Cited by 792Alzheimer's disease research and treatmentsMitochondrial Function and PathologyDementia and Cognitive Impairment Research

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Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction

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Devi, Latha, Prabhu, Badanavalu M., Galati, Domenico F., Avadhani, Narayan G., Anandatheerthavarada, Hindupur K.·2006·The Journal of Neuroscience

DOI 10.1523/jneurosci.1469-06.2006PMC PMC6675337

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Abstract

Mitochondrial dysfunction is one of the major intracellular lesions of Alzheimer's disease (AD). However, the causative factors involved in the mitochondrial dysfunction in human AD are not well understood. Here we report that nonglycosylated full-length and C-terminal truncated amyloid precursor protein (APP) accumulates exclusively in the protein import channels of mitochondria of human AD brains but not in age-matched controls. Furthermore, in AD brains, mitochondrially associated APP formed stable approximately 480 kDa complexes with the translocase of the outer mitochondrial membrane 40 (TOM40) import channel and a super complex of approximately 620 kDa with both mitochondrial TOM40 and the translocase of the inner mitochondrial membrane 23 (TIM23) import channel TIM23 in an "N(in mitochondria)-C(out cytoplasm)" orientation. Accumulation of APP across mitochondrial import channels, which varied with the severity of AD, inhibited the entry of nuclear-encoded cytochrome c oxidase subunits IV and Vb proteins, which was associated with decreased cytochrome c oxidase activity and increased levels of H2O2. Regional distribution of mitochondrial APP showed higher levels in AD-vulnerable brain regions, such as the frontal cortex, hippocampus, and amygdala. Mitochondrial accumulation of APP was also observed in the cholinergic, dopaminergic, GABAergic, and glutamatergic neuronal types in the category III AD brains. The levels of translocationally arrested mitochondrial APP directly correlated with mitochondrial dysfunction. Moreover, apolipoprotein genotype analysis revealed that AD subjects with the E3/E4 alleles had the highest content of mitochondrial APP. Collectively, these results suggest that abnormal accumulation of APP across mitochondrial import channels, causing mitochondrial dysfunction, is a hallmark of human AD pathology.

