Ultracytochemical characteristics of cultured goat brain microvascular endothelial cells [corrected]

Vorbrodt, A; Trowbridge, R. S.

doi:10.1177/39.11.1655877

Cited by 24 publications

(16 citation statements)

References 20 publications

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“…Conversely, the TNAP activity was mainly detected in the abluminal plasma membrane of rat BCECs (Inomata et al 1984), in luminal plasma membrane of mice brain capillaries and in both luminal and abluminal plasma membranes in arterioles (Vorbrodt et al 1986). Again, the TNAP activity is detected both on the luminal and abluminal walls of BCECs in frog (Lazzari et al 1989) and goat (Vorbrodt and Trowbridge 1991). This discrepancy of localisation comes likely from methods used to fix tissue that inactivate the TNAP.…”

Section: Cell Localisationmentioning

confidence: 80%

“…Indeed, many authors have reported the existence of BBB in many vertebrates (Abbott 2005). Several studies demonstrated the presence of AP activity in capillary endothelium of rat brain (Meunier and Bouchaud 1978;Liu et al 1979;Inomata et al 1984), mouse brain (Vorbrodt et al 1981(Vorbrodt et al , 1986, goat brain (Vorbrodt and Trowbridge 1991), avian species (Stewart and Wiley 1981), frog brain (Latker et al 1987;Lazzari et al 1989), cat brain (Vorbrodt et al 1985), primate brain (Shi and Audus 1994), bovine brain (Brunel et al 1969). Recently, the impermeability of cerebral microvessels has been first reported in zebrafish following in vivo experimentation of permeability assays (sulfo-NHS-biotin and horseradish peroxydase) and immunoreactivity towards integral proteins (Claudin-5 and Zonula Occludens-1) of the tight junctions (Jeong et al 2008).…”

Section: Species Specificitymentioning

confidence: 95%

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Tissue Non-specific Alkaline Phosphatase (TNAP) in Vessels of the Brain

Deracinois

Lenfant

Dehouck

et al. 2015

Subcellular Biochemistry

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The microvessels of the brain represent around 3-4 % of the brain compartment but constitute the most important length (400 miles) and surface of exchange (20 m(2)) between the blood and the parenchyma of brain. Under influence of surrounding tissues, the brain microvessel endothelium expresses a specific phenotype that regulates and restricts the entry of compounds and cells from blood to brain, and defined the so-called blood-brain barrier (BBB). Evidences that alkaline phosphatase (AP) is a characteristic feature of the BBB phenotype that allows differentiating capillary endothelial cells from brain to those of the periphery have rapidly emerge. Thenceforth, AP has been rapidly used as a biomarker of the blood-brain barrier phenotype. In fact, brain capillary endothelial cells (BCECs) express exclusively tissue non-specific alkaline phosphatase (TNAP). There are several lines of evidence in favour of an important role for TNAP in brain function. TNAP is thought to be responsible for the control of transport of some compounds across the plasma membrane of the BCECs. Here, we report that levamisole-mediated inhibition of TNAP provokes an increase of the permeability to Lucifer Yellow of the endothelial monolayer. Moreover, we illustrate the disruption of the cytoskeleton organization. Interestingly, all observed effects were reversible 24 h after levamisole removal and correlated with the return of a full activity of the TNAP. This reversible effect remains to be studied in details to evaluate the potentiality of a levamisole treatment to enhance the entry of drugs in the brain parenchyma.

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Section: Cell Localisationmentioning

confidence: 80%

Section: Species Specificitymentioning

confidence: 95%

Tissue Non-specific Alkaline Phosphatase (TNAP) in Vessels of the Brain

Deracinois

Lenfant

Dehouck

et al. 2015

Subcellular Biochemistry

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“…Alkaline phosphatase is an enzyme anchored in the apical membrane of cells that possess P-glycoprotein (Moss, 1982;1992;Robinson & Karnovsky, 1983;Fojo et al, 1987;Vorbrodt & Trowbridge, 1991). All these cells -intestinal epithelium, kidney proximal tubules, hepatocytes, blood-brain barrier, placenta -are lining surfaces endowed with intense transport activities (secretion and absorption).…”

Section: Calculations and Statisticsmentioning

confidence: 99%

Inward transport of [³H]‐1‐methyl‐4‐phenylpyridinium in rat isolated hepatocytes: putative involvement of a P‐glycoprotein transporter

