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A classic example of the enzymatic barrier and an early example of the NVU.
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Sandoval, D. A., Obici, S. & Seeley, R. J. Targeting the CNS to treat type 2 diabetes. Nat. Rev. Drug Discov. 8, 386–398 (2009).
Shows the fundamental role of the BBB in controlling blood glucose levels via its transport of insulin into the CNS.
Scherer, T. et al. Brain insulin controls adipose tissue lipolysis and lipogenesis. Cell Metab. 13, 183–194 (2011).
Banks, W. A., DiPalma, C. R. & Farrell, C. L. Impaired transport of leptin across the blood–brain barrier in obesity. Peptides 20, 1341–1345 (1999).
Romeo, G., Liu, W. H., Asnaghi, V., Kern, T. S. & Lorenzi, M. Activation of nuclear factor-κB induced by diabetes and high glucose regulates a proapoptotic program in retinal pericytes. Diabetes 51, 2241–2248 (2002).
Huber, J. D., VanGilder, R. L. & Houser, K. A. Streptozotocin-induced diabetes progressively increases blood–brain barrier permeability in specific brain regions in rats. Am. J. Physiol. 291, H2660–H2668 (2006).
Starr, J. M. et al. Increased blood–brain barrier permeability in type II diabetes demonstrated by gadolinium magnetic resonance imaging. J. Neurol. Neurosurg. Psychiatry 74, 70–76 (2003).
References 152 and 153 establish that BBB disruption occurs in diabetes.
Shah, G. N., Morofuji, Y., Banks, W. A. & Price, T. O. High glucose-induced mitochondrial resistance and reactive oxygen species in mouse cerebral pericytes is reversed by pharmacological inhibition of mitochondrial carbonic anhydrase: implications for cerbral microvascular disease in diabetes. Biochem. Biophys. Res. Commun. 440, 354–358 (2013).
Demonstrates that BBB disruption occurs because of oxidative stress arising from excess mitochondrial respiration.
Kowluru, R. A. Diabetic retinopathy: mitochondrial dysfunction and retinal capillary cell death. Antioxid. Redox Signal. 7, 1581–1587 (2005).
Weiwei, Z. & Hu, R. Targeting carbonic anhydrase to treat diabetic retinopathy: emerging evidences and encouraging results. Biochem. Biophys. Res. Commun. 390, 368–371 (2009).
Banks, W. A. et al. Triglycerides induce leptin resistance at the blood–brain barrier. Diabetes 53, 1253–1260 (2004).
Kastin, A. J. & Akerstrom, V. Glucose and insulin increase the transport of leptin through the blood–brain barrier in normal mice but not in streptozotocin-diabetic mice. Neuroendocrinology 73, 237–242 (2001).
Ito, S. et al. 1α,25-dihydroxyvitam D3 enhances cerebral clearance of human amyloid-β peptide(1-40) from mouse brain across the blood–brain barrier. Fluids Barriers CNS 8, 20 (2011).
Moon, J. H. et al. The effect of rosiglitazone on LRP1 expression and amyloid β uptake in human brain microvascular endothelial cells: a possible role of a low-dose thiazolidinedione for dementia treatment. Int. J. Neuropsychopharmacol. 1, 1–8 (2011).
O'Donnell, M. E., Lam, T. I., Tran, L. Q., Foroutan, S. & Anderson, S. E. Estradiol reduces activity of the blood–brain barrier Na-K-Cl cotransporter and decreases edema formation in permenent middle cerebral artery occlusion. J. Cereb. Blood Flow Metab. 26, 1234–1249 (2006).
Lyden, P. et al. Phase 1 safety, tolerability and pharmacokinetics of 3K3A-APC in healthy adult vounteers. Curr. Pharm. Design 19, 7479–7485 (2013).
McGuire, T. R. et al. Release of prostaglandin E-2 in bovine brain endothelial cells after exposure to three unique forms of the antifungal drug amphotericin-B: role of COX-2 in amphotericin-B induced fever. Life Sci. 72, 2581–2590 (2003).
Sury, M. D. et al. Evidence that N-acetylcysteine inhibits TNF-α-induced cerebrovascular endothelin-1 upregulation via inhibition of mitogen- and stress-activated protein kinase. Free Radic. Biol. Med. 41, 1372–1383 (2006).
Didier, N., Banks, W. A., Creminon, C., Dereuddre-Bosquet, N. & Mabondzo, A. HIV-1-induced production of endothelin-1 in an in vitro model of the human blood–brain barrier. Neuroreport 13, 1179–1183 (2002).
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Li, J. et al. Immune activation of human brain microvascular endothelial cells inhibits HIV replication in macrophages. Blood 121, 2934–2942 (2013).
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Reese, T. S. & Karnovsky, M. J. Fine structural localization of a blood–brain barrier to endogenous peroxidase. J. Cell Biol. 34, 207–217 (1967).
A classic paper demonstrating the ultrastructural basis for the BBB: the presence of tight junctions and decreased transcytotic vesicles.
Coisne, C., Mao, W. & Engelhardt, B. Cutting edge: natalizumab blocks adhesion but not initial contact of human T cells to the blood–brain barrier in vivo in an animal model of multiple sclerosis. J. Immunol. 182, 5909–5913 (2009).