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PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,394
Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
Schägger, H., & von JAGOW, G. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90094-a · Cited by 2,267
The cholinergic hypothesis of Alzheimer’s disease: A review of progress
Francis, P. T., Palmer, A. M., Snape, M., & Wilcock, G. K. (1999) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp.66.2.137 · Cited by 2,198 · cited 1×
“In addition to cholinergic neurons, several other neuronal types, such as dopaminergic, GABAergic, and glutamatergic neurons, have been shown to be affected in the later stages of the pathogenesis of AD (Francis et al., 1999; Francis, 2003).”
Background
Copper, iron and zinc in Alzheimer's disease senile plaques
Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120
Editorial on Consensus Recommendations for the Postmortem Diagnosis of Alzheimer Disease from the National Institute on Aging and the Reagan Institute Working Group on Diagnostic Criteria for the Neuropathological Assessment of Alzheimer Disease
HYMAN, B. T., & TROJANOWSKI, J. Q. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199710000-00002 · Cited by 1,542
Treatment with a Copper-Zinc Chelator Markedly and Rapidly Inhibits β-Amyloid Accumulation in Alzheimer's Disease Transgenic Mice
Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447
Mitochondrial abnormalities in Alzheimer's disease
Hirai, K., Aliev, G., Nunomura, A., Fujioka, H., Russell, R. L., Atwood, C. S., Johnson, A. B., Kress, Y., Vinters, H. V., Tabaton, M., et al. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-09-03017.2001 · Cited by 1,367
Translating cell biology into therapeutic advances in Alzheimer's disease
Selkoe, D. J. (1999) · Nature · doi:10.1038/399a023 · Cited by 1,166
Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression
Manczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., & Reddy, P. H. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl066 · Cited by 1,104
Consensus Recommendations for the Postmortem Diagnosis of Alzheimer’s Disease
(1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00057-2 · Cited by 981
Mitochondria take center stage in aging and neurodegeneration
Beal, M. F. (2005) · Annals of Neurology · doi:10.1002/ana.20624 · Cited by 957
Consensus recommendations for the postmortem diagnosis of Alzheimer's disease. The National Institute on Aging, and Reagan Institute Working Group on Diagnostic Criteria for the Neuropathological Assessment of Alzheimer's Disease.
(1997) · PubMed · Cited by 745
Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
Caspersen, C., Wang, N., Yao, J., Sosunov, A., Chen, X., Lustbader, J. W., Xu, H. W., Stern, D., McKhann, G., & Du Yan, S. (2005) · The FASEB Journal · doi:10.1096/fj.05-3735fje · Cited by 738
Characterization of the human heart mitochondrial proteome
Taylor, S. W., Fahy, E., Zhang, B., Glenn, G. M., Warnock, D. E., Wiley, S. E., Murphy, A. N., Gaucher, S. P., Capaldi, R., Gibson, B. W., et al. (2003) · Nature Biotechnology · doi:10.1038/nbt793 · Cited by 702
Cytochrome oxidase deficiency in Alzheimer’s disease
Parker, W. D., Filley, C. M., & Parks, J. K. (1990) · Neurology · doi:10.1212/wnl.40.8.1302 · Cited by 598 · cited 1×
“Altered mitochondrial fluidity and the activity of mitochondrial cytochrome c oxidase, which is the terminal oxidase in the respiratory chain, have been reported to be low in the AD brains (Parker, 1991; Sims, 1996; Maurer et al., 2000).”
Background
MUTANT GENES IN FAMILIAL ALZHEIMER'S DISEASE AND TRANSGENIC MODELS
Price, D. L., & Sisodia, S. S. (1998) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.21.1.479 · Cited by 581
Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells
Anandatheerthavarada, H. K., Biswas, G., Robin, M.-A., & Avadhani, N. G. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207030 · Cited by 571
A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients
Maurer, I. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00112-3 · Cited by 475
Untitled work
Selkoe (1999) · doi:10.1038/19866 · Cited by 468
Differential Expression of Oxidative Phosphorylation Genes in Patients With Alzheimer's Disease: Implications for Early Mitochondrial Dysfunction and Oxidative Damage
Mańczak, M., Park, B. S., Jung, Y., & Reddy, P. H. (2004) · NeuroMolecular Medicine · doi:10.1385/nmm:5:2:147 · Cited by 434
Altered Metabolism of the Amyloid β Precursor Protein Is Associated with Mitochondrial Dysfunction in Down's Syndrome
Busciglio, J., Pelsman, A., Wong, C., Pigino, G., Yuan, M., Mori, H., & Yankner, B. A. (2002) · Neuron · doi:10.1016/s0896-6273(02)00604-9 · Cited by 387
The role of metals in neurodegenerative processes: aluminum, manganese, and zinc
