The innate immunity protein IFITM3 modulates γ-secretase in Alzheimer's disease.
Age of Onset
Aged, 80 and over
Aging
/ genetics
Alzheimer Disease
/ genetics
Amyloid Precursor Protein Secretases
/ chemistry
Amyloid beta-Protein Precursor
/ chemistry
Animals
Astrocytes
/ metabolism
Catalytic Domain
Disease Models, Animal
Female
HEK293 Cells
Humans
Immunity, Innate
Inflammation
Male
Membrane Proteins
/ deficiency
Mice
Mice, Inbred C57BL
Mice, Transgenic
Presenilin-1
/ metabolism
RNA-Binding Proteins
/ genetics
Risk
Up-Regulation
Journal
Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462
Informations de publication
Date de publication:
10 2020
10 2020
Historique:
received:
20
07
2019
accepted:
29
05
2020
pubmed:
4
9
2020
medline:
15
1
2021
entrez:
4
9
2020
Statut:
ppublish
Résumé
Innate immunity is associated with Alzheimer's disease
Identifiants
pubmed: 32879487
doi: 10.1038/s41586-020-2681-2
pii: 10.1038/s41586-020-2681-2
pmc: PMC7919141
mid: NIHMS1599391
doi:
Substances chimiques
APP protein, human
0
Amyloid beta-Protein Precursor
0
IFITM3 protein, human
0
Membrane Proteins
0
PSEN1 protein, human
0
Presenilin-1
0
RNA-Binding Proteins
0
Amyloid Precursor Protein Secretases
EC 3.4.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
735-740Subventions
Organisme : NIA NIH HHS
ID : R01 AG026660
Pays : United States
Organisme : NIA NIH HHS
ID : RF1 AG057440
Pays : United States
Organisme : NIA NIH HHS
ID : P30 AG062429
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA008748
Pays : United States
Organisme : NIA NIH HHS
ID : R01 AG061350
Pays : United States
Organisme : NIA NIH HHS
ID : R01 AG018440
Pays : United States
Organisme : NIA NIH HHS
ID : R01 AG006170
Pays : United States
Organisme : NIA NIH HHS
ID : RF1 AG057593
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS096275
Pays : United States
Organisme : NIA NIH HHS
ID : U01 AG046170
Pays : United States
Organisme : NIA NIH HHS
ID : R01 AG057907
Pays : United States
Organisme : NIH HHS
ID : S10 OD018522
Pays : United States
Organisme : NIH HHS
ID : S10 OD026880
Pays : United States
Organisme : NIA NIH HHS
ID : K01 AG062683
Pays : United States
Commentaires et corrections
Type : CommentIn
Références
Shi, Y. & Holtzman, D. M. Interplay between innate immunity and Alzheimer disease: APOE and TREM2 in the spotlight. Nat. Rev. Immunol. 18, 759–772 (2018).
pubmed: 30140051
pmcid: 6425488
Griciuc, A. et al. Alzheimer’s disease risk gene CD33 inhibits microglial uptake of amyloid beta. Neuron 78, 631–643 (2013).
pubmed: 23623698
pmcid: 3706457
Wang, Y. et al. TREM2 lipid sensing sustains the microglial response in an Alzheimer’s disease model. Cell 160, 1061–1071 (2015).
pubmed: 25728668
pmcid: 4477963
De Strooper, B. Aph-1, Pen-2, and Nicastrin with Presenilin generate an active γ-secretase complex. Neuron 38, 9–12 (2003).
pubmed: 12691659
Gertsik, N., Chiu, D. & Li, Y. M. Complex regulation of γ-secretase: from obligatory to modulatory subunits. Front. Aging Neurosci. 6, 342 (2015).
pubmed: 25610395
pmcid: 4285130
Villa, J. C. et al. Nontranscriptional role of Hif-1α in activation of γ-secretase and notch signaling in breast cancer. Cell Rep. 8, 1077–1092 (2014).
pubmed: 25131208
pmcid: 4346175
Crump, C. J., Johnson, D. S. & Li, Y.-M. Development and mechanism of γ-secretase modulators for Alzheimer’s disease. Biochemistry 52, 3197–3216 (2013).
