The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Matrix Metalloproteinase-Mediated Disruption of Tight Junction Proteins in Cerebral Vessels is Reversed by Synthetic Matrix Metalloproteinase Inhibitor in Focal Ischemia in Rat
Abstract
Matrix metalloproteinases (MMPs) disrupt the blood-brain barrier (BBB) during reperfusion. Occludin and claudins are recently described tight junction proteins (TJPs) that form the BBB. We hypothesized that the opening of the BBB was because of the degradation of TJPs by the MMPs. Spontaneously hypertensive rats had a 90 mins middle cerebral artery occlusion with reperfusion for 2, 3, or 24 h. Matrix metalloproteinases were measured by immunohistochemistry and in situ and gel zymography. Real-time polymerase chain reaction (PCR) measured mRNAs of MMP-2 and -9, furin, membrane-type MMP (MT1-MMP), occludin, and claudin-5. There was opening of the BBB in the piriform cortex after 3 h of reperfusion, and an MMP inhibitor, BB-1101 (30 mg/kg), prevented the opening. At 3 h, in situ zymograms showed gelatinase activity. Zymography and PCR showed greater increases in MMP-2 than in MMP-9. There were increased mRNA and immunohistochemistry for MT1-MMP and furin, which activate MMP-2. Claudin-5 and occludin mRNA expression decreased at 2 h in both hemispheres with fragments of both proteins seen on Western blot by 3 h on the ischemic side; treatment with BB-1101 reversed the degradation of the TJPs. Immunohistochemistry at 3 h showed fragmented TJPs within the endothelial cell clefts. By 24 h, in situ zymography showed gelatinase activity and gel zymography showed elevated levels of MMP-9. Disrupted TJPs previously seen in endothelial cells appeared in the surrounding astrocytes. Our results provide direct evidence that MMPs open the BBB by degrading TJPs and that an MMP inhibitor prevents degradation of the TJPs by MMPs.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Thus, the complex signaling pathway is constituted by the sequence of selectins, chemokines and integrins at the interface blood/CNS, resulting in emperipolesis through matrix metalloproteinases type 9 (MMP9) activation and tight-junctions disruption [74,75].”
From GANAB and N-Glycans Substrates Are Relevant in Human Physiology, Polycystic Pathology and Multiple Sclerosis: A Review (2022) · cites this paper as [74]
Citations
Cites
The blood-brain barrier/neurovascular unit in health and disease
Hawkins, B. T., & Davis, T. P. (2005) · Pharmacological Reviews · doi:10.1124/pr.57.2.4 · Cited by 2,661
Occludin: a novel integral membrane protein localizing at tight junctions.
Furuse, M., Hirase, T., Itoh, M., Nagafuchi, A., Yonemura, S., Tsukita, S., & Tsukita, S. (1993) · The Journal of cell biology · doi:10.1083/jcb.123.6.1777 · Cited by 2,580
Multifunctional strands in tight junctions
Tsukita, S., Furuse, M., & Itoh, M. (2001) · Nature reviews. Molecular cell biology · doi:10.1038/35067088 · Cited by 2,578
The blood–brain barrier: an overview
Ballabh, P., Braun, A., & Nedergaard, M. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.12.016 · Cited by 2,276
Furuse, M., Fujita, K., Hiiragi, T., Fujimoto, K., & Tsukita, S. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.7.1539 · Cited by 2,100
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
Mechanisms, challenges and opportunities in stroke
