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Rho-mediated regulation of tight junctions during monocyte migration across the blood-brain barrier in HIV-1 encephalitis (HIVE)
Open accessAbstract
The blood-brain barrier (BBB) is compromised during progressive HIV-1 infection, but how this occurs is incompletely understood. We studied the integrity of tight junctions (TJs) of brain microvascular endothelial cells (BMVECs) in an in vitro BBB system and in human brain tissues with HIV-1 encephalitis (HIVE). A downregulation of TJ proteins, claudin-5 and occludin, paralleled monocyte migration into the brain during HIVE. Because small G proteins (such as Rho) can play a role in BMVEC TJ assembly, an artificial BBB system explored the relationship among TJs, Rho/Rho kinase (RhoK) activation, and transendothelial monocyte migration. Coculture of monocytes with endothelial cells led to Rho activation and phosphorylation of TJ proteins. Rho and RhoK inhibitors blocked migration of infected and uninfected monocytes. The RhoK inhibitor protected BBB integrity and reversed occludin/claudin-5 phosphorylation associated with monocyte migration. BMVEC transfection with a constitutively active mutant of RhoK led to dislocation of occludin from the membrane and loss of BMVEC cell contacts. When dominant-negative RhoK-transfected BMVECs were used in BBB constructs, monocyte migration was reduced by 84%. Thus, loss of TJ integrity was associated with Rho activation caused by monocyte brain migration, suggesting that Rho/RhoK activation in BMVECs could be an underlying cause of BBB impairment during HIVE.
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“Post mortem brain tissue studies in HAD or HIV encephalitis report microvascular degeneration and BBB breakdown including reduced pericyte coverage (439), reduced and disrupted TJs (471, 664), capillary basement membrane changes (471), perivascular macrophage infiltration (471), and reduced brain endothelial ABCB1 (P-gp) expression (346).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [471]
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Cites
Size-selective loosening of the blood-brain barrier in claudin-5–deficient mice
Nitta, T., Hata, M., Gotoh, S., Seo, Y., Sasaki, H., Hashimoto, N., Furuse, M., & Tsukita, S. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302070 · Cited by 1,917
Fanning, A. S., Jameson, B. J., Jesaitis, L. A., & Anderson, J. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.45.29745 · Cited by 1,432
Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase
Amano, M., Chihara, K., Kimura, K., Fukata, Y., Nakamura, N., Matsuura, Y., & Kaibuchi, K. (1997) · Science · doi:10.1126/science.275.5304.1308 · Cited by 1,077
Self-citationTHE CELL BIOLOGY OF THE BLOOD-BRAIN BARRIER
Rubin, L. L., & Staddon, J. M. (1999) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.22.1.11 · Cited by 1,017
Regulation of the Cytoskeleton and Cell Adhesion by the Rho Family GTPases in Mammalian Cells
Kaibuchi, K., Kuroda, S., & Amano, M. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.459 · Cited by 1,017
Self-citationMorita, K., Sasaki, H., Furuse, M., & Tsukita, S. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.1.185 · Cited by 867
Leukocyte–endothelial-cell interactions in leukocyte transmigration and the inflammatory response
Müller, W. A. (2003) · Trends in Immunology · doi:10.1016/s1471-4906(03)00117-0 · Cited by 824
Gendelman, H. E., Orenstein, J. M., Martin, M. A., Ferrua, C., Mitra, R., Phipps, T. J., Wahl, L. A., Lane, H. C., Fauci, A. S., & Burke, D. (1988) · The Journal of Experimental Medicine · doi:10.1084/jem.167.4.1428 · Cited by 781
Brain metabolism: a perspective from the blood-brain barrier
Pardridge, W. M. (1983) · Physiological Reviews · doi:10.1152/physrev.1983.63.4.1481 · Cited by 745
Yang, L., Froio, R. M., Sciuto, T. E., Dvořàk, A. M., Alon, R., & Luscinskas, F. W. (2005) · Blood · doi:10.1182/blood-2004-12-4942 · Cited by 735
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González-Mariscal, L., Tapia, R., & Chamorro, D. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.08.018 · Cited by 759
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Luissint, A.-C., Artus, C., Glacial, F., Ganeshamoorthy, K., & Couraud, P.-O. (2012) · Fluids and Barriers of the CNS · doi:10.1186/2045-8118-9-23 · Cited by 654