pubmed: 23614767
Wagner, S. L. et al. Soluble γ-secretase modulators selectively inhibit the production of the 42-amino acid amyloid β peptide variant and augment the production of multiple carboxy-truncated amyloid β species. Biochemistry 53, 702–713 (2014).
pubmed: 24401146
pmcid: 3929337
Wagner, S. L. et al. Pharmacological and toxicological properties of the potent oral γ-secretase modulator BPN-15606. J. Pharmacol. Exp. Ther. 362, 31–44 (2017).
pubmed: 28416568
pmcid: 5454592
Kounnas, M. Z. et al. Modulation of γ-secretase reduces β-amyloid deposition in a transgenic mouse model of Alzheimer’s disease. Neuron 67, 769–780 (2010).
pubmed: 20826309
pmcid: 2947312
Pozdnyakov, N. et al. γ-Secretase modulator (GSM) photoaffinity probes reveal distinct allosteric binding sites on presenilin. J. Biol. Chem. 288, 9710–9720 (2013).
pubmed: 23396974
pmcid: 3617273
Bailey, C. C., Zhong, G., Huang, I. C. & Farzan, M. IFITM-family proteins: the cell’s first line of antiviral defense. Annu. Rev. Virol. 1, 261–283 (2014).
pubmed: 25599080
pmcid: 4295558
Kumar, D. K. et al. Amyloid-β peptide protects against microbial infection in mouse and worm models of Alzheimer’s disease. Sci. Transl. Med. 8, 340ra72 (2016).
pubmed: 27225182
Eimer, W. A. et al. Alzheimer’s disease-associated β-amyloid is rapidly seeded by Herpesviridae to protect against brain infection. Neuron 100, 1527–1532 (2018).
pubmed: 30571943
Oakley, H. et al. Intraneuronal β-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer’s disease mutations: potential factors in amyloid plaque formation. J. Neurosci. 26, 10129–10140 (2006).
pubmed: 17021169
pmcid: 6674618
Allen, M. et al. Human whole genome genotype and transcriptome data for Alzheimer’s and other neurodegenerative diseases. Sci. Data 3, 160089 (2016).
pubmed: 27727239
pmcid: 5058336
GTEx Consortium. Human genomics. The Genotype-Tissue Expression (GTEx) pilot analysis: multitissue gene regulation in humans. Science 348, 648–660 (2015).
Wang, M. et al. The Mount Sinai cohort of large-scale genomic, transcriptomic and proteomic data in Alzheimer’s disease. Sci. Data 5, 180185 (2018).
pubmed: 30204156
pmcid: 6132187
Allen, E. K. et al. SNP-mediated disruption of CTCF binding at the IFITM3 promoter is associated with risk of severe influenza in humans. Nat. Med. 23, 975–983 (2017).
pubmed: 28714988
pmcid: 5702558
Frost, G. R. & Li, Y. M. The role of astrocytes in amyloid production and Alzheimer’s disease. Open Biol. 7, 170228 (2017).
pubmed: 29237809
pmcid: 5746550
Zhang, B. et al. Integrated systems approach identifies genetic nodes and networks in late-onset Alzheimer’s disease. Cell 153, 707–720 (2013).
pubmed: 23622250
pmcid: 3677161
Imamura, Y. et al. Inhibition of gamma-secretase activity by helical beta-peptide foldamers. J. Am. Chem. Soc. 131, 7353–7359 (2009).
pubmed: 19432477
Wakabayashi, T. et al. Analysis of the γ-secretase interactome and validation of its association with tetraspanin-enriched microdomains. Nat. Cell Biol. 11, 1340–1346 (2009).
pubmed: 19838174
Jonsson, T. et al. Variant of TREM2 associated with the risk of Alzheimer’s disease. N. Engl. J. Med. 368, 107–116 (2013).
pubmed: 23150908
Guerreiro, R. et al. TREM2 variants in Alzheimer’s disease. N. Engl. J. Med. 368, 117–127 (2013).
pubmed: 23150934
Bertram, L. et al. Genome-wide association analysis reveals putative Alzheimer’s disease susceptibility loci in addition to APOE. Am. J. Hum. Genet. 83, 623–632 (2008).