Lo, E. H., Dalkara, T., & Moskowitz, M. A. (2003) · Nature reviews. Neuroscience · doi:10.1038/nrn1106 · Cited by 1,808
Mechanism Of Cell Surface Activation Of 72-kDa Type IV Collagenase
Strongin, A. Y., Collier, I. E., Bannikov, G. A., Marmer, B. L., Grant, G. A., & Goldberg, G. I. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5331 · Cited by 1,589
Endothelial Cell-to-Cell Junctions: Molecular Organization and Role in Vascular Homeostasis
Bazzoni, G., & Dejana, E. (2004) · Physiological Reviews · doi:10.1152/physrev.00035.2003 · Cited by 1,384
Morita, K., Furuse, M., Fujimoto, K., & Tsukita, S. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.2.511 · Cited by 1,126
Flagged first, then by citations
Cited by
Sorted by citations
Items 601–700 of 1,000
Li, S., Li, G., Luo, X., Huang, Y. Q., Wen, L., & Li, J. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.736309 · Cited by 27
Zhao, Z., Huang, G.-Z., Wang, B., & Zhong, Y. (2012) · Behavioural Brain Research · doi:10.1016/j.bbr.2012.10.018 · Cited by 27
Li, X., Luo, D., Hou, Y., Hou, Y., Chen, S., Zhan, J., Luan, J., Wang, L., & Lin, D. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/3949575 · Cited by 27
Al-Ahmad, A. J., Pervaiz, I., & Karamyan, V. T. (2021) · Journal of Neuroendocrinology · doi:10.1111/jne.12931 · Cited by 27
Modulation of Tight Junction Proteins in the Perineurium to Facilitate Peripheral Opioid Analgesia
Rittner, H. L., Amasheh, S., Moshourab, R. A., Hackel, D., Yamdeu, R.-S., Mousa, S. A., Fromm, M., Stein, C., & Brack, A. (2012) · Anesthesiology · doi:10.1097/aln.0b013e318256eeeb · Cited by 27
Hemostasis and Alterations of the Central Nervous System
del Zoppo, G. D., Izawa, Y., & Hawkins, B. (2013) · Seminars in Thrombosis and Hemostasis · doi:10.1055/s-0033-1357490 · Cited by 24
Reuter, B., Rodemer, C., Grudzenski, S., Couraud, P., Weksler, B. B., Romero, I. A., Meairs, S. P., Bugert, P., Hennerici, M. G., & Fatar, M. (2013) · Cerebrovascular Diseases · doi:10.1159/000350731 · Cited by 27
Blood brain barrier breakdown was found in non-infarcted area after 2-h MCAO
Wang, X., Liu, Y., Sun, Y., Liu, W., & Jin, X. (2016) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2016.02.035 · Cited by 27
Self-citationYoshida, Y., Takagi, T., Kuramoto, Y., Tatebayashi, K., Shirakawa, M., Yamahara, K., Doe, N., & Yoshimura, S. (2021) · Cell Transplantation · doi:10.1177/09636897211024183 · Cited by 27
Frontczak‐Baniewicz, M., Chrapusta, S. J., & Sulejczak, D. (2011) · PubMed · Cited by 27
Activation of sulfonate ester based matrix metalloproteinase proinhibitors by hydrogen peroxide
Daniel, K. B., Jourden, J. L. M., Negoescu, K. E., & Cohen, S. M. (2010) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-010-0727-x · Cited by 28
Rosenberg, G. A. (2016) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0277-4 · Cited by 27
Self-citationWang, J., Zhang, Y., Xia, J., Cai, T., Du, J., Chen, J., Li, P., Shen, Y., Zhang, A., Fu, B., et al. (2018) · Journal of the American Heart Association · doi:10.1161/jaha.117.007197 · Cited by 26
Pharmacological therapy to cerebral ischemia-reperfusion injury: Focus on saponins
Zeng, M., Zhang, R., Yang, Q., Guo, L., Zhang, X., Yu, B., Gan, J., Yang, Z., Li, H., Wang, Y., et al. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113696 · Cited by 26
Role of microbial dysbiosis in the pathogenesis of Alzheimer's disease