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Cardoso, F. L., Brites, D. M. T. O., & Brito, M. A. (2010) · Brain Research Reviews · doi:10.1016/j.brainresrev.2010.05.003 · Cited by 604
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Neuwelt, E., Abbott, N. J., Abrey, L., Banks, W. A., Blakley, B., Davis, T., Engelhardt, B., Grammas, P., Nedergaard, M., Nutt, J., et al. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(07)70326-5 · Cited by 474
Muneer, P. M. A., Chandra, N., & Haorah, J. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8752-3 · Cited by 476
Self-citationJunctional proteins of the blood-brain barrier: New insights into function and dysfunction
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Günzel, D., & Fromm, M. (2012) · Comprehensive physiology · doi:10.1002/cphy.c110045 · Cited by 401
Schreibelt, G., Kooij, G., Reijerkerk, A., van Doorn, R., Gringhuis, S. I., van der Pol, S., Weksler, B. B., Romero, I. A., Couraud, P., Piontek, J., et al. (2007) · The FASEB Journal · doi:10.1096/fj.07-8329com · Cited by 347
Haorah, J., Ramirez, S. H., Schall, K. A., Smith, D. L., Pandya, R., & Persidsky, Y. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04393.x · Cited by 334
Self-citationCong, X., & Kong, W. (2019) · Cellular Signalling · doi:10.1016/j.cellsig.2019.109485 · Cited by 312
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Chen, L., Yokel, R. A., Hennig, B., & Toborek, M. J. (2008) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-008-9131-5 · Cited by 300
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Jin, L., Li, J., Wang, K., Xia, W., Zhu, Z., Wang, C., Li, X., & Liu, H. (2020) · Journal of Neurotrauma · doi:10.1089/neu.2020.7413 · Cited by 301
Liu, W., Wang, Z., Zhang, L., Wei, X., & Li, L. (2012) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2012.00340.x · Cited by 258
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Wegmann, F., Petri, B., Khandoga, A. G., Moser, C., Khandoga, A., Volkery, S., Li, H., Nasdala, I., Brandau, O., Fässler, R., et al. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20060565 · Cited by 249
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Yamamoto, M., Ramirez, S. H., Sato, S., Kiyota, T., Cerny, R. L., Kaibuchi, K., Persidsky, Y., & Ikezu, T. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.070076 · Cited by 241
Self-citationRamirez, S. H., Haskó, J., Skuba, A., Fan, S., Dykstra, H., McCormick, R. C., Reichenbach, N. L., Krizbai, I. A., Mahadevan, A., Zhang, M., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.4628-11.2012 · Cited by 243
Self-citationDaniels, B. P., Holman, D. W., Cruz-Orengo, L., Jujjavarapu, H., Durrant, D. M., & Klein, R. S. (2014) · mBio · doi:10.1128/mbio.01476-14 · Cited by 235
Kanmogne, G. D., Schall, K. A., Leibhart, J., Knipe, B., Gendelman, H. E., & Persidsky, Y. (2006) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600330 · Cited by 230
Self-citationRamirez, S. H., Potula, R., Fan, S., Eidem, T. M., Papugani, A., Reichenbach, N. L., Dykstra, H., Weksler, B. B., Romero, I. A., Couraud, P. O., et al. (2009) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2009.112 · Cited by 212
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Stamatovic, S. M., Keep, R. F., Wang, M. M., Janković, I., & Andjelkovic, A. V. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.000521 · Cited by 203
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Chen, X., Lan, X., Roche, I., Liu, R., & Geiger, J. D. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05697.x · Cited by 189
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Dörfel, M. J., & Huber, O. (2012) · BioMed Research International · doi:10.1155/2012/807356 · Cited by 188
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Coisne, C., & Engelhardt, B. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3929 · Cited by 191
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Bogush, M., Heldt, N. A., & Persidsky, Y. (2017) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-017-9752-7 · Cited by 175
Self-citationThe role of claudin-5 in blood-brain barrier (BBB) and brain metastases (Review)
Jia, W., Lu, R., Martin, T. A., & Jiang, W. G. (2013) · Molecular Medicine Reports · doi:10.3892/mmr.2013.1875 · Cited by 159
The blood-retinal barrier: structure and functional significance
Runkle, E. A., & Antonetti, D. A. (2011) · Methods in Molecular Biology · doi:10.1007/978-1-60761-938-3_5 · Cited by 171
