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Journal articles on the topic 'Blood-brain barrier'

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Published: 4 June 2021
Last updated: 29 July 2024

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1

KANDA, Takashi. "Blood-Brain Barrier and Blood-Nerve Barrier." Yamaguchi Medical Journal 54, no. 1 (2005): 5–11. http://dx.doi.org/10.2342/ymj.54.5.

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2

Shalaby, Mohamed Adel. "Blood-Brain Barrier." Al-Azhar Medical Journal 45, no. 3 (July 2016): i—vi. http://dx.doi.org/10.12816/0033115.

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3

Lawther, Bradley K., Sajith Kumar, and Hari Krovvidi. "Blood–brain barrier." Continuing Education in Anaesthesia Critical Care & Pain 11, no. 4 (August 2011): 128–32. http://dx.doi.org/10.1093/bjaceaccp/mkr018.

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4

Dunn, Jeff F., and Albert M. Isaacs. "The impact of hypoxia on blood-brain, blood-CSF, and CSF-brain barriers." Journal of Applied Physiology 131, no. 3 (September 1, 2021): 977–85. http://dx.doi.org/10.1152/japplphysiol.00108.2020.

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The blood-brain barrier (BBB), blood-cerebrospinal fluid (CSF) barrier (BCSFB), and CSF-brain barriers (CSFBB) are highly regulated barriers in the central nervous system comprising complex multicellular structures that separate nerves and glia from blood and CSF, respectively. Barrier damage has been implicated in the pathophysiology of diverse hypoxia-related neurological conditions, including stroke, multiple sclerosis, hydrocephalus, and high-altitude cerebral edema. Much is known about the damage to the BBB in response to hypoxia, but much less is known about the BCSFB and CSFBB. Yet, it is known that these other barriers are implicated in damage after hypoxia or inflammation. In the 1950s, it was shown that the rate of radionucleated human serum albumin passage from plasma to CSF was five times higher during hypoxic than normoxic conditions in dogs, due to BCSFB disruption. Severe hypoxia due to administration of the bacterial toxin lipopolysaccharide is associated with disruption of the CSFBB. This review discusses the anatomy of the BBB, BCSFB, and CSFBB and the impact of hypoxia and associated inflammation on the regulation of those barriers.
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5

Koziara, J. M., P. R. Lockman, D. D. Allen, and R. J. Mumper. "The Blood-Brain Barrier and Brain Drug Delivery." Journal of Nanoscience and Nanotechnology 6, no. 9 (September 1, 2006): 2712–35. http://dx.doi.org/10.1166/jnn.2006.441.

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The present report encompasses a thorough review of drug delivery to the brain with a particular focus on using drug carriers such as liposomes and nanoparticles. Challenges in brain drug delivery arise from the presence of one of the strictest barriers in vivo—the blood-brain barrier (BBB). This barrier exists at the level of endothelial cells of brain vasculature and its role is to maintain brain homeostasis. To better understand the principles of brain drug delivery, relevant knowledge of the blood-brain barrier anatomy and physiology is briefly reviewed. Several approaches to overcome the BBB have been reviewed including the use of carrier systems. In addition, strategies to enhance brain drug delivery by specific brain targeting are discussed.
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6

Cho, Choi-Fong. "The Blood-Brain Barrier." Oncology Times 40, no. 2 (January 2018): 1. http://dx.doi.org/10.1097/01.cot.0000530114.97923.aa.

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7

Mizee, Mark Ronald, and Helga Eveline de Vries. "Blood-brain barrier regulation." Tissue Barriers 1, no. 5 (December 2013): e26882. http://dx.doi.org/10.4161/tisb.26882.

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8

Dobbing, John. "The Blood-Brain Barrier." Developmental Medicine & Child Neurology 3, no. 6 (November 12, 2008): 610–12. http://dx.doi.org/10.1111/j.1469-8749.1961.tb10430.x.

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9

Dobbing, John. "The Blood-Brain Barrier." Developmental Medicine & Child Neurology 3, no. 4 (November 12, 2008): 311–14. http://dx.doi.org/10.1111/j.1469-8749.1961.tb15323.x.

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10

Daneman, Richard, and Alexandre Prat. "The Blood–Brain Barrier." Cold Spring Harbor Perspectives in Biology 7, no. 1 (January 2015): a020412. http://dx.doi.org/10.1101/cshperspect.a020412.