Susmitha, G., & Kumar, R. K. (2023) · Neuropharmacology · doi:10.1016/j.neuropharm.2023.109478 · Cited by 27
Low-intensity open-field blast exposure effects on neurovascular unit ultrastructure in mice
Li, C., Chen, S., Siedhoff, H. R., Grant, D. G., Liu, P., Balderrama, A., Jackson, M. A., Zuckerman, A., Greenlief, C. M., Kobeissy, F. H., et al. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01636-4 · Cited by 27
Hasan, G. M., Anwar, S., Shamsi, A., Sohal, S. S., & Hassan, M. I. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1330098 · Cited by 26
Silva, T. M., Chaar, L. J. E., Silva, R. C., Takakura, A. C. T., Câmara, N. O. S., Antunes, V. R., & Moreira, T. S. (2018) · Experimental Physiology · doi:10.1113/ep086780 · Cited by 26
Targeting Water in the Brain: Role of Aquaporin-4 in Ischemic Brain Edema
Mamtilahun, M., Tang, G., Zhang, Z., Wang, Y., Tang, Y., & Yang, G. (2019) · Current Drug Targets · doi:10.2174/1389450120666190214115309 · Cited by 26
Evran, Ş., Çalış, F., Akkaya, E., Baran, O., Çevik, S., Katar, S., Gürevin, E. G., Hanımoğlu, H., Hatiboğlu, M. A., Armutak, E. İ., et al. (2019) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2019.10.013 · Cited by 26
Ma, T., Zhou, Y., Xia, Y., Meng, X., Jin, H., Wang, B., Chen, Y., Qiu, J., Wu, J., Ding, J., et al. (2020) · Environmental Science & Technology · doi:10.1021/acs.est.0c01701 · Cited by 26
Fu, Z., Chen, Y., Qin, F., Yang, S., Deng, X., Ding, R., Feng, L., Li, W., & Zhu, J. (2014) · Europe PMC (PubMed Central) · Cited by 26
Nanomaterial-Based Drug Delivery Systems for Ischemic Stroke
Jiang, C., Zhou, Y., Chen, R., Yang, M., Zhou, H., Tang, Z., Shi, H., & Qin, D. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15122669 · Cited by 25
Yamashita, T., Kamiya, T., Deguchi, K., Inaba, T., Zhang, H., Shang, J., Miyazaki, K., Ohtsuka, A., Katayama, Y., & Abe, K. (2010) · Okayama Igakkai Zasshi (Journal of Okayama Medical Association) · doi:10.4044/joma.122.195 · Cited by 25
Chen, T., Wang, W., Li, J., Xu, H., Peng, Y., Fan, L., Yan, F., Gu, C., Wang, L., & Chen, G. (2016) · Brain Research · doi:10.1016/j.brainres.2016.05.005 · Cited by 25
Xia, Z.-Y., Luo, C., Liu, B., Bian, X.-Q., Yang, L., Pang, A. M., Xu, Y., Tan, H.-M., & Zhao, Y. (2019) · Phytomedicine · doi:10.1016/j.phymed.2019.153158 · Cited by 26
Xu, L., Qu, C., Qu, C., Shen, J., Song, H., Li, Y., Li, T., Zheng, J., & Zhang, J. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2020.135437 · Cited by 25
Mamtilahun, M., Wei, Z., Qin, C., Wang, Y., Tang, Y., Shen, F., Tian, H., Zhang, Z., & Yang, G. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.610714 · Cited by 25
Blood–Brain Barrier Mechanisms in Stroke and Trauma
Li, W., Cao, F., Takase, H., Arai, K., Lo, E. H., & Lok, J. M. (2020) · Handbook of experimental pharmacology · doi:10.1007/164_2020_426 · Cited by 26
Xu, H., Cai, Y., Yu, M., Sun, J., Cai, J., Li, J., Qin, B., Ying, G., Chen, T., Shen, Y.-F., et al. (2021) · Aging · doi:10.18632/aging.203221 · Cited by 25
Small Vessel Disease: Ancient Description, Novel Biomarkers
Moretti, R., & Caruso, P. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073508 · Cited by 25
Marine Natural Products from the Russian Pacific as Sources of Drugs for Neurodegenerative Diseases
Khotimchenko, Y. S., Silachev, D. N., & Katanaev, V. L. (2022) · Marine Drugs · doi:10.3390/md20110708 · Cited by 25
