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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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Self-citationJones, L. D., Jackson, J. W., & Maggirwar, S. B. (2016) · PLoS ONE · doi:10.1371/journal.pone.0151702 · Cited by 57
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Roberts, T. K. (2009) · Frontiers in bioscience · doi:10.2741/3631 · Cited by 56
Bertrand, L., Dygert, L., & Toborek, M. J. (2016) · Scientific Reports · doi:10.1038/srep39738 · Cited by 57
Persidsky, Y., Fan, S., Dykstra, H., Reichenbach, N. L., Rom, S., & Ramirez, S. H. (2015) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-015-9591-3 · Cited by 53
Self-citationPu, H., Hayashi, K., Andras, I. E., Eum, S. Y., Hennig, B., & Toborek, M. J. (2007) · Brain Research · doi:10.1016/j.brainres.2007.09.063 · Cited by 48
Salvador, E., Kessler, A. F., Domröse, D., Hörmann, J., Schaeffer, C. M., Giniunaite, A., Burek, M., Tempel-Brami, C., Voloshin, T., Volodin, A., et al. (2022) · Biomolecules · doi:10.3390/biom12101348 · Cited by 52
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Baumer, Y., Burger, S., CURRY, F. E., Golenhofen, N., Drenckhahn, D., & Waschke, J. (2007) · Histochemistry and Cell Biology · doi:10.1007/s00418-007-0358-7 · Cited by 42
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Sriram, U., Cenna, J. M., Haldar, B., Fernandes, N. C., Razmpour, R., Fan, S., Ramirez, S. H., & Potula, R. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.4a0814-395rr · Cited by 37
Wu, H., Jiang, X., Li, Y., Dong, Y., Zheng, J., Li, L., Li, Y., Wang, J., Lin, X., Zhang, X., et al. (2023) · Nano Today · doi:10.1016/j.nantod.2023.101800 · Cited by 37
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Günzel, D., & Fromm, M. (2012) · Comprehensive physiology · doi:10.1002/j.2040-4603.2012.tb00450.x · Cited by 37
Manda, V. K., Mittapalli, R. K., Geldenhuys, W. J., & Lockman, P. R. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06948.x · Cited by 36
Alvarez, J. I., & Teale, J. M. (2007) · Brain Research · doi:10.1016/j.brainres.2007.07.010 · Cited by 36
Leibrand, C. R., Paris, J. J., Jones, A. M., Masuda, Q. N., Halquist, M. S., Kim, W., Knapp, P. E., Kashuba, A. D. M., Hauser, K. F., & McRae, M. (2019) · Journal of NeuroVirology · doi:10.1007/s13365-019-00757-8 · Cited by 36
Selvakumar, K., Prabha, R. L., Saranya, K., Bavithra, S., Krishnamoorthy, G., & Arunakaran, J. (2012) · Human & Experimental Toxicology · doi:10.1177/0960327112464798 · Cited by 36
Coelho-Santos, V., Socodato, R., Portugal, C., Leitão, R. A., Rito, M., Barbosa, M., Couraud, P.-O., Romero, I. A., Weksler, B., Minshall, R. D., et al. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2301-3 · Cited by 36
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Dörfel, M. J., & Huber, O. (2012) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2012.06536.x · Cited by 34
Yan, B. C., Xu, P., Gao, M., Wang, J., Jiang, D., Zhu, X., Won, M., & Su, P. Q. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00775 · Cited by 34
Montagne, A., Huuskonen, M. T., Rajagopal, G., Sweeney, M. D., Nation, D. A., Sepehrband, F., D’Orazio, L. M., Harrington, M. G., Chui, H. C., Law, M., et al. (2019) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2019.07.012 · Cited by 33
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Wei, S., Li, Y., Polster, S. P., Weber, C. R., Awad, I. A., & Shen, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020675 · Cited by 32
Império, G. E., Lye, P., Bloise, E., & Matthews, S. G. (2021) · Tissue Barriers · doi:10.1080/21688370.2020.1860616 · Cited by 30
Lai, A. Y., & McLaurin, J. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14130 · Cited by 31
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Eum, S. Y., Andras, I. E., Couraud, P., Hennig, B., & Toborek, M. J. (2007) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2007.10.019 · Cited by 30
Louboutin, J., Reyes, B. A. S., Agrawal, L., Maxwell, C. R., Bockstaele, E. J. V., & Strayer, D. S. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.02.007 · Cited by 30
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Morofuji, Y., Nakagawa, S., So, G., Hiu, T., Horai, S., Hayashi, K., Tanaka, K., Suyama, K., Deli, M. A., Nagata, I., et al. (2010) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-010-9497-9 · Cited by 28
