Brain microvessel endothelial cells in tissue culture: A model for study of blood‐brain barrier permeability

Bowman, Phillip D.; Ennis, Steven R.; Rarey, Kyle E.; Betz, A. Lorris; Goldstein, Gary W.

doi:10.1002/ana.410140403

Cited by 305 publications

(148 citation statements)

References 23 publications

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“…Similar Factor VIII antigen la beling was recently used by Bowman et al (1983) to identify cerebral endothelial cells in culture that possessed a number of features of the morpholog ical BBB (contiguity by tight junctions, paucity of pinocytotic vesicules). Thus, even if the contami nating cells possessed zero MAO activity, their presence could not account for a MAO activity nearly ninefold less than that in the fresh microves sels.…”

Section: Figmentioning

confidence: 95%

Monoamine Oxidase Activity in the Cerebral Vasculature: Comparison between Fresh Microvessels from Different Structures and Cell Cultures Derived from Microvessels

Sercombe¹,

Lasbennes²,

Drouet

et al. 1984

J Cereb Blood Flow Metab

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Summary: Monoamine oxidase (MAO) activity was studied in various preparations of porcine brain micro vessels to explore further the role of this enzyme in the blood-brain barrier to catecholamines, No difference was noted (V m and Km) between microvessels isolated from three structures (caudate nucleus, thalamus, and ce rebral cortex) in which the responses to circulating cat echolamines in vivo are markedly different. Large and small microvessels from the caudate nucleus and the thal amus presented the same specific activity. Cell cultures obtained from small microvessels were rich in endothelial cells as identified by the presence of Factor VIII -relatedIn a recent paper (Lasbennes et aI., 1983), we showed that the level of monoamine oxidase (MAO; EC 1.4.3.4) activity in brain microvessels, as mea sured by V m (the maximum activity of the enzyme with respect to a given substrate), was high for both artificial and natural substrates, with a high Km (the concentration of substrate giving one-half V m) ' sug gesting that this enzyme could play an efficient part in blood-brain barrier (BBB) mechanisms. It is generally believed that the cerebrovascular MAO is situated to a great extent in the endothelium, since a characteristic green fluorescence is seen in the endothelium after L-3,4-dihydroxyphenylalanine (L-DOPA) injection in animals treated with a MAO inhibitor (Bertler et al., 1966; Hardebo et aI., 1979). However, in spite of the BBB, circulating cateAddress correspondence and reprint requests to Dr. Sercombe at INSERM U 182, 10 avenue de Verdun, 75010 Paris, France.Abbreviations used: BBB, Blood-brain barrier; BSA, bovine serum albumin; HEPES, N-2-hydroxyethyl piperazine-N'-2-eth anesulfonic acid; 6-k-PGF la , 6-keto-prostaglandin Fla; L-DOPA, L-3,4-dihydroxyphenylalanine; M 199, medium 199; MAO, monoamine oxidase; NA, noradrenaline; PBS, phosphate-buff ered salt solution; PGE2, prostaglandin E2. 415antigen. These preparations displayed an MAO activity about ninefold less than freshly isolated microvessels, al though their prostaglandin synthetase activity appeared normal. These results suggest that MAO activity is not the main factor determining the regional differences in the cerebrovascular reactions to catecholamines, that MAO is not specifically localized in the endothelium but must be also present in the smooth muscle, and that the MAO activity is greatly decreased during cell culture.