El-Baz, F. K., Salama, A., Ali, S. I., & Elgohary, R. (2022) · Scientific Reports · doi:10.1038/s41598-022-25252-9 · Cited by 25
Accumulation of macromolecules in brain parenchyma in acute phase of cerebral infarction/reperfusion
Ishii, T., Asai, T., Urakami, T., & Oku, N. (2010) · Brain Research · doi:10.1016/j.brainres.2010.01.039 · Cited by 25
A close look at brain dynamics: Cells and vessels seen by in vivo two-photon microscopy
Fumagalli, S., Ortolano, F., & Simoni, M. G. D. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2014.06.005 · Cited by 27
Edvinsson, L. I., & Povlsen, G. K. (2010) · Acta Physiologica · doi:10.1111/j.1748-1716.2010.02227.x · Cited by 25
Establishment and evaluation of an experimental animal model of high altitude cerebral edema
Guo, P., Luo, H., Fan, Y., Luo, Y., & Zhou, Q. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.05.008 · Cited by 25
Matrix metalloproteinases and small artery remodeling
Martinez‐Lemus, L. A., & Galiñanes, E. L. (2011) · Drug Discovery Today Disease Models · doi:10.1016/j.ddmod.2011.06.002 · Cited by 25
Debrah, L. B., Albers, A., Debrah, A. Y., Brockschmidt, F. F., Becker, T., Herold, C., Hofmann, A., Osei-Mensah, J., Mubarik, Y., Fröhlich, H., et al. (2017) · Human Genomics · doi:10.1186/s40246-017-0121-7 · Cited by 25
Wu, T., Jia, Z., Dong, S., Han, B., Zhang, R., Liang, Y., Zhang, S., & Sun, J. (2019) · Journal of Vascular Research · doi:10.1159/000494935 · Cited by 25
Zhao, H., Zheng, T., Yang, X., Fan, M., Zhu, L., Liu, S., Wu, L., & Sun, C. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00381 · Cited by 26
Broekaart, D. W. M., van Scheppingen, J., Anink, J. J., Wierts, L., Hof, B. V. H., Jansen, F. E., Spliet, W. G. M., van Rijen, P. C., Kamphuis, W. W., de Vries, H. E., et al. (2019) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12572 · Cited by 25
Bennett, M., Chin, A., Lee, H. J., Cestero, E. M., Strazielle, N., Ghersi‐Egea, J., Threlkeld, S. W., Schmidt, T. A., Richendrfer, H. A., Szmydynger‐Chodobska, J., et al. (2020) · Journal of Neurotrauma · doi:10.1089/neu.2020.7229 · Cited by 25
Blood-brain barrier disruption in the striatum of rats treated with 3-nitropropionic acid
Duran‐Vilaregut, J., del Valle, J., Camins, A., Pallàs, M., Pelegrí, C., & Vilaplana, J. (2008) · NeuroToxicology · doi:10.1016/j.neuro.2008.10.007 · Cited by 27
Microfluidic models of the neurovascular unit: a translational view
Wevers, N. R., & de Vries, H. E. (2023) · Fluids and Barriers of the CNS · doi:10.1186/s12987-023-00490-9 · Cited by 25
Dhapola, R., Medhi, B., & HariKrishnaReddy, D. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09597-0 · Cited by 24
Blom, C., Deller, B., Fraser, D. D., Patterson, E. K., Martin, C. M., Young, G. B., Liaw, P. C., Yazdan-Ashoori, P., Ortiz, A., Webb, B., et al. (2015) · Critical Care · doi:10.1186/s13054-015-0883-z · Cited by 24
Zhai, L., Liu, M., Wang, T., Zhang, H., Li, S., & Guo, Y. (2017) · PLoS ONE · doi:10.1371/journal.pone.0174414 · Cited by 24
Qu, C., Xu, L., Shen, J., Li, Y., Qu, C., Song, H., & Zhang, J. (2019) · Behavioural Brain Research · doi:10.1016/j.bbr.2019.112385 · Cited by 25
Fujishima, M. C., Yazdanpanah, A., Horne, S., Lamont, A., Lopez, P. G., Zuend, C. F., Birse, K., Taverner, M. K., Greenslade, R., Abou, M., et al. (2023) · Mucosal Immunology · doi:10.1016/j.mucimm.2023.04.001 · Cited by 25