pubmed: 18976728
pmcid: 2668052
Baruch, K. et al. Aging-induced type I interferon response at the choroid plexus negatively affects brain function. Science 346, 89–93 (2014).
pubmed: 25147279
pmcid: 4869326
Li, Y. M. et al. Photoactivated gamma-secretase inhibitors directed to the active site covalently label presenilin 1. Nature 405, 689–694 (2000).
pubmed: 10864326
Chun, J., Yin, Y. I., Yang, G., Tarassishin, L. & Li, Y. M. Stereoselective synthesis of photoreactive peptidomimetic gamma-secretase inhibitors. J. Org. Chem. 69, 7344–7347 (2004).
pubmed: 15471490
Gertsik, N., Chau, D. M. & Li, Y. M. γ-secretase inhibitors and modulators induce distinct conformational changes in the active sites of γ-secretase and signal peptide peptidase. ACS Chem. Biol. 10, 1925–1931 (2015).
pubmed: 26030233
pmcid: 5436900
Crump, C. J. et al. Development of sulfonamide photoaffinity inhibitors for probing cellular γ-secretase. ACS Chem. Neurosci. 7, 1166–1173 (2016).
pubmed: 27253220
pmcid: 5576034
Crump, C. J. et al. Piperidine acetic acid based γ-secretase modulators directly bind to Presenilin-1. ACS Chem. Neurosci. 2, 705–710 (2011).
pubmed: 22229075
pmcid: 3249837
Crump, C. J. et al. BMS-708,163 targets presenilin and lacks notch-sparing activity. Biochemistry 51, 7209–7211 (2012).
pubmed: 22931393
pmcid: 3470910
Yang, G. et al. Stereo-controlled synthesis of novel photoreactive gamma-secretase inhibitors. Bioorg. Med. Chem. Lett. 19, 922–925 (2009).
pubmed: 19097779
Xu, M. et al. γ -Secretase: characterization and implication for Alzheimer disease therapy. Neurobiol. Aging 23, 1023–1030 (2002).
pubmed: 12470798
Pettersson, M. et al. Discovery of indole-derived pyridopyrazine-1,6-dione γ-secretase modulators that target presenilin. Bioorg. Med. Chem. Lett. 25, 908–913 (2015).
pubmed: 25582600
Sung, J. Y. et al. WAVE1 controls neuronal activity-induced mitochondrial distribution in dendritic spines. Proc. Natl Acad. Sci. USA 105, 3112–3116 (2008).
pubmed: 18287015
Ho, S. M. et al. Rapid Ngn2-induction of excitatory neurons from hiPSC-derived neural progenitor cells. Methods 101, 113–124 (2016).
pubmed: 26626326
Stanley, S. et al. Profiling of glucose-sensing neurons reveals that GHRH neurons are activated by hypoglycemia. Cell Metab. 18, 596–607 (2013).
pubmed: 24093682
Heiman, M., Kulicke, R., Fenster, R. J., Greengard, P. & Heintz, N. Cell type-specific mRNA purification by translating ribosome affinity purification (TRAP). Nat. Protoc. 9, 1282–1291 (2014).
pubmed: 24810037
R Core Team. A Language and Environment for Statistical Computing, R Foundation for Statistical Computing; https://www.R-project.org/ (Vienna, Austria 2017).
Chau, D. M., Crump, C. J., Villa, J. C., Scheinberg, D. A. & Li, Y. M. Familial Alzheimer disease presenilin-1 mutations alter the active site conformation of γ-secretase. J. Biol. Chem. 287, 17288–17296 (2012).
pubmed: 22461631
pmcid: 3366784
Shelton, C. C. et al. Modulation of γ-secretase specificity using small molecule allosteric inhibitors. Proc. Natl Acad. Sci. USA 106, 20228–20233 (2009).
pubmed: 19906985
Wong, E. et al. GSAP modulates γ-secretase specificity by inducing conformational change in PS1. Proc. Natl Acad. Sci. USA 116, 6385–6390 (2019).
