucheryavykh, L., Rivera, J. O., Ermolinsky, B., Tsytsarev, V., Cary, L., Alves, J., Reyes, A., de la Cruz-Rivera, N., Gonzalez, K. R., Irizarry, F. N., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110450 · Cited by 1
“Given that extracellular A β oligomers form soluble filamentous plaques in rodents [30], our data may represent the first detection of such soluble A β oligomers in the glioma microenvironment, as previously hypothesized [31,32].”
Vidal, R., & Ghetti, B. F. (2012) · Prion · doi:10.4161/pri.21023 · Cited by 1
Li, J., Liu, G.-L., Wang, X.-T., Song, Z., Chen, H., Hou, H.-W., & Hu, Q.-Y. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1929468
The Uppsala APP Mutation Promotes Wild‐Type Amyloid‐β Aggregation and Deposition In Vivo
Ge, J.-Y., de la Vega, M. P., Zampar, S., Cerilli, E., Koutarapu, S., Wu, L., Fraser, P. E., Arkan, S., Giedraitis, V., Lannfelt, L., et al. (2026) · Advancement of science · doi:10.1002/advs.202514179
“Murine A β does not seem to contribute to plaque formation in these models, meaning that their A β pathology typically consists of human A β only [ 8, 9 ].”
Behrangi, N., Stadler, M.-S., Reinbach, C., Burkert, L., Hawlitschka, A., Kaddatz, H., Wenzel, L., Llovera, G., Wree, A., Hoornaert, C., et al. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-06107-0
“…The Jackson Laboratory), which co-express the chimeric mouse/human amyloid precursor protein (APP695, Swedish K670M/N671L mutation, Mo/HuAPPswe) and human pre-senilin-1 (PS1dE9, exon-9 deletion) under the control of the mouse prion protein promoter [24] were used as a model for Alzheimer’s disease.”
The Icelandic mutation APPA673T on amyloid-β plaque burden in the 5xFAD Alzheimer modelPreprint
Anschuetz, A., Listyono, R., Vorley, T., Platt, B., Harrington, C. R., Riedel, G., & Schwab, K. (2025) · bioRxiv · doi:10.1101/2025.11.05.686739
“On the contrary, Jankowsky and co-workers showed that overexpression of mouse APP did not alter Aβ pathology when expressed on a PS1dE9 background, while it increased Aβ pathology when expressed on a more aggressive APPswe/PS1dE9 background (Jankowsky et al., 2007).”
Auboyer, L. (2018) · theses.fr (ABES) · doi:10.70675/07243ef7zb974z4ad8z97d9zd046801798b1
“Par ailleurs, le peptide Aβ d’origine murine reste présent chez ces souris et pourrait éventuellement interférer avec les différentes étapes de la mise en place de la pathologie dans le modèle (Fung et al., 2004; Jankowsky et al., 2007; Ye et al., 2006).”
Background
Metadata
- Authors
- Jankowsky, J. L., Younkin, L. H., Gonzales, V., Fadale, D. J., Slunt, H. H., Lester, H. A., Younkin, S. G., & Borchelt, D. R.
- Affiliations
- California Institute of Technology (US)
- Mayo Clinic (US)
- Johns Hopkins University (US)
- University of Florida (US)
- Corresponding author
- Jankowsky, Joanna L.
- Borchelt, David R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-08
- Volume
- 282
- Issue
- 31
- Pages
- 22707-22720
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC4435736
- OpenAlex
- W2156398762
- Cited by
- 122
- References
- 56
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 5 · 2023: 8 · 2022: 4 · 2021: 13 · 2020: 9 · 2019: 3 · 2018: 7 · 2017: 4 · 2016: 3 · 2015: 7 · 2014: 4 · 2013: 6 · 2012: 10
- FWCI
- 3.80
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- John Douglas French Alzheimer's Foundation
- National Institutes of Health
- National Institute on Aging (K01 AG26144-01, AG06656, 1 P01 AG-98-003, K01AG026144, 1 P50 AG-14-248)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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-beta, amyloid precursor protein, APPswe, transgenic mice, Alzheimer's disease, amyloid deposition, detergent solubility, vascular amyloid, triple transgenic mice
- MeSH terms
- Amino Acid Sequence, Amyloid, Animals, Humans, Mice, Inbred C57BL, Mice, Transgenic, Molecular Sequence Data, Peptides, Solubility, Amyloid beta-Peptides, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Transgenes, Mice, Presenilin-1
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