Association of Plasma Claudin-5 with Age and Alzheimer Disease
Tachibana, K., Hirayama, R., Sato, N., Hattori, K., Kato, T., Takeda, H., & Kondoh, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031419 · Cited by 23
Dohi, K., Satoh, K., Miyamoto, K., Momma, S., Fukuda, K., Higuchi, R., Ohtaki, H., & Banks, W. A. (2017) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.16-87 · Cited by 23
Herrera, E. A., & González‐Candia, A. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.717550 · Cited by 23
Wang, X., Yu, Z., Dong, F., Li, J., Niu, P., Ta, Q., Kan, J., Ma, C., Han, M., Yu, J., et al. (2023) · Molecular Diversity · doi:10.1007/s11030-023-10607-9 · Cited by 23
Carvacrol decreases blood–brain barrier permeability post-diffuse traumatic brain injury in rats
Abbasloo, E., Khaksari, M., Sanjari, M., Kobeissy, F. H., & Thomas, T. C. (2023) · Scientific Reports · doi:10.1038/s41598-023-40915-x · Cited by 23
Blood-brain barrier biomarkers
Zapata-Acevedo, J. F., Mantilla-Galindo, A., Vargas-Sánchez, K., & González-Reyes, R. E. (2024) · Advances in clinical chemistry · doi:10.1016/bs.acc.2024.04.004 · Cited by 23
Wang, Q., Ishikawa, T., Michiue, T., Zhu, B.-L., Guan, D.-W., & Maeda, H. (2013) · International Journal of Legal Medicine · doi:10.1007/s00414-013-0868-x · Cited by 26
Genome response to tissue plasminogen activator in experimental ischemic stroke
Jickling, G. C., Zhan, X., Ander, B. P., Turner, R. J., Stamova, B. S., Xu, H., Tian, Y., Liu, D., Davis, R. R., Lapchak, P. A., et al. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-254 · Cited by 23
New hypothesis for insulin resistance in hypertension due to receptor cleavage
DeLano, F. A., Zhang, H., Tran, E. D., Zhang, C., & Schmid‐Schönbein, G. W. (2010) · Expert Review of Endocrinology & Metabolism · doi:10.1586/eem.09.64 · Cited by 23
Du, Y., Xu, J.-T., Jin, H., Zhao, R., Zhao, D. H., Du, S., Xue, Y., Xie, X., & Wang, Q. (2017) · Scientific Reports · doi:10.1038/s41598-017-01923-w · Cited by 23
Amtul, Z., Hill, D. J., Arany, E. J., & Cechetto, D. F. (2018) · Scientific Reports · doi:10.1038/s41598-018-22985-4 · Cited by 23
Limb remote ischemic postconditioning protects integrity of the blood-brain barrier after stroke
Qi, C., Zhang, X., Li, J., Hu, X.-S., Zhou, F., Li, S., Lin, Y.-S., & Qi, W.-Q. (2018) · Neural Regeneration Research · doi:10.4103/1673-5374.237122 · Cited by 23
Muri, L., Perny, M., Zemp, J., Grandgirard, D., & Leib, S. L. (2019) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00220-19 · Cited by 23
Thompson, D., Sorenson, J., Greenmyer, J. R., Brissette, C. A., & Watt, J. A. (2020) · PLoS ONE · doi:10.1371/journal.pone.0234993 · Cited by 24
Huang, Q., Wang, X., Lin, X., Zhang, J., You, X., & Shao, A. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110647 · Cited by 23
Chelluboina, B., Nalamolu, K. R., Mendez, G. G., Klopfenstein, J. D., Pinson, D. M., Wang, D. Z., & Veeravalli, K. K. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000485533 · Cited by 23
MMP-12 knockdown prevents secondary brain damage after ischemic stroke in mice
Arruri, V. K., Chokkalla, A. K., Jeong, S., Chelluboina, B., Mehta, S. L., Veeravalli, K. K., & Vemuganti, R. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105432 · Cited by 23
Is there a role for herpes simplex virus type 1 in multiple sclerosis?
