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Effects of PS1 Deficiency on Membrane Protein Trafficking in Neurons
Open accessAbstract
We have examined the trafficking and metabolism of the beta-amyloid precursor protein (APP), an APP homolog (APLP1), and TrkB in neurons that lack PS1. We report that PS1-deficient neurons fail to secrete Abeta, and that the rate of appearance of soluble APP derivatives in the conditioned medium is increased. Remarkably, carboxyl-terminal fragments (CTFs) derived from APP and APLP1 accumulate in PS1-deficient neurons. Hence, PS1 plays a role in promoting intramembrane cleavage and/or degradation of membrane-bound CTFs. Moreover, the maturation of TrkB and BDNF-inducible TrkB autophosphorylation is severely compromised in neurons lacking PS1. We conclude that PS1 plays an essential role in modulating trafficking and metabolism of a selected set of membrane and secretory proteins in neurons.
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“Tail biopsy samples were used to isolate DNA to confirm the genotype of the strain using previously established primers by PCR93–95.”
From Serum amyloid P secreted by bone marrow adipocytes drives skeletal amyloidosis (2025) · cites this paper as [95]
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Alzheimer's presenilin 1 is a putative membrane receptor for rab GDP dissociation inhibitor
Scheper, W. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.2.303 · Cited by 45
“This is supported by studies in which deletion of PS-1 or its Caenorhabditis elegans homolog affect sorting/maturation of proteins such as the TrkB receptor (32) and the Not receptor (33).”
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“…that PS1 is required for endoproteolytic processing at residues 42 and 43 (Kim and Sisodia, unpublished observation) within the transmembrane segment of the APP homolog, termed APLP1 (Naruse et al., 1998); notably, the transmembrane domains of APP and APLP1 have very little sequence homology.”
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Suppression of APP‐containing vesicle trafficking and production of β‐amyloid by AID/DHHC‐12 protein
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“…supporting a role for Psen1 in intramembranous, ‘γ-secretase’ processing not only of the β-amyloid precursor protein (APP) (De Strooper et al., 1998; Naruse et al., 1998), but also an increasing list of various type I membrane proteins, including Notch1 (De Strooper et al., 1999; Struhl and…”
BackgroundSelf-citationPresenilin and γ‐secretase: structure meets function
Wolfe, M. S. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00245.x · Cited by 43
“These ®ndings argue strongly against a direct traf®cking, chaperoning or folding role of presenilins in facilitating g-secretase activity, although presenilins may have some indirect effect on these functions (Naruse et al. 1998).”
BackgroundMureşan, V., & Muresan, Z. L. (2009) · Future Neurology · doi:10.2217/fnl.09.54 · Cited by 41
Neurotrophins and Neurodegenerative Diseases: Receptors Stuck in Traffic?
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Amyloid, Presenilins, and Alzheimer’s Disease
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Self-citationγ-Secretase Inhibitors as Molecular Probes of Presenilin Function
Wolfe, M. S. (2001) · Journal of Molecular Neuroscience · doi:10.1385/jmn:17:2:199 · Cited by 40
“These include roles in protein trafficking (Naruse et al., 1998), apoptosis (Wolozin et al., 1996), cell adhesion (Schwarzman et al., 1999), and signal transduction (De Strooper et al., 1999a).”
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Wilson, C., Doms, R. W., & Lee, V. M. ‐. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10776 · Cited by 37
“Concomitantly, there is an accumulation of pre- cleavage APP carboxy-terminal fragments (CTFs), suggesting that the blockade of A production occurs at the level of -secretase (De Strooper et al., 1998; Naruse et al., 1998).”
BackgroundResultInfluentialWrigley, J. D. J., Schurov, I., Nunn, E. J., Martin, A. C. L., Clarke, E. E., Ellis, S., Bonnert, T. P., Shearman, M. S., & Beher, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413086200 · Cited by 37
Presenilin-Dependent Gamma-Secretase Activity Modulates Neurite Outgrowth
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Physiologic and Pathologic Events Mediated by Intramembranous and Juxtamembranous Proteolysis
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Paganelli, A. R., Ocaña, O. H., Prat, M. I., Franco, P. G., López, S. L., Morelli, L., Adamo, A. M., Riccomagno, M. M., Matsubara, E., Shoji, M., et al. (2001) · Mechanisms of Development · doi:10.1016/s0925-4773(01)00458-0 · Cited by 35
“Other lines of research have proposed that presenilins play a role in traf®cking and metabolism of membrane and secreted proteins in neurons (Naruse et al., 1998).”