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11

Goldstein, N., R. Goldstein, D. Terterov, A. A. Kamensky, G. I. Kovalev, Yu A. Zolotarev, G. N. Avakyan, and S. Terterov. "Blood-brain barrier unlocked." Biochemistry (Moscow) 77, no. 5 (May 2012): 419–24. http://dx.doi.org/10.1134/s000629791205001x.

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12

Goldstein, Gary W., and A. Lorris Betz. "The Blood-Brain Barrier." Scientific American 255, no. 3 (September 1986): 74–83. http://dx.doi.org/10.1038/scientificamerican0986-74.

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13

Engelhardt, B. "Blood-Brain Barrier Differentiation." Science 334, no. 6063 (December 22, 2011): 1652–53. http://dx.doi.org/10.1126/science.1216853.

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14

Pan, Weihong, and Abba J. Kastin. "The Blood-Brain Barrier." Neuroscientist 23, no. 2 (July 7, 2016): 124–36. http://dx.doi.org/10.1177/1073858416639005.

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Sleep and its disorders are known to affect the functions of essential organs and systems in the body. However, very little is known about how the blood-brain barrier (BBB) is regulated. A few years ago, we launched a project to determine the impact of sleep fragmentation and chronic sleep restriction on BBB functions, including permeability to fluorescent tracers, tight junction protein expression and distribution, glucose and other solute transporter activities, and mediation of cellular mechanisms. Recent publications and relevant literature allow us to summarize here the sleep-BBB interactions in five sections: (1) the structural basis enabling the BBB to serve as a huge regulatory interface; (2) BBB transport and permeation of substances participating in sleep-wake regulation; (3) the circadian rhythm of BBB function; (4) the effect of experimental sleep disruption maneuvers on BBB activities, including regional heterogeneity, possible threshold effect, and reversibility; and (5) implications of sleep disruption-induced BBB dysfunction in neurodegeneration and CNS autoimmune diseases. After reading the review, the general audience should be convinced that the BBB is an important mediating interface for sleep-wake regulation and a crucial relay station of mind-body crosstalk. The pharmaceutical industry should take into consideration that sleep disruption alters the pharmacokinetics of BBB permeation and CNS drug delivery, being attentive to the chrono timing and activation of co-transporters in subjects with sleep disorders.
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15

JOÓ, FERENC. "The blood–brain barrier." Nature 329, no. 6136 (September 1987): 208. http://dx.doi.org/10.1038/329208b0.

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16

Pardridge, William M. "Blood-Brain Barrier Genomics." Stroke 38, no. 2 (February 2007): 686–90. http://dx.doi.org/10.1161/01.str.0000247887.61831.74.

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17

Palmer, Alan M. "The blood–brain barrier." Neurobiology of Disease 37, no. 1 (January 2010): 1–2. http://dx.doi.org/10.1016/j.nbd.2009.09.023.

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18

Li, Jian Yi, Ruben J. Boado, and William M. Pardridge. "Blood—Brain Barrier Genomics." Journal of Cerebral Blood Flow & Metabolism 21, no. 1 (January 2001): 61–68. http://dx.doi.org/10.1097/00004647-200101000-00008.

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The blood–brain barrier (BBB) is formed by the brain microvascular endothelium, and the unique transport properties of the BBB are derived from tissue-specific gene expression within this cell. The current studies developed a gene microarray approach specific for the BBB by purifying the initial mRNA from isolated rat brain capillaries to generate tester cDNA. A polymerase chain reaction–based subtraction cloning method, suppression subtractive hybridization (SSH), was used, and the BBB cDNA was subtracted with driver cDNA produced from mRNA isolated from rat liver and kidney. Screening 5% of the subtracted tester cDNA resulted in identification of 50 gene products and more than 80% of those were selectively expressed at the BBB; these included novel gene sequences not found in existing databases, ESTs, and known genes that were not known to be selectively expressed at the BBB. Genes in the latter category include tissue plasminogen activator, insulin-like growth factor-2, PC-3 gene product, myelin basic protein, regulator of G protein signaling 5, utrophin, IκB, connexin-45, the class I major histocompatibility complex, the rat homologue of the transcription factors hbrm or EZH1, and organic anion transporting polypeptide type 2. Knowledge of tissue-specific gene expression at the BBB could lead to new targets for brain drug delivery and could elucidate mechanisms of brain pathology at the microvascular level.
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19

Stoker, Andrew W. "Blood–brain barrier breached." Trends in Genetics 17, no. 3 (March 2001): 129. http://dx.doi.org/10.1016/s0168-9525(01)02246-6.