Duarte, L. F., Gatica, S., Castillo, A., Kalergis, A. M., Bueno, S. M., Riedel, C. A., & González, P. A. (2022) · Microbes and Infection · doi:10.1016/j.micinf.2022.105084 · Cited by 24
Optogenetic Activation of Astrocytes Reduces Blood-Brain Barrier Disruption via IL-10 In Stroke
Suo, Q., Deng, L., Chen, T., Wu, S., Qi, L., Liu, Z., He, T., Tian, H.-L., Li, W., Tang, Y., et al. (2023) · Aging and Disease · doi:10.14336/ad.2023.0226 · Cited by 23
Fattakhov, N. S., Ngo, A., Torices, S., Joseph, J.-A., Okoro, A., Moore, C., Naranjo, O., Becker, S., & Toborek, M. J. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00600.2023 · Cited by 22
Research progress and challenges of stem cell therapy for ischemic stroke
Cha, Z., Qiao, Y., Lu, Q., Wang, Q., Lu, X., Zhou, H., & Li, T. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1410732 · Cited by 22
Baş, D. F., Topçuoğlu, M. A., Özdemir, Y., Saatçi, I., Bodur, E., & Dalkara, T. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07952.x · Cited by 23
Huang, W., Rha, G. B., Chen, L., Seelbach, M. J., Zhang, B., Andras, I. E., Bruemmer, D., Hennig, B., & Toborek, M. J. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01126.2009 · Cited by 23
Dekker, S. E., Nikolian, V. C., Sillesen, M., Bambakidis, T., Schober, P. R., & Alam, H. B. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24125 · Cited by 22
Peripheral Nerve Injury Induces Dynamic Changes of Tight Junction Components
Wang, X., Miao, Y., Ni, J., Wang, Y., Qian, T., Yu, J. J., Liu, Q., Wang, P., & Yi, S. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01519 · Cited by 22
Potential Tear Biomarkers for the Diagnosis of Parkinson’s Disease—A Pilot Study
Acera, A., Gómez‐Esteban, J. C., Murueta‐Goyena, A., Galdós, M., Azkargorta, M., Elortza, F., Ruzafa, N., Ibarrondo, O., Pereiro, X., & Vecino, E. (2022) · Proteomes · doi:10.3390/proteomes10010004 · Cited by 25
Modulation of tight junction proteins in the perineurium for regional pain control
Hackel, D., Brack, A., Fromm, M., & Rittner, H. L. (2012) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2012.06499.x · Cited by 22
Setz, C., Brand, Y., Radojevic, V., Hanusek, C., Mullen, P. J., Levano, S., Listyo, A., & Bodmer, D. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.02.043 · Cited by 22
Zhu, J.-C., Si, M., Li, Y., Chen, H., Fan, Z., Xie, Q., & Jiao, X. (2016) · Hematological Oncology · doi:10.1002/hon.2289 · Cited by 22
Meprin β: A novel regulator of blood–brain barrier integrity
Gindorf, M., Storck, S. E., Ohler, A., Scharfenberg, F., Becker-Pauly, C., & Pietrzik, C. U. (2021) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x20905206 · Cited by 21
Role of hydrogen sulfide in subarachnoid hemorrhage
Lu, D., Wang, L., Liu, G., Wang, S., Wang, Y. N., Wu, Y. H., Wang, J., & Sun, X. (2022) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13828 · Cited by 21
Alzheimer’s disease is an inherent, natural part of human brain aging: an integrated perspective
Ferrer, I. (2022) · Free Neuropathology · doi:10.17879/freeneuropathology-2022-3806 · Cited by 25
Metalloproteinases and neurodegenerative diseases: pathophysiological and therapeutic perspectives
Rosenberg, G. A. (2015) · Metalloproteinases In Medicine · doi:10.2147/mnm.s68849 · Cited by 21
Self-citationTraweger, A., Toepfer, S., Wagner, R. N., Zweimueller-Mayer, J., Gehwolf, R., Lehner, C., Tempfer, H., Krizbai, I. A., Wilhelm, I., Bauer, H., et al. (2013) · Tissue Barriers · doi:10.4161/tisb.25039 · Cited by 21
Pelz, J. O., Härtig, W., Weise, C. M., Hobohm, C., Schneider, D., Krueger, M., Kacza, J., & Michalski, D. (2013) · European Journal of Histochemistry · doi:10.4081/ejh.2013.e38 · Cited by 21
Bonaventura, A., Montecucco, F., & Dallegri, F. (2016) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2016.1227779 · Cited by 22
Li, H., Li, Y., Chen, Z., Zhang, X., Zheng, X.-W., Yang, W.-T., Chen, S., & Zheng, G. (2016) · Neural Plasticity · doi:10.1155/2016/7308261 · Cited by 21
Lee, J. M., Baek, S., Kim, T.-W., Park, H.-S., Park, S.-S., Park, J., Kim, Y., Lee, H.-S., & Shin, M. (2019) · Journal of Exercise Rehabilitation · doi:10.12965/jer.1938274.137 · Cited by 21
Bonetti, N. R., Liberale, L., Akhmedov, A. T., Pasterk, L., Gobbato, S., Puspitasari, Y. M., Vukolic, A., Saravi, S. S. S., Coester, B., Horváth, C., et al. (2021) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2021.04.005 · Cited by 22
De Masi, R., & Orlando, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137373 · Cited by 20
“Thus, the complex signaling pathway is constituted by the sequence of selectins, chemokines and integrins at the interface blood/CNS, resulting in emperipolesis through matrix metalloproteinases type 9 (MMP9) activation and tight-junctions disruption [74,75].”