Secretases as therapeutic targets for the treatment of Alzheimer's disease
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Sun, Y., Islam, S., Michikawa, M., & Zou, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031757 · Cited by 33
Novel Role of Presenilins in Maturation and Transport of Integrin β1
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Inhibition of neurite outgrowth by familial Alzheimer's disease-linked presenilin-1 mutations
Dowjat, W. K., Wısnıewskı, T., Efthimiopoulos, S., & Wı́sniewski, H. M. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00351-1 · Cited by 32
Biology of presenilins as causative molecules for Alzheimer disease
Nishimura, M., Yu, G., & George‐Hyslop, P. S. (1999) · Clinical Genetics · doi:10.1034/j.1399-0004.1999.550401.x · Cited by 32
“This fact supports a hypothesis that the PS-deficiency alters trafficking of proteolytic C-terminal fragments of APP and APLP1 to specific subcellular compartments that contain ‘g-secretase activity’ rather than the alternative speculation that PSs play a direct role in APP processing by g-secretase (29).”
BackgroundTMP21 degradation is mediated by the ubiquitin‐proteasome pathway
Liu, S., Bromley‐Brits, K., Xia, K., Mittelholtz, J., Wang, R., & Song, W. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06497.x · Cited by 32
What Can Rodent Models Tell Us About Cognitive Decline in Alzheimer's Disease?
Davis, S., & Laroche, S. (2003) · Molecular Neurobiology · doi:10.1385/mn:27:3:249 · Cited by 32
Presenilin 1 Interacts with Acetylcholinesterase and Alters Its Enzymatic Activity and Glycosylation
Silveyra, M. X., Evin, G. M., Montenegro, M. F., Vidal, C. J., Martı́nez, S., Culvenor, J. G., & Sáez‐Valero, J. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02065-07 · Cited by 32
Suga, K., Saito, A., Tomiyama, T., Mori, H., & Akagawa, K. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03210.x · Cited by 30
Convergence of Presenilin- and Tau-Mediated Pathways on Axonal Trafficking and Neuronal Function
Peethumnongsin, E., Li, Y., Kallhoff, V., Hu, L., Takashima, A., Pautler, R. G., & Zheng, H. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1964-10.2010 · Cited by 30
“Loss of presenilin in primary neurons results in decreased maturation and membrane localization of TrkB, the primary receptor for BDNF (Naruse et al., 1998).”
BackgroundCellular and molecular basis of beta-amyloid precursor protein metabolism
Xu, H. (1998) · Frontiers in bioscience · doi:10.2741/a283 · Cited by 30
Trafficking in neurons: Searching for new targets for Alzheimer's disease future therapies
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Intracellular Retention of Caveolin 1 in Presenilin-deficient Cells
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Mutant presenilin (A260V) affects Rab8 in PC12D cell
Kametani, F., Usami, M., Tanaka, K., Kume, H., & Mori, H. (2003) · Neurochemistry International · doi:10.1016/s0197-0186(03)00176-1 · Cited by 28
Presenilin‐1 and intracellular calcium stores regulate neuronal glutamate uptake
Yang, Y., Kinney, G. A., Spain, W. J., Breitner, J. C. S., & Cook, D. G. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02279.x · Cited by 28
“These findings are consistent with previous studies showing that PS1 affects protein trafficking at the cell surface in a protein specific manner (Naruse et al. 1998; Cai et al. 2002; Goutte et al. 2002; Leem et al. 2002a,b).”
BackgroundResultRole of presenilin in γ-secretase cleavage of amyloid precursor protein
Xia, W. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00111-x · Cited by 28
Kuzuya, A., Uemura, K., Kitagawa, N., Aoyagi, N., Kihara, T., Ninomiya, H., Ishiura, S., Takahashi, R., & Shimohama, S. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.21104 · Cited by 28
“Indeed, PS1 deficiency affects the intracellular trafficking and maturation of TrkB, as well as ICAM5/telenchephalin in neurons (Naruse et al., 1998; Annaert et al., 2001).”