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20

Dyrna, Felix, Sophie Hanske, Martin Krueger, and Ingo Bechmann. "The Blood-Brain Barrier." Journal of Neuroimmune Pharmacology 8, no. 4 (June 6, 2013): 763–73. http://dx.doi.org/10.1007/s11481-013-9473-5.

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21

Younger, David S. "The Blood-Brain Barrier." Neurologic Clinics 37, no. 2 (May 2019): 235–48. http://dx.doi.org/10.1016/j.ncl.2019.01.009.

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22

Bradbury, MW. "The blood-brain barrier." Experimental Physiology 78, no. 4 (July 1, 1993): 453–72. http://dx.doi.org/10.1113/expphysiol.1993.sp003698.

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23

Fehervari, Zoltan. "Blood–brain barrier integrity." Nature Immunology 20, no. 1 (December 11, 2018): 1. http://dx.doi.org/10.1038/s41590-018-0286-9.

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24

Serlin, Yonatan, Jonathan Ofer, Gal Ben-Arie, Ronel Veksler, Gal Ifergane, Ilan Shelef, Jeffrey Minuk, Anat Horev, and Alon Friedman. "Blood-Brain Barrier Leakage." Stroke 50, no. 5 (May 2019): 1266–69. http://dx.doi.org/10.1161/strokeaha.119.025247.

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25

MNH. "The Blood-Brain Barrier." Journal of Neuropathology & Experimental Neurology 62, no. 10 (October 2003): 1086. http://dx.doi.org/10.1093/jnen/62.10.1086.

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26

Wright, Karen. "The Blood-Brain Barrier." Scientific American 260, no. 3 (March 1989): 27–30. http://dx.doi.org/10.1038/scientificamerican0389-27.

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27

Pardridge, William M. "Blood–brain barrier delivery." Drug Discovery Today 12, no. 1-2 (January 2007): 54–61. http://dx.doi.org/10.1016/j.drudis.2006.10.013.

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28

Arvanitis, Costas D., Gino B. Ferraro, and Rakesh K. Jain. "The blood–brain barrier and blood–tumour barrier in brain tumours and metastases." Nature Reviews Cancer 20, no. 1 (October 10, 2019): 26–41. http://dx.doi.org/10.1038/s41568-019-0205-x.

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29

Mineiro, Rafael, Tânia Albuquerque, Ana Raquel Neves, Cecília R. A. Santos, Diana Costa, and Telma Quintela. "The Role of Biological Rhythms in New Drug Formulations to Cross the Brain Barriers." International Journal of Molecular Sciences 24, no. 16 (August 8, 2023): 12541. http://dx.doi.org/10.3390/ijms241612541.

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For brain protection, the blood–brain barrier and blood–cerebrospinal fluid barrier limit the traffic of molecules between blood and brain tissue and between blood and cerebrospinal fluid, respectively. Besides their protective function, brain barriers also limit the passage of therapeutic drugs to the brain, which constitutes a great challenge for the development of therapeutic strategies for brain disorders. This problem has led to the emergence of novel strategies to treat neurological disorders, like the development of nanoformulations to deliver therapeutic agents to the brain. Recently, functional molecular clocks have been identified in the blood–brain barrier and in the blood–cerebrospinal fluid barrier. In fact, circadian rhythms in physiological functions related to drug disposition were also described in brain barriers. This opens the possibility for chronobiological approaches that aim to use time to improve drug efficacy and safety. The conjugation of nanoformulations with chronobiology for neurological disorders is still unexplored. Facing this, here, we reviewed the circadian rhythms in brain barriers, the nanoformulations studied to deliver drugs to the brain, and the nanoformulations with the potential to be conjugated with a chronobiological approach to therapeutic strategies for the brain.
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30

Moody, Dixon M. "The Blood-Brain Barrier and Blood-Cerebral Spinal Fluid Barrier." Seminars in Cardiothoracic and Vascular Anesthesia 10, no. 2 (June 2006): 128–31. http://dx.doi.org/10.1177/1089253206288992.