Zatta, P. F., Lucchini, R. G., van Rensburg, S. J., & Taylor, A. (2003) · Brain Research Bulletin · doi:10.1016/s0361-9230(03)00182-5 · Cited by 344
Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease
Gouras, G. K., Almeida, C. G., & Takahashi, R. H. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.05.022 · Cited by 338
Copper-Dependent Inhibition of Human Cytochrome c Oxidase by a Dimeric Conformer of Amyloid-β1-42
Crouch, P. J., Blake, R., Duce, J. A., Ciccotosto, G. D., Li, Q.-X., Barnham, K. J., Curtain, C. C., Cherny, R. A., Cappai, R., Dyrks, T., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4276-04.2005 · Cited by 327
The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70–Tim44
Dekker, P., Martin, F., Maarse, A. C., Bömer, U., Müller, H., Guiard, B., Meijer, M., Rassow, J., & Pfanner, N. (1997) · The EMBO Journal · doi:10.1093/emboj/16.17.5408 · Cited by 305
Are mitochondria critical in the pathogenesis of Alzheimer's disease?
Reddy, P. H., & Beal, M. F. (2005) · Brain Research Reviews · doi:10.1016/j.brainresrev.2005.03.004 · Cited by 294
Amyloid β-induced Changes in Nitric Oxide Production and Mitochondrial Activity Lead to Apoptosis
Keil, U., Bonert, A., Marques, C. A., Scherping, I., Weyermann, J., Strosznajder, J. B., Müller-Spahn, F., Haass, C., Czech, C., Pradier, L., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405600200 · Cited by 287
Brain aluminum in aging and Alzheimer disease
MCDERMOTT, J. R., Smith, A. I., Iqbal, K., & Wı́sniewski, H. M. (1979) · Neurology · doi:10.1212/wnl.29.6.809 · Cited by 263
Glutamatergic systems in Alzheimer's disease
Francis, P. T. (2003) · International Journal of Geriatric Psychiatry · doi:10.1002/gps.934 · Cited by 255
The βA4 amyloid precursor protein binding to copper
Hesse, L., Beher, D., Masters, C. L., & Multhaup, G. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00658-x · Cited by 247
Energy Hypometabolism in Posterior Cingulate Cortex of Alzheimer's Patients: Superficial Laminar Cytochrome Oxidase Associated with Disease Duration
Valla, J. E., Berndt, J. D., & Gonzalez-Lima, F. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-13-04923.2001 · Cited by 241
Increased regional brain concentrations of ceruloplasmin in neurodegenerative disorders
Loeffler, D. A., LeWitt, P. A., Juneau, P. L., Sima, A. A. F., Nguyen, H.-U., DeMaggio, A. J., Brickman, C. M., Brewer, G. J., Dick, R. D., Troyer, M. D., et al. (1996) · Brain Research · doi:10.1016/s0006-8993(96)00782-2 · Cited by 237
Metals and trace elements in plasma and cerebrospinal fluid in normal aging and Alzheimer's disease.
Basun, H., Forssell, L. G., Wetterberg, L., & Winblad, B. G. (1991) · PubMed · Cited by 228
Protein Kinase A-mediated Phosphorylation Modulates Cytochrome c Oxidase Function and Augments Hypoxia and Myocardial Ischemia-related Injury
Prabu, S. K., Anandatheerthavarada, H. K., Raza, H., Srinivasan, S., Spear, J. F., & Avadhani, N. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507741200 · Cited by 190
Single translation—dual destination: mechanisms of dual protein targeting in eukaryotes
Karniely, S., & Pines, O. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400394 · Cited by 172
Morphological Characterization of Thioflavin-S-Positive Amyloid Plaques in Transgenic Alzheimer Mice and Effect of Passive Aβ Immunotherapy on Their Clearance
Bussière, T., Bard, F., Barbour, R., Grajeda, H., Guido, T., Khan, K., Schenk, D., Games, D., Seubert, P. A., & Buttini, M. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63360-3 · Cited by 170
Molecular Genetics of Late‐Onset Alzheimer's Disease
Kamboh, M. I. (2004) · Annals of Human Genetics · doi:10.1046/j.1529-8817.2004.00110.x · Cited by 170
Differential involvement of protein kinase C isozymes in Alzheimer's disease
Masliah, E., Cole, G. M., Shimohama, S., Hansen, L. A., DeTeresa, R. M., Terry, R. D., & Saitoh, T. (1990) · Journal of Neuroscience · doi:10.1523/jneurosci.10-07-02113.1990 · Cited by 165
Shaping the mitochondrial proteome
Gabaldón, T., & Huynen, M. A. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.07.011 · Cited by 156
Presenilin function and γ‐secretase activity
Brunkan, A. L., & Goate, A. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03099.x · Cited by 149
Targeting of NH2-terminal–processed Microsomal Protein to Mitochondria: A Novel Pathway for the Biogenesis of Hepatic Mitochondrial P450MT2
Addya, S., Anandatheerthavarada, H. K., Biswas, G., Bhagwat, S. V., Mullick, J., & Avadhani, N. G. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.3.589 · Cited by 137
Dual targeting of cytochrome P4502B1 to endoplasmic reticulum and mitochondria involves a novel signal activation by cyclic AMP‐dependent phosphorylation at Ser128
Anandatheerthavarada, H. K., Biswas, G., Mullick, J., Sepuri, N. B. V., Otvos, L., Pain, D., & Avadhani, N. G. (1999) · The EMBO Journal · doi:10.1093/emboj/18.20.5494 · Cited by 132