BackgroundRac1 changes the substrate specificity of γ-secretase between amyloid precursor protein and Notch1
Boo, J. H., Sohn, J. H., Kim, J. E., Song, H., & Mook-Jung, I. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.05.153 · Cited by 32
Presenilin Promotes Dietary Copper Uptake
Southon, A. G., Greenough, M. A., Ganio, G., Bush, A. I., Burke, R., & Camakaris, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062811 · Cited by 27
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“…trafficking of APP can be a key factor in generation of Ab42, supporting the conclusions of others who have worked in continuously cultured cells (Naruse et al. 1998; Chen et al. 2000; Kaether et al. 2002; Leem et al. 2002; Cai et al. 2003; Wrigley et al. 2003; Wang et al. 2004b, 2006; Zhang et…”
BackgroundSingh, J., & Mlodzik, M. (2012) · Developmental Cell · doi:10.1016/j.devcel.2012.04.021 · Cited by 27
“Transcriptional Regulation of hbs Expression In contrast to Nct and Psn, which appear to be uniformly expressed in Drosophila (Nowotny et al., 2000; Ye and Fortini, 1998), hbs expression is highly regulated and under the control of several signaling pathways in different tissues (although hbs is…”
BackgroundShirotani, K., Takahashi, K., Araki, W., Maruyama, K., & Tabira, T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3681 · Cited by 27
Intracellular trafficking of TREM2 is regulated by presenilin 1
Zhao, Y., Li, X., Huang, T. Y., Jiang, L.-L., Tan, Z., Zhang, M., Cheng, I. H.-J., Wang, X., Bu, G., Zhang, Y., et al. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.200 · Cited by 26
Presenilin Function in APP Processing
Annaert, W. G., Cupers, P., Säftig, P., & Strooper, B. D. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06917.x · Cited by 27
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“However, for APP and the mouse APP paralogue, the APP-like protein 1, a ,42 kDa C-terminal fragment accumulated in addition to shorter a-secretase cleaved fragments [34].”
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Alzheimer’s disease manifests abnormal sphingolipid metabolism
Uranbileg, B., Isago, H., Sakai, E., Kubota, M., Saito, Y., & Kurano, M. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1368839 · Cited by 24
A Review of the Familial Alzheimer’s Disease Locus PRESENILIN 2 and Its Relationship to PRESENILIN 1
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Presenilins, β-amyloid precursor protein and the molecular basis of Alzheimer's disease
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Morton, R. A., Kuenzi, F. M., Fitzjohn, S. M., Rosahl, T. W., Smith, D., Zheng, H., Shearman, M. S., Collingridge, G. L., & Seabrook, G. R. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(01)02512-5 · Cited by 23
Presenilin‐1‐mediated Retention of APP Derivatives in Early Biosynthetic Compartments
Réchards, M., Xia, W., Oorschot, V. M. J., van Dijk, S., Annaert, W. G., Selkoe, D. J., & Klumperman, J. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00388.x · Cited by 23
“Indeed, pulse-chase studies (12,13) and in vitro budding assays (14) have indicated enhanced transport of APP through the biosynthetic pathway in the absence of functional PS-1.”
BackgroundTorp, R., Ottersen, O. P., Cotman, C. W., & Head, E. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00320-8 · Cited by 23
γ-Secretase Modulatory Proteins: The Guiding Hand Behind the Running Scissors
Wong, E., Frost, G. R., & Li, Y. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.614690 · Cited by 23
“(2) Cultured neurons isolated from PS1-deficient mice produce significantly less Aβ and APP fragments that are not processed by γ-secretase is being accumulated (Naruse et al., 1998; De Strooper et al., 1998).”