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Section: Figmentioning

confidence: 95%

Monoamine Oxidase Activity in the Cerebral Vasculature: Comparison between Fresh Microvessels from Different Structures and Cell Cultures Derived from Microvessels

Sercombe¹,

Lasbennes²,

Drouet

et al. 1984

J Cereb Blood Flow Metab

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“…These brains were devoid of any pathologic abnormalities, as described, and the isolation and purification procedures were conducted according to the method developed by Bowman et al (18), with minor modifications. These cells were then immortalized (17) and characterized in our laboratory, as described elsewhere (25).…”

Section: Hbecmentioning

confidence: 99%

TGF-β1 Released from Activated Platelets Can Induce TNF-Stimulated Human Brain Endothelium Apoptosis: A New Mechanism for Microvascular Lesion during Cerebral Malaria

Wassmer

Souza

Frère

et al. 2006

The Journal of Immunology

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Platelets have recently been shown to accumulate in brain microvessels of patients with cerebral malaria and to modulate the binding of Plasmodium falciparum-infected red cells to human brain endothelium in vitro. In the present study we used a platelet-endothelial cell coculture model to investigate the mechanisms by which platelets modify the function of human brain microvascular endothelial cells (HBEC). Platelets were found to have a proapoptotic effect on TNF-activated HBEC, and this was contact-dependent, as inhibiting platelet binding prevented endothelial cell killing. We also showed that the supernatants of thrombin-activated platelets killed TNF-stimulated HBEC and that TGF-β1 was the main molecule involved in endothelial cell death, because its inhibition completely abrogated the activated-platelet supernatant effect. Our data illustrate another aspect of the duality of TGF-β1 in malaria and may provide new insights into the pathogenesis of cerebral malaria.

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“…PBCECs were prepared and cultured according to Bowman et al (1983) as modified by Tewes et a!. (1997).…”

Section: Cell Culturementioning

confidence: 99%

Basement Membrane Proteins Influence Brain Capillary Endothelial Barrier Function In Vitro

Tilling

Korte

Hoheisel

et al. 1998

Journal of Neurochemistry

164

109

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Abstract:The influence of basement membrane proteins on cellular barrier properties of primary cultures of porcine brain capillary endothelial cells grown on permeable filter inserts has been investigated. Measurements of transcellular electrical resistance (TEA) by impedance spectroscopy were performed with cells cultured on type IV collagen, fibronectin, laminin, and one-to-one mixtures of these proteins. Moreover, a one-to-one combination of type IV collagen and SPARC (secreted protein acidic and rich in cysteine) has been studied. Rat tail collagen has been used as a reference substratum. If TERs of cells from a given preparation were low (-~350Q x cm 2) on the reference substratum, type IV collagen, fibronectin, and laminin as well as one-to-one combinations of these proteins elevated transcellular resistances significantly (2.3-to 2.9-fold) compared with rat tail collagen. TER of cells exhibiting a high reference level (~-~1 000~l x cm2) could, by contrast, be increased only 1.1-to 1.2-fold. The type IV collagen/SPARC mixture did not elevate TER. Our findings suggest that type IV collagen, fibronectin, and laminin are involved in tight junction formation between cerebral capillary endothelial cells. The differential effects observed for individual preparations probably reflect more or less dedifferentiated states of the endothelium, in which basement membrane proteins can influence cellular differentiation more or less strongly. However, our results indicate that type IV collagen, fibronectin, and laminin enhance the reliability and suitability of primary microvascular endothelial cell cultures as an in vitro model of the blood-brain barrier. Key Words: Bloodbrain barrier-Primary cell culture-Transcellular electrical resistance-Basement membrane proteins-Extracellular matrix.

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Brain microvessel endothelial cells in tissue culture: A model for study of blood‐brain barrier permeability

Cited by 305 publications

References 23 publications

Monoamine Oxidase Activity in the Cerebral Vasculature: Comparison between Fresh Microvessels from Different Structures and Cell Cultures Derived from Microvessels

Monoamine Oxidase Activity in the Cerebral Vasculature: Comparison between Fresh Microvessels from Different Structures and Cell Cultures Derived from Microvessels

TGF-β1 Released from Activated Platelets Can Induce TNF-Stimulated Human Brain Endothelium Apoptosis: A New Mechanism for Microvascular Lesion during Cerebral Malaria

Basement Membrane Proteins Influence Brain Capillary Endothelial Barrier Function In Vitro

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