Molecular mechanisms of neuroinvasion by monocytes-macrophages in HIV-1 infection
Gras, G. S., & Kaul, M. (2010) · Retrovirology · doi:10.1186/1742-4690-7-30 · Cited by 150
Mahajan, S. D., Aalinkeel, R., Sykes, D. E., Reynolds, J. L., Bindukumar, B., Adal, A., Qi, M., Toh, J., Xu, G., Prasad, P. N., et al. (2008) · Brain Research · doi:10.1016/j.brainres.2008.01.093 · Cited by 139
Leech, S., Kirk, J., Plumb, J., & McQuaid, S. (2007) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2006.00781.x · Cited by 137
Sun, J., Huang, Y., Gong, J., Wang, J., Fan, Y., Cai, J., Wang, Y., Qiu, Y., Wei, Y., Xiong, C., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19042-y · Cited by 132
Merkel, S. F., Andrews, A. M., Lutton, E. M., Mu, D., Hudry, E., Hyman, B. T., Maguire, C. A., & Ramirez, S. H. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.13861 · Cited by 132
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Eugenín, E. A., & Berman, J. W. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4154-07.2007 · Cited by 130
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Banerjee, A., Zhang, X., Manda, K. R., Banks, W. A., & Nuran Ercal, A. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.02.023 · Cited by 122
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Ivey, N., MacLean, A. G., & Lackner, A. A. (2009) · Journal of NeuroVirology · doi:10.1080/13550280902769764 · Cited by 118
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Razzak, R. A., Florence, G. J., & Gunn‐Moore, F. J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20123108 · Cited by 118
Zhong, Y., Smart, E. J., Weksler, B. B., Couraud, P., Hennig, B., & Toborek, M. J. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0061-08.2008 · Cited by 111
Huang, W., Eum, S. Y., Andras, I. E., Hennig, B., & Toborek, M. J. (2009) · The FASEB Journal · doi:10.1096/fj.08-121624 · Cited by 109
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Worzfeld, T., & Schwaninger, M. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x15608644 · Cited by 104
Ramirez, S. H., Heilman, D., Morsey, B., Potula, R., Haorah, J., & Persidsky, Y. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.3.1854 · Cited by 105
Self-citationShen, W., Li, S., Chung, S. H., Zhu, L., Stayt, J., Su, T., Couraud, P., Romero, I. A., Weksler, B. B., & Gillies, M. C. (2010) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.10.013 · Cited by 113
Akiyama, T., Niyonsaba, F., Kiatsurayanon, C., Nguyen, T. T., Ushio, H., Fujimura, T., Ueno, T., Okumura, K., Ogawa, H., & Ikeda, S. (2014) · Journal of Innate Immunity · doi:10.1159/000362789 · Cited by 108
Manthari, R. K., Tikka, C., Ommati, M. M., Niu, R., Sun, Z., Wang, J., Zhang, J., & Wang, J. (2018) · Archives of Toxicology · doi:10.1007/s00204-018-2304-y · Cited by 100
Afonso, P. V., Ozden, S., Prévost, M., Schmitt, C., Seilhean, D., Weksler, B. B., Couraud, P., Antoine Gessain, A., Romero, I. A., & Ceccaldi, P. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.4.2576 · Cited by 97
Yamagami, K., Oka, T., Wang, Q., Ishizu, T., Lee, J., Miwa, K., Akazawa, H., Naito, A. T., Sakata, Y., & Komuro, I. (2015) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00137.2015 · Cited by 96
Zhu, H., Wang, Z., Xing, Y., Gao, Y., Ma, T., Lou, L., Lou, J., Gao, Y., Wang, S., & Wang, Y. (2011) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2011.08.063 · Cited by 94
Seelbach, M. J., Chen, L., Powell, A., Choi, Y. J., Zhang, B., Hennig, B., & Toborek, M. J. (2009) · Environmental Health Perspectives · doi:10.1289/ehp.0901334 · Cited by 94
Toborek, M. J., Seelbach, M. J., Rashid, C. S., Andras, I. E., Chen, L., Park, M., & Esser, K. A. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-22 · Cited by 91
Shi, H., Sheng, B., Zhang, F., Wu, C., Zhang, R., Zhu, J., Xu, K., Kuang, Y., Jameson, S. C., Lin, Z., et al. (2013) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00712.2012 · Cited by 91
Choi, Y. J., Seelbach, M. J., Pu, H., Eum, S. Y., Chen, L., Zhang, B., Hennig, B., & Toborek, M. J. (2010) · Environmental Health Perspectives · doi:10.1289/ehp.0901751 · Cited by 91
Gandhi, N. H., Saiyed, Z. M., Napuri, J., Samikkannu, T., Reddy, P. V. B., Agudelo, M., Khatavkar, P., Saxena, S. K., & Nair, M. (2010) · Journal of NeuroVirology · doi:10.3109/13550284.2010.499891 · Cited by 88
Muneer, P. M. A., Alikunju, S., Szlachetka, A. M., & Haorah, J. (2012) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.112.247668 · Cited by 87