BackgroundAlternative transcripts of presenilin-1 associated with frontotemporal dementia
Evin, G. M., Smith, M. J., Tziotis, A., McLean, C., Canterford, L. D., Sharples, R. A., Cappai, R., Weidemann, A., Beyreuther, K. T., Cotton, R. G. H., et al. (2002) · Neuroreport · doi:10.1097/00001756-200204160-00036 · Cited by 22
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Presenilin 1 mutations influence processing and trafficking of the ApoE receptor apoER2
Wang, W., Moerman, A., Slaton, A., & Barger, S. W. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.10.005 · Cited by 23
“Presenilins appear to influence intracellular protein trafficking independently of γ-secretase activity (L’HernaultArduengo, 1992; Naruse et al., 1998; Nishimura et al., 1999).”
BackgroundResultHamano, T., Mutoh, T., Tabira, T., Araki, W., Kuriyama, M., Mihara, T., Yano, S., & Yamamoto, H. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2005.02.018 · Cited by 21
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What Can N-glycomics and N-glycoproteomics of Cerebrospinal Fluid Tell Us about Alzheimer Disease?
Gaunitz, S., Tjernberg, L. O., & Schedin‐Weiss, S. (2021) · Biomolecules · doi:10.3390/biom11060858 · Cited by 20
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“In addition, it has been demonstrated that the steady-state levels of functional TrkB receptors, which are activated by brain-derived neurotrophic factor, are diminished in PS1-deficient neurons (Naruse et al., 1998).”
BackgroundProteolysis by presenilins and the renaissance of tau
Haass, C., & Mandelkow, E. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01576-7 · Cited by 20
The Role of Presenilin in Protein Trafficking and Degradation—Implications for Metal Homeostasis
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“Zinc”
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γ-Secretase: never more enigmatic
Sisodia, S. S., Annaert, W. G., Kim, S., & Strooper, B. D. (2001) · Trends in Neurosciences · doi:10.1016/s0166-2236(01)00002-9 · Cited by 18
Self-citationSuga, K., Saito, A., Tomiyama, T., Mori, H., & Akagawa, K. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp138 · Cited by 17
Alternative transcripts of presenilin-1 associated with frontotemporal dementia
Evin, G. M., Smith, M. J., Tziotis, A., McLean, C., Canterford, L. D., Sharples, R. A., Cappai, R., Weidemann, A., Beyreuther, K. T., Cotton, R. G. H., et al. (2002) · Neuroreport · doi:10.1097/00001756-200205070-00036 · Cited by 17
Piccini, A., Fassio, A., Pasqualetto, E., Vitali, A., Borghi, R., Palmieri, D., Nacmias, B., Sorbi, S., Sitia, R., & Tabaton, M. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.11.013 · Cited by 17
“…proteins with similar topology (Cook et al., 1996), and are part of a complex that operates the intramembrane cleavage of different type I transmembrane proteins, such as APP (De Strooper et al., 1998), APLP 1 (Naruse et al., 1998), Notch 1 (De Strooper et al., 1999), and ErbB4 (Lee et al., 2002).”
BackgroundSerum amyloid P secreted by bone marrow adipocytes drives skeletal amyloidosis
Kumar, S., Song, K., Wang, J., Baghel, M. S., Zeng, Y., Shen, K., Zheng, J., Crane, J., Demehri, S., Gao, P., et al. (2025) · Nature Aging · doi:10.1038/s43587-025-00924-z · Cited by 16
“Tail biopsy samples were used to isolate DNA to confirm the genotype of the strain using previously established primers by PCR 93–95 .”
Self-citationBiogenesis and processing of the amyloid precursor protein in the early secretory pathway
Selivanova, A. V., Winblad, B. G., Dantuma, N. P., & Farmery, M. R. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.062 · Cited by 15
“presenilin-1 may be important for regulation of intracellular trafficking of certain membrane proteins [15,16], including APP since delivery of APP at the cell surface is dependent on presenilin-1 [17].”
BackgroundSteiner, H., Winkler, E., Shearman, M. S., Prywes, R., & Haass, C. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0405 · Cited by 15
“…are required for the g-secretase cleavage of selected type I transmembrane proteins (for review see Steiner and Haass, 2000) such as bAPP (De Strooper et al., 1998) and its homologues (Naruse et al., 1998) as well as Notch (De Strooper et al., 1999) a protein required for cellular differentiation.”