BackgroundContributions of Drug Transporters to Blood-Brain Barriers
Liu, L., & Liu, X. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-7647-4_9 · Cited by 21
Gong, M., & Jia, J. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.949129 · Cited by 20
Kim, S.-A., Jong, Y.-C., Kang, M.-S., & Yu, C. (2022) · Journal of Molecular Modeling · doi:10.1007/s00894-022-05264-y · Cited by 20
Pansieri, J., Hadley, G., Lockhart, A., Pisa, M., & DeLuca, G. C. (2023) · Frontiers in Neurology · doi:10.3389/fneur.2023.1199491 · Cited by 21
Zhang, Y., Yang, H., Hou, S., Xia, Y., & Wang, Y. (2024) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2024.5354 · Cited by 23
Su, Q., Su, C., Zhang, Y., Guo, Y., Liu, Y., Liu, Y., Yong, V. W., & Xue, M. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.111962 · Cited by 20
Cogill, S. A., Lee, J.-H., Jeon, M., Kim, D.-G., & Chang, Y. (2024) · Cells · doi:10.3390/cells13100789 · Cited by 20
Yang, F., Zhang, X., Sun, Y., Wang, B., Zhou, C., Luo, Y., & Ge, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057869 · Cited by 20
Brain Edema and Disorders of Cerebrospinal Fluid Circulation
Rosenberg, G. A. (2008) · Elsevier eBooks · doi:10.1016/b978-0-7506-7525-3.50101-1 · Cited by 20
Self-citationZhang, B., Xu, X., Chu, X., Yu, X., & Zhao, Y. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.03.001 · Cited by 20
Metadata
- Authors
- Yang, Y., Estrada, E. Y., Thompson, J. F., Liu, W., & Rosenberg, G. A.
- Affiliations
- University of New Mexico Health Sciences Center (US)
- Corresponding author
- Rosenberg, Gary A
- Venue
- Journal of Cerebral Blood Flow & Metabolism
- Publisher
- SAGE Publications
- Published
- 2007-04
- Volume
- 27
- Issue
- 4
- Pages
- 697-709
- ISSN
- 0271-678X (ISSN-L)
- 1559-7016
- OpenAlex
- W2005675003
- Cited by
- 1,060
- References
- 46
- Citations by year
- 2026: 35 · 2025: 43 · 2024: 37 · 2023: 58 · 2022: 74 · 2021: 67 · 2020: 60 · 2019: 57 · 2018: 55 · 2017: 64 · 2016: 59 · 2015: 65 · 2014: 54 · 2013: 59 · 2012: 56
- FWCI
- 24.32
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Cerebral Blood Flow & Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (R01NS045847)
- Topics
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Clinical Neurology › Acute Ischemic Stroke Management
- Keywords
- matrix metalloproteinases, tight junction proteins, blood-brain barrier disruption, focal cerebral ischemia, ischemia-reperfusion injury, occludin, claudin-5, MMP-2, MMP-9, MT1-MMP, furin, middle cerebral artery occlusion, astrocytes, cerebral vasculature
- MeSH terms
- Animals, Astrocytes, Blood-Brain Barrier, Cerebral Arteries, Brain Ischemia, Cerebral Veins, Evans Blue, Immunohistochemistry, Male, Membrane Proteins, Nerve Tissue Proteins, Protease Inhibitors, Rats, Inbred SHR, RNA, Messenger, Sucrose, Blotting, Western, Reperfusion Injury, Gelatinases, Tight Junctions, Reverse Transcriptase Polymerase Chain Reaction, Infarction, Middle Cerebral Artery, Enzyme Activators, Matrix Metalloproteinase 2, Matrix Metalloproteinases, Endothelial Cells, Furin, Rats, Matrix Metalloproteinase Inhibitors, Claudin-5, Occludin
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review