Cited by 383Barrier Structure and Function StudiesCell Adhesion Molecules ResearchCaveolin-1 and cellular processes

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Potential role of MCP-1 in endothelial cell tight junction `opening': signaling via Rho and Rho kinase

Stamatovic, Svetlana M., Keep, Richard F., Kunkel, Steven L., Andjelkovic, Anuska V.·2003·Journal of Cell Science

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Abstract

The expression of the monocyte chemoattractant protein-1 (MCP-1) receptor CCR2 by brain endothelial cells suggests that MCP-1 may have other functions than purely driving leukocyte migration into brain parenchyma during inflammation. This study examines one of these potential novel roles of MCP-1 regulation of endothelial permeability using primary cultures of mouse brain endothelial cells. MCP-1 induces reorganization of actin cytoskeleton (stress fiber formation) and redistribution of tight junction proteins, ZO-1, ZO-2 occludin and claudin-5, from the Triton X-100-soluble to the Triton X-100-insoluble fractions. These morphological changes are associated with a decrease in transendothelial electrical membrane resistance and an increase in [14C]inulin permeability. MCP-1 did not induce these events in brain endothelial cells prepared from mice genotype CCR2-/-. The Rho kinase inhibitor Y27632 and inhibition of Rho (C3 exoenzyme, and dominant negative mutant of Rho, RhoT19N) prevented MCP-1-induced stress fiber assembly, reorganization of tight junction proteins and alterations in endothelial permeability. In all, this suggests that a small GTPase Rho and Rho kinase have a pivotal role in MCP-1-induced junction disarrangement. These data are the first to strongly suggest that MCP-1, via CCR2 present on brain endothelial cells, contributes to increased brain endothelial permeability.

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Rho GTPases in cell biology
Etienne-Manneville, S., & Hall, A. (2002) · Nature · doi:10.1038/nature01148 · Cited by 4,965
Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase)
Kimura, K., Ito, M., Amano, M., Chihara, K., Fukata, Y., Nakafuku, M., Yamamori, B., Feng, J., Nakano, T., Okawa, K., et al. (1996) · Science · doi:10.1126/science.273.5272.245 · Cited by 2,889
Chemokines
Rollins, B. J. (1997) · Blood · doi:10.1182/blood.v90.3.909.909_909_928 · Cited by 2,126
Phosphorylation and Activation of Myosin by Rho-associated Kinase (Rho-kinase)
Amano, M., Ito, M., Kimura, K., Fukata, Y., Chihara, K., Nakano, T., Matsuura, Y., & Kaibuchi, K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20246 · Cited by 2,009
Decreased lesion formation in CCR2−/− mice reveals a role for chemokines in the initiation of atherosclerosis
Boring, L., Gosling, J., Cleary, M., & Charo, I. F. (1998) · Nature · doi:10.1038/29788 · Cited by 1,965
Junctional Adhesion Molecule, a Novel Member of the Immunoglobulin Superfamily That Distributes at Intercellular Junctions and Modulates Monocyte Transmigration
Martín-Padura, I., Lostaglio, S., Schneemann, M., Williams, L., Romano, M., Fruscella, P., Panzeri, C., Stoppacciaro, A., Ruco, L., Villa, A., et al. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.1.117 · Cited by 1,387
The Molecular Biology of Leukocyte Chemoattractant Receptors
Murphy, P. M. (1994) · Annual Review of Immunology · doi:10.1146/annurev.iy.12.040194.003113 · Cited by 1,197
THE 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
Signalling to and from tight junctions
Matter, K., & Balda, M. (2003) · Nature reviews. Molecular cell biology · doi:10.1038/nrm1055 · Cited by 926
Matrix Metalloproteinases and TIMPs Are Associated With Blood-Brain Barrier Opening After Reperfusion in Rat Brain
Rosenberg, G. A., Estrada, E. Y., & Dencoff, J. E. (1998) · Stroke · doi:10.1161/01.str.29.10.2189 · Cited by 861

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Rollins, B. J. (1997). Chemokines.Blood90, 909-928. · DOI
Wolburg, H. and Risau, W. (1995). Formation of the blood-brain barrier. In Neuroglia (ed. H. Kettenmann and B. R. Ransom), pp. 763-776. Oxford: Oxford University Press.