BackgroundCell-Free Generation of the Notch1 Intracellular Domain (NICD) and APP-CTFγ
Ikeuchi, T., & Sisodia, S. S. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:1:1:43 · Cited by 15
“…PS in intramembrane “γ-secretase” processing of type I membrane proteins, including the β-amyloid precursor proteins (APP) (De Strooper et al., 1998; Naruse et al., 1998) and the receptor, Notch1 (De Strooper et al., 1999). γ-secretase processing of a set of APP derivatives, termed APP-CTFs,…”
BackgroundSelf-citationWong, P. C., Cai, H., Borcheit, D. R., & Price, D. L. (2001) · Journal of Molecular Neuroscience · doi:10.1385/jmn:17:2:233 · Cited by 14
“…acts as an aspartyl protease (i.e., γ-secretase), functions as a co-factor critical for the activity of γ-secretase, or exerts its influence by playing a role in trafficking of APP to the proper compartment for γ-secretase cleavage (De Strooper et al. 1998; Naruse et al., 1998; Wolfe et al., 1999).”
BackgroundSelf-citationSuga, K., Saito, A., & Akagawa, K. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.01.001 · Cited by 13
Histologic and molecular characterizations of megakaryocytic leukemia in mice
Hao, X., Shin, M. S., Zhou, J. X., Lee, C. H., Chen, Q., Naghashfar, Z., Hartley, J. W., Fredrickson, T. N., Ward, J. M., & Morse, H. C. (2005) · Leukemia Research · doi:10.1016/j.leukres.2005.08.021 · Cited by 13
Cook, D. G., Li, X., Cherry, S. D., & Cantrell, A. R. (2005) · Journal of Neurophysiology · doi:10.1152/jn.00745.2005 · Cited by 13
“Presenilin 1 Deficiency Alters the Activity of Voltage-Gated Ca2 Channels in Cultured Cortical Neurons”
BackgroundMurphy, M. P., Uljon, S., Golde, T. E., & Wang, R. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(01)00098-9 · Cited by 12
Jiang, H., Pederson, S., Newman, M., Dong, Y., Barthelson, K., & Lardelli, M. T. (2020) · PLoS ONE · doi:10.1371/journal.pone.0232559 · Cited by 13
“The absence of PSEN1 is thought to reduce γ-secretase activity in mammalian cells [8, 9], while the absence of both PSEN1 and PSEN2 is thought to eliminate it completely [10, 11] although some data does not agree with this (reviewed in Jayne et al.”
BackgroundLu, Q., Ding, K., Frosch, M. P., Jones, S. B., Wolfe, M. S., Xia, W., & Lanford, G. W. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100585 · Cited by 11
“PS1 overexpression promoted the production of Aβ42 [8], and the PS1 knockout mice showed reduced Aβ42 production [9] and Aβ secretion [10].”
Wnt-1 expression in PC12 cells induces exon 15 deletion and expression of L-APP
Morin, P. J., Medina, M., Semënov, M. V., Brown, A. M. C., & Kosik, K. S. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.01.004 · Cited by 11
“PS1 disruption has also been associated with defective trafficking of APP (Kim et al., 2001) and other neuronal membrane proteins (Naruse et al., 1998), suggesting that PS1 may be important for a trafficking function in early biosynthetic membrane compartments.”
BackgroundGamliel, A., Teicher, C., Hartmann, T., Beyreuther, K. T., & Stein, R. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00830-8 · Cited by 11
Analysis of Presenilin 1 and 2 interacting proteins in mouse cerebral cortex during development
Kumar, A., & Thakur, M. K. (2014) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2014.08.010 · Cited by 10
APLP1 as a cerebrospinal fluid biomarker for γ-secretase modulator treatment
Sjödin, S., Andersson, K. K. A., Mercken, M. H., Zetterberg, H., Borghys, H., Blennow, K., & Portelius, E. (2015) · Alzheimer s Research & Therapy · doi:10.1186/s13195-015-0160-z · Cited by 10
Secretases as targets for beta‐amyloid lowering drugs
Walter, J., & Haass, C. (2002) · Drug Development Research · doi:10.1002/ddr.10076 · Cited by 10
“It was then shown that gsecretase activity is strongly reduced in cells derived from PS1 knockout mice [Naruse et al., 1998; Harriman et al., 2000; Zhang et al., 2000] and is not detectable in PS1/PS2 double knockout cells [Herreman et al., 2000; Zhang et al., 2000], strongly indicating that PSs…”
Parent, A., & Thinakaran, G. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2010/825918 · Cited by 10
“As supported by mouse model studies, it appears that PS1 contributes largely to total β-amyloid (Aβ) production in the brain [11, 12].”