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An intact blood-brain barrier and normal production, circulation, and absorption of cerebrospinal fluid are critical for normal brain function. Minor disruptions of barrier function are without clinical consequences. Major disruptions accompany most significant acute brain injuries. The anatomic location of the blood-brain barrier is the endothelial cells of arterioles, capillaries, veins, and the epithelial cell surface of the choroid plexus. However, endothelial cells require the presence of glial cells to maintain barrier function. During cardiopulmonary bypass, several factors may result in a temporary disruption of the barrier; the most important are systemic inflammatory response and focal ischemia due to emboli. Lacking a lymphatic system, the brain depends on the circulation of cerebrospinal fluid to remove the products of metabolism, and the circulation of cerebrospinal fluid depends on a vascular systolic pulse wave to drive this fluid antegrade along the brain paravascular spaces. Although it is not possible to identify this paravavscular space histologically, its presence is confirmed by tracer methods.
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31

Paulson, O. "Blood–brain barrier, brain metabolism and cerebral blood flow." European Neuropsychopharmacology 12, no. 6 (December 2002): 495–501. http://dx.doi.org/10.1016/s0924-977x(02)00098-6.

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32

Schlosshauer, Burkhard, and Heiko Steuer. "The Blood-brain Barrier and the Outer Blood-retina Barrier." Medicinal Chemistry Reviews - Online 2, no. 1 (February 1, 2005): 11–26. http://dx.doi.org/10.2174/1567203052997031.

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33

McCabe, Shannon Morgan, and Ningning Zhao. "The Potential Roles of Blood–Brain Barrier and Blood–Cerebrospinal Fluid Barrier in Maintaining Brain Manganese Homeostasis." Nutrients 13, no. 6 (May 27, 2021): 1833. http://dx.doi.org/10.3390/nu13061833.

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Manganese (Mn) is a trace nutrient necessary for life but becomes neurotoxic at high concentrations in the brain. The brain is a “privileged” organ that is separated from systemic blood circulation mainly by two barriers. Endothelial cells within the brain form tight junctions and act as the blood–brain barrier (BBB), which physically separates circulating blood from the brain parenchyma. Between the blood and the cerebrospinal fluid (CSF) is the choroid plexus (CP), which is a tissue that acts as the blood–CSF barrier (BCB). Pharmaceuticals, proteins, and metals in the systemic circulation are unable to reach the brain and spinal cord unless transported through either of the two brain barriers. The BBB and the BCB consist of tightly connected cells that fulfill the critical role of neuroprotection and control the exchange of materials between the brain environment and blood circulation. Many recent publications provide insights into Mn transport in vivo or in cell models. In this review, we will focus on the current research regarding Mn metabolism in the brain and discuss the potential roles of the BBB and BCB in maintaining brain Mn homeostasis.
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34

Francesca, Bonomini, and Rita Rezzani. "Aquaporin and Blood Brain Barrier." Current Neuropharmacology 8, no. 2 (June 1, 2010): 92–96. http://dx.doi.org/10.2174/157015910791233132.

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35

McMahon, Andrew P., and Justin K. Ichida. "Repairing the blood-brain barrier." Science 375, no. 6582 (February 18, 2022): 715–16. http://dx.doi.org/10.1126/science.abn7921.

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36

Rustenhoven, Justin, and Jonathan Kipnis. "Bypassing the blood-brain barrier." Science 366, no. 6472 (December 19, 2019): 1448–49. http://dx.doi.org/10.1126/science.aay0479.

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37

Chen, Yi-Je, Breanna K. Wallace, Natalie Yuen, David P. Jenkins, Heike Wulff, and Martha E. O’Donnell. "Blood–Brain Barrier KCa3.1 Channels." Stroke 46, no. 1 (January 2015): 237–44. http://dx.doi.org/10.1161/strokeaha.114.007445.

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38

Neuwelt, E. A., P. A. Barnett, C. I. McCormick, E. P. Frenkel, and J. D. Minna. "Osmotic blood-brain barrier modification." Neurosurgery 17, no. 3 (September 1985): 419???23. http://dx.doi.org/10.1097/00006123-198509000-00005.

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39

Schulze, C. "Understanding the Blood-Brain-Barrier." Neuropathology and Applied Neurobiology 23, no. 3 (June 1997): 150–51. http://dx.doi.org/10.1046/j.1365-2990.1997.t01-1-90098900.x.

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40

Schulze, Dr C. "Understanding the Blood-Brain-Barrier." Neuropathology and Applied Neurobiology 23, no. 2 (April 1997): 150–51. http://dx.doi.org/10.1111/j.1365-2990.1997.tb01197.x.