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Roberts, T. K., Eugenin, E. A., Lopez, L., Romero, I. A., Weksler, B. B., Couraud, P.-O., & Berman, J. W. (2012) · Laboratory Investigation · doi:10.1038/labinvest.2012.80 · Cited by 115
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Ivey, N., MacLean, A. G., & Lackner, A. A. (2009) · Journal of NeuroVirology · doi:10.1080/13550280902769764 · Cited by 118
Cytokines and Pathogenesis of Central Retinal Vein Occlusion
Noma, H., Yasuda, K., & Shimura, M. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9113457 · Cited by 112
Involvement of Cytokines in the Pathogenesis of Diabetic Macular Edema
Noma, H., Yasuda, K., & Shimura, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073427 · Cited by 115
Expression of Chemokines and Their Receptors by Human Brain Endothelium: Implications for Multiple Sclerosis
Subileau, E. A., Rezaie, P., Davies, H. A., Colyer, F. M., Greenwood, J., Male, D. K., & Romero, I. A. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318197eca7 · Cited by 111
Bradykinin increases blood–tumor barrier permeability by down‐regulating the expression levels of ZO‐1, occludin, and claudin‐5 and rearranging actin cytoskeleton
Liu, L., Xue, Y., Liu, Y., & Wang, Y. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21558 · Cited by 111
C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins
Vogelsgesang, M., Pautsch, A., & Aktories, K. (2006) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-006-0113-y · Cited by 111
Plasmin-Dependent Modulation of the Blood–Brain Barrier: A Major Consideration during tPA-Induced Thrombolysis?
Niego, B., & Medcalf, R. L. (2014) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2014.99 · Cited by 103
Dendritic cell CNS recruitment correlates with disease severity in EAE via CCL2 chemotaxis at the blood–brain barrier through paracellular transmigration and ERK activation
Sagar, D., Lamontagne, A., Foss, C. A., Khan, Z. K., Pomper, M. G., & Jain, P. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-245 · Cited by 106
Activation of Peroxisome Proliferator-Activated Receptor γ (PPARγ) Suppresses Rho GTPases in Human Brain Microvascular Endothelial Cells and Inhibits Adhesion and Transendothelial Migration of HIV-1 Infected Monocytes
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
Chemokine CCL2 and its receptor CCR2 are increased in the hippocampus following pilocarpine-induced status epilepticus
Foresti, M. L., Arisi, G. M., Katki, K. A., Montañez, A., Sanchez, R. M., & Shapiro, L. A. (2009) · Journal of Neuroinflammation · doi:10.1186/1742-2094-6-40 · Cited by 105
Control of Chemokine Gradients by the Retinal Pigment Epithelium
Shi, G., Maminishkis, A., Banzon, T., Jalickee, S., Li, R., Hammer, J., & Miller, S. S. (2008) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.08-1816 · Cited by 102
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The inflammatory response to silver and titanium dioxide nanoparticles in the central nervous system.
Wu, T.-S., & Tang, M. (2018) · Nanomedicine · doi:10.2217/nnm-2017-0270 · Cited by 90
Influence of silver and titanium dioxide nanoparticles on in vitro blood-brain barrier permeability
Chen, I.-C., Hsiao, I., Lin, H.-C., Wu, C., Chuang, C., & Huang, Y.-J. (2016) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2016.09.009 · Cited by 99
Dengue virus infection: current concepts in immune mechanisms and lessons from murine models
Guabiraba, R., & Ryffel, B. (2013) · Immunology · doi:10.1111/imm.12188 · Cited by 98
Brain Cytokines and Chemokines: Roles in Ischemic Injury and Pain
Minami, M., Katayama, T., & Satoh, M. (2006) · Journal of Pharmacological Sciences · doi:10.1254/jphs.crj06005x · Cited by 100
MK2 controls the level of negative feedback in the NF-κB pathway and is essential for vascular permeability and airway inflammation
Gorska, M. M., Liang, Q., Stafford, S. J., Goplen, N., Dharajiya, N. G., Guo, L., Sur, S. A., Gaestel, M., & Alam, R. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20062621 · Cited by 97
Baicalin reduces the permeability of the blood–brain barrier during hypoxia in vitro by increasing the expression of tight junction proteins in brain microvascular endothelial cells
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
Tight junctions contain oligomeric protein assembly critical for maintaining blood–brain barrier integrity in vivo
McCaffrey, G., Staatz, W. D., Quigley, C. A., Nametz, N., Seelbach, M. J., Campos, C. R., Brooks, T. A., Egleton, R. D., & Davis, T. P. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04943.x · Cited by 93
Mechanisms of macular edema
Haydinger, C. D., Ferreira, L. B., Williams, K. A., & Smith, J. R. (2023) · Frontiers in Medicine · doi:10.3389/fmed.2023.1128811 · Cited by 100
The CCL2‐CCR2 system affects the progression and clearance of intracerebral hemorrhage
Yao, Y., & Tsirka, S. E. (2012) · Glia · doi:10.1002/glia.22323 · Cited by 91
Cytokines and junction restructuring during spermatogenesis—a lesson to learn from the testis
Xia, W., Mruk, D. D., Lee, W. M., & Cheng, C. Y. (2005) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2005.05.007 · Cited by 90
Chemokine CCL2 contributes to BBB disruption via the p38 MAPK signaling pathway following acute intracerebral hemorrhage
Guo, F., Xu, D., Lin, Y., Wang, G., Wang, F., Gao, Q., Wei, Q., & Lei, S. (2019) · The FASEB Journal · doi:10.1096/fj.201902203rr · Cited by 91