BackgroundSelf-citationConditionally targeted deletion of PSEN1 leads to diastolic heart dysfunction
Song, X., Yuan, Q., Tang, Y., Cao, M., Shen, Y., Zeng, Z., Lei, C., Li, S., Zhao, X., & YANG, Y.-J. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26057 · Cited by 10
“…severe than those of three other conditional PSEN1 knockout mice, indicating that PSEN1 also has functions beyond the heart, such as acting as a protease of the γ-secretase complex to regulate the microenvironment of myocardial cells through cutting membrane embedded proteins (Naruse et al., 1998).”
BackgroundMutation of conserved aspartates affect maturation of presenilin 1 and presenilin 2 complexes
Yu, G., Chen, F., Nishimura, M., Steiner, H., Tandon, A., Kawarai, T., Arawaka, S., Supala, A., Song, Y., Rogaeva, E. A., et al. (2000) · Acta Neurologica Scandinavica · doi:10.1034/j.1600-0404.2000.00301.x · Cited by 9
Presenilin 1 Modulates Acetylcholinesterase Trafficking and Maturation
Cortés‐Gómez, M., Barberá, V. M., Alom, J., Sáez‐Valero, J., & García‐Ayllón, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021437 · Cited by 9
“CHO-PS1 cells overexpress human wild-type APP together with PS1, leading to an increase in generation of Aβ42 peptide.”
BackgroundInfluentialNeurobiology of Alzheimer’s Disease
Wong, P. C., Savonenko, A. V., Li, T., & Price, D. L. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-374947-5.00046-8 · Cited by 9
Self-citationPitsi, D., Kienlen‐Campard, P., & Octave, J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01138.x · Cited by 10
“These results are in line with many other reports suggesting an upstream role of PS1 in the metabolism of APP, and possibly of other proteins (Naruse et al. 1998).”
ResultInteraction between the APOE ɛ4 allele and the APH-1b c+651T>G SNP in Alzheimer's disease
Poli, M., Gatta, L. B., Lovati, C., Mariani, C. B., Galimberti, D., Scarpini, E. A., Biunno, I., Musicco, M., Dominici, R., Albertini, A., et al. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.03.019 · Cited by 8
Metadata
- Authors
- Naruse, S., Thinakaran, G., Luo, J.-J., Kusiak, J. W., Tomita, T., Iwatsubo, T., Qian, X., Ginty, D. D., Price, D. L., Borchelt, D. R., Wong, P. C., & Sisodia, S. S.
- Affiliations
- University of Chicago (US)
- Johns Hopkins University (US)
- National Institute on Aging (US)
- The University of Tokyo (JP)
- Corresponding author
- Sisodia, Sangram S
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1998-11
- Volume
- 21
- Issue
- 5
- Pages
- 1213-1221
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W1994453752
- Cited by
- 355
- References
- 43
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 2 · 2023: 3 · 2022: 1 · 2021: 2 · 2020: 3 · 2019: 2 · 2018: 2 · 2017: 4 · 2016: 5 · 2015: 4 · 2014: 4 · 2013: 12 · 2012: 7
- FWCI
- 22.15
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Neuron (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (1PO1 AG 14248, P50AG005146, P01AG014248, AG 05146)
- National Institute of Neurological Disorders and Stroke (NS-20471)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- presenilin 1, APP, APLP1, amyloid-beta, carboxyl-terminal fragment, membrane protein trafficking, TrkB, brain-derived neurotrophic factor, autophosphorylation, intramembrane cleavage, protein degradation, Alzheimer's disease, neurons
- MeSH terms
- Alzheimer Disease, Animals, Cells, Cultured, Cerebral Cortex, Fetus, Membrane Proteins, Molecular Sequence Data, Neurons, Amyloid beta-Protein Precursor, Mice, Knockout, Mice, Presenilin-1
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