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41

Stern, Peter. "Developing the blood-brain barrier." Science 361, no. 6404 (August 23, 2018): 763.11–765. http://dx.doi.org/10.1126/science.361.6404.763-k.

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42

Simpson, Ian A., Nathan M. Appel, Mitsuhiko Hokari, Jun Oki, Geoffrey D. Holman, Fran Maher, Ellen M. Koehler-Stec, Susan J. Vannucci, and Quentin R. Smith. "Blood-Brain Barrier Glucose Transporter." Journal of Neurochemistry 72, no. 1 (January 1999): 238–47. http://dx.doi.org/10.1046/j.1471-4159.1999.0720238.x.

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43

Keaney, James, and Matthew Campbell. "The dynamic blood-brain barrier." FEBS Journal 282, no. 21 (September 8, 2015): 4067–79. http://dx.doi.org/10.1111/febs.13412.

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44

Sánchez-Navarro, Macarena, Ernest Giralt, and Meritxell Teixidó. "Blood–brain barrier peptide shuttles." Current Opinion in Chemical Biology 38 (June 2017): 134–40. http://dx.doi.org/10.1016/j.cbpa.2017.04.019.

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45

Ermisch, A., H. J. Rühle, R. Landgraf, and J. Hess. "Blood—Brain Barrier and Peptides." Journal of Cerebral Blood Flow & Metabolism 5, no. 3 (September 1985): 350–57. http://dx.doi.org/10.1038/jcbfm.1985.49.

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The brain is both the source and the recipient of peptide signals. The question is: Do endogenous, blood-borne peptide molecules influence brain function? Brain regions with the tight capillaries of the blood–brain barrier (BBB) extract low but measurable amounts of labeled peptide molecules from an intracarotid bolus injection. In the rat, the extraction fractions of β-casomorphin-5, DesGlyNH2-arginine-vasopressin, arginine-vasopressin, lysine-vasopressin, oxytocin, gonadoliberin, substance P, and β-endorphin, studied in this laboratory, range from 0.5% (substance P) to 2.4% (arginine-vasopressin). Extraction varies little among the 15 examined brain regions. As shown for arginine-vasopressin, the extracted peptides may be bound in part to specific binding sites located on the luminal membrane of the tight endothelial cells. Transport of peptide molecules across the BBB cannot be ruled out, but it is unlikely that endogenous peptides pass the BBB in physiologically significant amounts. In contrast, in brain regions with leaky capillaries, e.g., selected circumventricular organs including the pineal gland, neurohypophysis, and choroid plexus, the peptide fraction extracted approaches that of water. Within the circumventricular organs, the peptide molecules actually reach the cellular elements of the tissue. However, no studies definitively show that peptides reach neurons in the deeper layers of the brain. On the other hand, blood-borne peptides influence the BBB permeability by altering the transport of essential substances. The effect may be mediated by specific peptide binding sites located at the luminal membrane of the endothelium. It is possible that the effect of peptides on the BBB is necessary for proper brain function. There is some evidence that peptides, released centrally into the synaptic clefts as well as peripherally into the bloodstream, support complex brain performances by both of these pathways.
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46

Bjorklund, Anders, and Clive Svendsen. "Breaking the brain-blood barrier." Nature 397, no. 6720 (February 1999): 569–70. http://dx.doi.org/10.1038/17495.

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47

Tuomanen, Elaine. "Breaching the Blood-Brain Barrier." Scientific American 268, no. 2 (February 1993): 80–84. http://dx.doi.org/10.1038/scientificamerican0293-80.

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48

Petrovskaya, A. V., E. P. Barykin, A. M. Tverskoi, K. B. Varshavskaya, V. A. Mitkevich, I. Yu Petrushanko, and A. A. Makarov. "Blood–Brain Barrier Transwell Modeling." Molecular Biology 56, no. 6 (December 2022): 1020–27. http://dx.doi.org/10.1134/s0026893322060140.

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49

Hampton, Tracy. "Restoring the Blood-Brain Barrier." JAMA 309, no. 5 (February 6, 2013): 431. http://dx.doi.org/10.1001/jama.2013.267.

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50

ÖZTAŞ, BARİA. "SEX AND BLOOD-BRAIN BARRIER." Pharmacological Research 37, no. 3 (March 1998): 165–67. http://dx.doi.org/10.1006/phrs.1997.0243.

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