Authors: Stamatovic, S. M., Keep, R. F., Kunkel, S. L., & Andjelkovic, A. V.
Affiliations: University of Michigan (US)
ORCID: Stamatovic, Svetlana M.
Keep, Richard F.
Kunkel, Steven L.
Andjelkovic, Anuska V.
Venue: Journal of Cell Science
Publisher: The Company of Biologists
Published: 2003-11-15
Volume: 116
Issue: 22
Pages: 4615-4628
ISSN: 0021-9533 (ISSN-L)
1477-9137
DOI: 10.1242/jcs.00755
OpenAlex: W1968099474
Cited by: 381
References: 119
Citations by year: 2026: 5 · 2025: 9 · 2024: 14 · 2023: 20 · 2022: 15 · 2021: 19 · 2020: 20 · 2019: 21 · 2018: 19 · 2017: 17 · 2016: 19 · 2015: 20 · 2014: 16 · 2013: 20 · 2012: 21
FWCI: 6.95
Type: journal article
Language: en
Open access: closed
Locations: Journal of Cell Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
Keywords: MCP-1, CCR2, brain endothelial cells, endothelial permeability, tight junctions, Rho kinase, Rho GTPases, actin cytoskeleton remodeling, stress fibers, ZO-1, occludin, claudin-5, transendothelial electrical resistance, leukocyte migration
MeSH terms: Acute-Phase Proteins, Animals, Brain, Cells, Cultured, Inulin, Membrane Proteins, Microscopy, Fluorescence, Mutation, Permeability, Electric Impedance, Protein Serine-Threonine Kinases, Octoxynol, Mice, Knockout, Chemokine CCL2, Tight Junctions, Receptors, Chemokine, Oligonucleotide Array Sequence Analysis, Stress Fibers, Endothelial Cells, Intracellular Signaling Peptides and Proteins, Mice, Receptors, CCR2, rho-Associated Kinases, Claudin-5, Occludin, Zonula Occludens-2 Protein

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Potential role of MCP-1 in endothelial cell tight junction `opening': signaling via Rho and Rho kinase

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