pubmed: 30850537
Hur, J. Y. et al. Active γ-secretase is localized to detergent-resistant membranes in human brain. FEBS J. 275, 1174–1187 (2008).
pubmed: 18266764
Placanica, L., Zhu, L. & Li, Y. M. Gender- and age-dependent gamma-secretase activity in mouse brain and its implication in sporadic Alzheimer disease. PLoS ONE 4, e5088 (2009).
pubmed: 19352431
pmcid: 2661375
Placanica, L. et al. Pen2 and presenilin-1 modulate the dynamic equilibrium of presenilin-1 and presenilin-2 γ-secretase complexes. J. Biol. Chem. 284, 2967–2977 (2009).
pubmed: 19036728
pmcid: 2631949
Li, Y. M. et al. Presenilin 1 is linked with γ-secretase activity in the detergent solubilized state. Proc. Natl Acad. Sci. USA 97, 6138–6143 (2000).
pubmed: 10801983
Frykman, S. et al. Synaptic and endosomal localization of active gamma-secretase in rat brain. PLoS ONE 5, e8948 (2010).
pubmed: 20126630
pmcid: 2812513
Hur, J. Y. et al. Identification of novel γ-secretase-associated proteins in detergent-resistant membranes from brain. J. Biol. Chem. 287, 11991–12005 (2012).
pubmed: 22315232
pmcid: 3320946
Ahn, K. et al. Activation and intrinsic γ-secretase activity of presenilin 1. Proc. Natl Acad. Sci. USA 107, 21435–21440 (2010).
pubmed: 21115843
Shelton, C. C., Tian, Y., Frattini, M. G. & Li, Y. M. An exo-cell assay for examining real-time gamma-secretase activity and inhibition. Mol. Neurodegener. 4, 22 (2009).
pubmed: 19490610
pmcid: 3224971
Placanica, L. et al. Pen2 and presenilin-1 modulate the dynamic equilibrium of presenilin-1 and presenilin-2 gamma-secretase complexes. J. Biol. Chem. 284, 2967–2977 (2009).
pubmed: 19036728
pmcid: 2631949
Tian, Y., Bassit, B., Chau, D. & Li, Y. M. An APP inhibitory domain containing the Flemish mutation residue modulates gamma-secretase activity for Aβ production. Nat. Struct. Mol. Biol. 17, 151–158 (2010).
pubmed: 20062056
Tian, Y., Crump, C. J. & Li, Y. M. Dual role of α-secretase cleavage in the regulation of γ-secretase activity for amyloid production. J. Biol. Chem. 285, 32549–32556 (2010).
pubmed: 20675367
pmcid: 2952257
Muller, P. Y., Janovjak, H., Miserez, A. R. & Dobbie, Z. Processing of gene expression data generated by quantitative real-time RT-PCR. Biotechniques 32, 1372–1374, 1376, 1378–1379 (2002).
pubmed: 12074169
Wang, J. C. et al. Risk for nicotine dependence and lung cancer is conferred by mRNA expression levels and amino acid change in CHRNA5. Hum. Mol. Genet. 18, 3125–3135 (2009).
pubmed: 19443489
pmcid: 2714722
Wang, J. C. et al. Genetic variation in the CHRNA5 gene affects mRNA levels and is associated with risk for alcohol dependence. Mol. Psychiatry 14, 501–510 (2009).
pubmed: 18414406
Smyth, G. K. Linear models and empirical bayes methods for assessing differential expression in microarray experiments. Stat. Appl. Genet Mol. Biol. 3, (2004).
Readhead, B. et al. Multiscale analysis of independent alzheimer’s cohorts finds disruption of molecular, genetic, and clinical networks by human herpesvirus. Neuron 99, 64–82 (2018).
pubmed: 29937276
pmcid: 6551233
Inoue, M. et al. Human brain proteins showing neuron-specific interactions with γ-secretase. FEBS J. 282, 2587–2599 (2015).
pubmed: 25893612
Teranishi, Y. et al. Proton myo-inositol cotransporter is a novel γ-secretase associated protein that regulates Aβ production without affecting Notch cleavage. FEBS J. 282, 3438–3451 (2015).
pubmed: 26094765