Self-citationStamatovic, S. M., Sladojević, N., Keep, R. F., & Andjelkovic, A. V. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06678-11 · Cited by 88
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Hauser, K. F., El‐Hage, N., Stiene‐Martin, A., Maragos, W. F., Nath, A., Persidsky, Y., Volsky, D. J., & Knapp, P. E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04227.x · Cited by 86
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Doolittle‐Hall, J., & Gomez, S. M. (2010) · Virology Journal · doi:10.1186/1743-422x-7-82 · Cited by 85
Ramirez, S. H., Fan, S., Zhang, M., Papugani, A., Reichenbach, N. L., Dykstra, H., Mercer, A. J., Tuma, R. F., & Persidsky, Y. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090671 · Cited by 85
Self-citationBurgener, A., Boutilier, J., Wachihi, C., Kimani, J., Carpenter, M. S., Westmacott, G., Cheng, K., Ball, T. B., & Plummer, F. A. (2008) · Journal of Proteome Research · doi:10.1021/pr800406r · Cited by 82
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Scalise, A. A., Kakogiannos, N., Zanardi, F., Iannelli, F., & Giannotta, M. (2021) · Tissue Barriers · doi:10.1080/21688370.2021.1926190 · Cited by 86
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Paul, D., Cowan, A. E., Ge, S., & Pachter, J. S. (2012) · Microvascular Research · doi:10.1016/j.mvr.2012.12.001 · Cited by 77
Zhong, Y., Zhang, B., Eum, S. Y., & Toborek, M. J. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.4266-11.2012 · Cited by 79
Chupel, M. U., Minuzzi, L. G., Furtado, G. E., Santos, M. L. A. S., Hogervorst, E., Filaire, E., & Teixeira, A. M. (2018) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2017-0775 · Cited by 78
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Wu, F., Liu, L., & Zhou, H. Y. (2017) · Journal of Leukocyte Biology · doi:10.1189/jlb.3ru0816-352rr · Cited by 83
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Heldt, N. A., Seliga, A., Winfield, M., Gajghate, S., Reichenbach, N. L., Yu, X., Rom, S., Tenneti, A., May, D., Gregory, B. D., et al. (2020) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2020.03.034 · Cited by 77
Self-citationSun, N., Hu, H., Wang, F., Li, L., Zhu, W., Shen, Y., Xiu, J., & Xu, Q. (2021) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2020.11.032 · Cited by 75
Mishra, R., & Singh, S. K. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.4796-12.2013 · Cited by 74
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McCaffrey, G., Seelbach, M. J., Staatz, W. D., Nametz, N., Quigley, C., Campos, C. R., Brooks, T. A., & Davis, T. P. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05582.x · Cited by 71
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Self-citation
Metadata
- Authors
- Persidsky, Y., Heilman, D., Haorah, J., Zelivyanskaya, M., Persidsky, R., Weber, G. A., Shimokawa, H., Kaibuchi, K., & Ikezu, T.
- Affiliations
- University of Nebraska Medical Center (US)
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2006-06-15
- Volume
- 107
- Issue
- 12
- Pages
- 4770-4780
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- PMC
- PMC1895810
- OpenAlex
- W2094716188
- Cited by
- 200
- References
- 74
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 7 · 2023: 6 · 2022: 4 · 2021: 7 · 2020: 11 · 2019: 6 · 2018: 10 · 2017: 6 · 2016: 13 · 2015: 13 · 2014: 11 · 2013: 8 · 2012: 17
- FWCI
- 10.30
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Blood (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University of Arizona
- National Institute on Alcohol Abuse and Alcoholism (R37AA015913, R01AA015913)
- National Institute of Mental Health (R01MH072539, R01MH065151, R01-MH65151)
- National Institute of Neurological Disorders and Stroke (P01NS043985)
- Topics
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- HIV-1 encephalitis, blood-brain barrier, tight junctions, Rho kinase, Rho activation, monocyte migration, brain microvascular endothelial cells, claudin-5, occludin, blood-brain barrier integrity
- MeSH terms
- Blood-Brain Barrier, Cell Movement, Cells, Cultured, Enzyme Activation, Humans, Membrane Proteins, Monocytes, Mutation, Transfection, HIV-1, Down-Regulation, HIV Infections, Encephalitis, Viral, Tight Junctions, Protein Transport, Protein Kinase Inhibitors, G-Protein-Coupled Receptor Kinase 1, Claudin-5, Occludin
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