Liu, R., Collier, J. M., Abdul‐Rahman, N., Capuk, O., Zhang, Z., & Begum, G. (2024) · Aging and Disease · doi:10.14336/ad.2023.1201 · Cited by 31
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Matsuhisa, K., Kondoh, M., Takahashi, A., & Yagi, K. (2009) · Expert Opinion on Drug Delivery · doi:10.1517/17425240902902315 · Cited by 25
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Chen, L., Choi, J. J., Choi, Y. J., Hennig, B., & Toborek, M. J. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.06.004 · Cited by 20
Wang, Z., Li, Y., Cai, S., Li, R., & Cao, G. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.3834 · Cited by 19
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Ghouri, M. D., Saleem, J., Ren, J., Liu, J., Umer, A., Cai, R., & Chen, C. (2021) · Advanced Materials Interfaces · doi:10.1002/admi.202101391 · Cited by 16
Wang, T., Xu, Y., Zhu, H., Andrus, T., Ivanov, S. B., Pan, C., Dolores, J. S., Dann, G. C., Zhou, M., Forte, D. M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065071 · Cited by 14
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Burgener, A., Sainsbury, J., Plummer, F. A., & Ball, T. B. (2010) · Current HIV/AIDS Reports · doi:10.1007/s11904-010-0039-3 · Cited by 15
Kim, J. H., Hossain, F. M. A., Patil, A. M., Choi, J. Y., Kim, S. B., Uyangaa, E., Park, S., Lee, J. H., Kim, B., Kim, K., et al. (2016) · Comparative Immunology Microbiology and Infectious Diseases · doi:10.1016/j.cimid.2016.07.007 · Cited by 15
Rom, S., Gajghate, S., Winfield, M., Reichenbach, N. L., & Persidsky, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134663 · Cited by 15
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Iyengar, S., Zhan, C., Lu, J., Korngold, R., & Schwartz, D. H. (2014) · Transplantation and Cellular Therapy · doi:10.1016/j.bbmt.2014.04.029 · Cited by 15
Zhao, H., Zhang, Q., Xue, Y., Chen, X., & Haun, R. S. (2011) · Experimental Brain Research · doi:10.1007/s00221-011-2702-3 · Cited by 13
Annadurai, N., & Kanmogne, G. D. (2024) · Cells · doi:10.3390/cells13171415 · Cited by 12
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Bogatcheva, N. V., & Verin, A. D. (2009) · Microvascular Research · doi:10.1016/s0026-2862(09)00021-1 · Cited by 12
Bhide, K., Mochnáčová, E., Tkáčová, Z., Petroušková, P., Kulkarni, A. D., & Bhide, M. R. (2022) · Scientific Reports · doi:10.1038/s41598-022-13043-1 · Cited by 10
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Rada, C. C., Yuki, K., Ding, J., & Kuo, C. J. (2023) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a041191 · Cited by 4
Butz, S., & Vestweber, D. (2007) · Birkhäuser Basel eBooks · doi:10.1007/978-3-7643-7975-9_11 · Cited by 3
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Mahajan, S. D., Aalinkeel, R., Reynolds, J. L., Nair, B. B., Mammen, M. J., Dai, L., Prasad, P. N., & Schwartz, S. A. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801317-5.00015-3 · Cited by 2
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Sagar, V. (2013) · FIU - Digital Commons (Florida International University) · doi:10.25148/etd.fi13080525 · Cited by 2
Nimjee, S. M., Grant, G. A., Winn, H. R., & Janigro, D. (2011) · Elsevier eBooks · doi:10.1016/b978-1-4160-5316-3.00009-5 · Cited by 1
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Yan, H., & Huo, Z.-H. (2007) · Shengming kexue
Identifying the role of RGMc in an animal model of Multiple Sclerosis
Vigouroux, R. J. (2015) · TSpace (University of Toronto)
Salimi, H., Cain, M. D., Jiang, X., Roth, R. A., Beatty, W. L., Sun, C., Klimstra, W. B., Hou, J., & Klein, R. S. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/805945
Control of Neuroinflammation and Protecting the Integrity of the Blood-Brain Barrier
Rom, S., & Persidsky, Y. (2024) · Springer eBooks · doi:10.1007/978-3-031-68237-7_42
Self-citationSphingosine-1-phosphate (S1P) and its receptor S1PR2 in central nervous system diseases: a review
Hu, L., Wang, Z., Zhao, Z., Chen, Y., Ke, C., & Qiu, F. (2026) · Discover Neuroscience · doi:10.1186/s13064-026-00299-w
Pan, S., An, Z., Pan, Y., Li, G., He, H., wang, J., qu, J., Tang, C., & Liu, X. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.154077
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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