Mitochondrial failures in Alzheimer's disease
Zhu, X., Smith, M. A., Perry, G. L., & Aliev, G. (2004) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/153331750401900611 · Cited by 125
Apolipoprotein E: a major piece in the Alzheimer's disease puzzle
Cedazo-Mı́nguez, Á., & Cowburn, R. F. (2001) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2001.tb00159.x · Cited by 123
Nitrogen disruption of synaptoneurosomes: an alternative method to isolate brain mitochondria
Brown, M. R., Sullivan, P. G., Dorenbos, K., Modafferi, E. F., Geddes, J. W., & Steward, O. (2004) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2004.02.028 · Cited by 114
Phosphorylation Enhances Mitochondrial Targeting of GSTA4-4 through Increased Affinity for Binding to Cytoplasmic Hsp70
Robin, M., Prabu, S. K., Raza, H., Anandatheerthavarada, H. K., & Avadhani, N. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301807200 · Cited by 107
The TIM17·23 preprotein translocase of mitochondria: composition and function in protein transport into the matrix
Moro, F., Sirrenberg, C., Schneider, H., Neupert, W., & Brunner, M. (1999) · The EMBO Journal · doi:10.1093/emboj/18.13.3667 · Cited by 103
Prostate Apoptosis Response‐4 Production in Synaptic Compartments Following Apoptotic and Excitotoxic Insults
Duan, W., Rangnekar, V. M., & Mattson, M. P. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0722312.x · Cited by 97
Alzheimers Disease: Interactions Between Cholinergic Functions and β- amyloid
Yan, Z., & Feng, J. (2004) · Current Alzheimer Research · doi:10.2174/1567205043331992 · Cited by 84
Cytochrome Oxidase Deficiency in Alzheimer's Diseasea
Parker, W. D. (1991) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1991.tb00191.x · Cited by 79
Apolipoprotein E Binding to Low Density Lipoprotein Receptor-related Protein-1 Inhibits Cell Migration via Activation of cAMP-dependent Protein Kinase A
Zhu, Y., & Hui, D. Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303171200 · Cited by 72
Familial Alzheimer's disease: Site of mutation influences clinical phenotype
Lippa, C. F., Swearer, J. M., Kane, K., Nochlin, D., Bird, T. D., Ghetti, B. F., Nee, L. E., George‐Hyslop, P. S., Pollen, D. A., & Drachman, D. A. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200009)48:3 · Cited by 67
Functional reconstitution of γ‐secretase through coordinated expression of presenilin, nicastrin, Aph‐1, and Pen‐2
Periz, G., & Fortini, M. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20203 · Cited by 65
Regional brain effects of sodium azide treatment on cytochrome oxidase activity: a quantitative histochemical study
Cada, A. M., Gonzalez-Lima, F., Rose, G. M., & Bennett, M. C. (1995) · Metabolic Brain Disease · doi:10.1007/bf02109361 · Cited by 58
Effects of apolipoprotein E (apoE) isoforms, β-amyloid (Aβ) and apoE/Aβ complexes on Protein Kinase C-α (PKC-α) translocation and amyloid precursor protein (APP) processing in human SH-SY5Y neuroblastoma cells and fibroblasts
Cedazo-Mı́nguez, A., Wiehager, B., Winblad, B., Hüttinger, M., & Cowburn, R. F. (2001) · Neurochemistry International · doi:10.1016/s0197-0186(00)00128-5 · Cited by 50
Effects of learning on cytochrome oxidase activity in cuttlefish brain
Agin, V., Chichery, R., & Chichery, M. (2001) · Neuroreport · doi:10.1097/00001756-200101220-00030 · Cited by 48
Energy metabolism, oxidative stress and neuronal degeneration in Alzheimer’s disease
Sims, N. R. (1996) · Neurodegeneration · doi:10.1006/neur.1996.0059 · Cited by 45 · cited 2×
“Mitochondrial dysfunction may play a role in the degeneration/cell death of neurons during the pathogenesis of AD (Sims, 1996; Zhu et al., 2004).”
Background
Effects of Chronic Sodium Azide on Brain and Muscle Cytochrome Oxidase Activity: A Potential Model to Investigate Environmental Contributions to Neurodegenerative Diseases
Berndt, J. D., Callaway, N. L., & Gonzalez-Lima, F. (2001) · Journal of Toxicology and Environmental Health · doi:10.1080/152873901750128380 · Cited by 41
Transport of proteins into mitochondria
Truscott, K. N., Pfanner, N., & Voos, W. (2007) · Springer eBooks · doi:10.1007/bfb0115593 · Cited by 41
The Human Brain in Dissection
Montemurro, D. G., & Bruni, J. (1981) · Medical Entomology and Zoology · Cited by 39
Tissue variant effects of heme inhibitors on the mouse cytochrome c oxidase gene expression and catalytic activity of the enzyme complex
Vijayasarathy, C., Damle, S., Lenka, N., & Avadhani, N. G. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00843.x · Cited by 38
Protein kinase C activity and protein levels in Alzheimer's disease.
Lanius, R. A., Wagey, R., Sahl, B., Beattie, B., Feldman, H., Pelech, S., & Krieger, C. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00422-8 · Cited by 19

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Research works printed but not linked: 2

Dasso M (1998) in Current protocols in cell biology, In vitro reconstitution, eds Bonifacino JS Dasso M Harford JB Lippincot-Schawartz J Yamada KM (Wiley, New York), pp 11.0.1–11.0.2.
Jagannatha Rao, 1999, Trace elements in the cerebrospinal fluid of Alzheimer’s disease, Alzheimers Rep, 2, 333

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Authors: Devi, L., Prabhu, B. M., Galati, D. F., Avadhani, N. G., & Anandatheerthavarada, H. K.
Affiliations: University of Pennsylvania (US)
ORCID: Galati, Domenico F.
Avadhani, Narayan G.
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 2006-08-30
Volume: 26
Issue: 35
Pages: 9057-9068
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.1469-06.2006
PMC: PMC6675337
OpenAlex: W2076241970
Cited by: 792
References: 62
Citations by year: 2026: 21 · 2025: 21 · 2024: 36 · 2023: 47 · 2022: 53 · 2021: 60 · 2020: 50 · 2019: 37 · 2018: 44 · 2017: 39 · 2016: 36 · 2015: 35 · 2014: 34 · 2013: 40 · 2012: 50
FWCI: 19.78
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-sa
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 182 d)
Locations: Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute on Aging (R01AG021920, AG 021920)
National Institute of General Medical Sciences (GM-49683, R01GM049683)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: amyloid precursor protein, Alzheimer's disease, mitochondrial dysfunction, Tom40, Tim23, cytochrome c oxidase, hydrogen peroxide, neuronal cell types
MeSH terms: Alzheimer Disease, Apolipoproteins E, Biological Transport, Brain, Cadaver, Electron Transport Complex IV, Glycosylation, Humans, Hydrogen Peroxide, Mitochondria, Neurons, Tissue Distribution, Case-Control Studies, Amyloid beta-Protein Precursor, Mitochondrial Proteins, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Apolipoprotein E3, Apolipoprotein E4

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Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction

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