Martel

Martins

Hipólito-Reis

et al. 1996

British J Pharmacology

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The liver has an important role in the detoxification of organic cations from the circulation. [3H]‐1‐methyl‐4‐phenylpyridinium ([3H]‐MPP+), a low molecular weight organic cation, is efficiently taken up and accumulated by rat hepatocytes through mechanisms partially unknown. The aim of the present work was to characterize further the uptake of MPP+ by rat isolated hepatocytes. The putative interactions of a wide range of drugs, including inhibitors/substrates of P‐glycoprotein, were studied. The uptake of MPP+ was investigated in rat freshly isolated hepatocytes (incubated in Krebs‐Henseleit medium with 200 nM [3H]‐MPP+ for 5 min) and in the rat liver in situ (perfused with Krebs‐Henseleit/BSA medium with 200 nM [3H]‐MPP+ for 30 min). [3H]‐MPP+ accumulation in the cells and in tissue was determined by liquid scintillation counting. Verapamil (100 μm), quinidine (100 μm), amiloride (1 mM), (+)‐tubocurarine (100 μm), vecuronium (45 μm), bilirubin (200 μm), progesterone (200 μm), daunomycin (100 μm), vinblastine (100 μm), cyclosporin A (100 μm) and cimetidine (100 μm) had a significant inhibitory effect on the accumulation of [3H]‐MPP+ in isolated hepatocytes. Tetraethylammonium (100 μm) had no effect. In the rat perfused liver, both cyclosporin A (100 μm) and verapamil (100 μm) had much less marked inhibitory effects as compared to their effects on isolated hepatocytes (0% against 35% and 45% against 96% of inhibition, respectively). Inhibition of alkaline phosphatase activity by increasing or decreasing the pH of the incubation medium or by the presence of vanadate (1 mM) or homoarginine (500 μm) led to a significant increase in the accumulation of [3H]‐MPP+ in isolated hepatocytes. It was concluded that, in addition to the type I organic cation hepatic transporter, [3H]‐MPP+ is taken up by rat isolated hepatocytes through P‐glycoprotein, a canalicular transport system that usually excretes endobiotics and xenobiotics. We proposed that the reversal of transport through P‐glycoprotein may be related to the loss of efficiency of alkaline phosphatase in isolated hepatocytes.

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“…Magnification 300 ase (g-GT) has been observed upon in vitro cultivation (Meyer et al 1990). In other in vitro model systems of the blood brain barrier, the ALP activity was reported to be not entirely absent, but reduced in comparison to in vivo conditions and decreasing with increasing passage number (Vorbrodt and Trowbridge 1991;Shi and Audus 1994). When, on the other hand, cell differentiation into capillary-like sprouts was induced in immortilized brain endothelial cells by b-FGF, these sprouts resumed expression of ALP (Roux et al 1994).…”

Section: Discussionmentioning

confidence: 95%

“…Another typical alteration observed in endothelial cells in vitro is a loss of plasmalemmal vesicles (Vorbrodt and Trowbridge 1991;Roberts and Sandra 1993). Since ALP activity in myocardial capillary endothelial cells is mainly located in plasmalemmal vesicles, i.e., on the plasmalemmal membrane ), this finding is likely to represent the morphological correlate of the observed enzyme activity loss.…”

Section: Discussionmentioning

confidence: 98%

Loss of myocardial capillary endothelial-cell alkaline phosphatase (ALP) activity in primary endothelial cell culture

Lindner

Behrends

Misumi

et al. 1998

Cell and Tissue Research

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Primary cultures of rat myocardial capillary endothelial cells were established and characterized. A range of typical endothelial cell-specific markers were retained in vitro. Cell kinetic studies in confluent endothelial-cell cultures in vitro revealed a roughly 50-fold increase in the proportion of cells in s-phase, indicating a very considerable shortening of cell turnover time, compared to in vivo conditions. Alkaline phosphatase enzyme activity and encoding mRNA are strongly expressed in myocardial capillary endothelial cells in vivo, but were not detectable in vitro. This was true in cell cultures from two strains of rat, which revealed significantly different enzyme expression levels in vivo. In co-cultures of pericytes and endothelial cells, positive ALP enzyme reaction was detected in pericytes, which in vivo show only very weak enzyme reactivity. Treatment of cell cultures with

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Ultracytochemical characteristics of cultured goat brain microvascular endothelial cells [corrected]

Cited by 24 publications

References 20 publications

Tissue Non-specific Alkaline Phosphatase (TNAP) in Vessels of the Brain

Tissue Non-specific Alkaline Phosphatase (TNAP) in Vessels of the Brain

Inward transport of [³H]‐1‐methyl‐4‐phenylpyridinium in rat isolated hepatocytes: putative involvement of a P‐glycoprotein transporter

Loss of myocardial capillary endothelial-cell alkaline phosphatase (ALP) activity in primary endothelial cell culture

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Ultracytochemical characteristics of cultured goat brain microvascular endothelial cells [corrected]

Cited by 24 publications

References 20 publications

Tissue Non-specific Alkaline Phosphatase (TNAP) in Vessels of the Brain

Tissue Non-specific Alkaline Phosphatase (TNAP) in Vessels of the Brain

Inward transport of [3H]‐1‐methyl‐4‐phenylpyridinium in rat isolated hepatocytes: putative involvement of a P‐glycoprotein transporter

Loss of myocardial capillary endothelial-cell alkaline phosphatase (ALP) activity in primary endothelial cell culture

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Inward transport of [³H]‐1‐methyl‐4‐phenylpyridinium in rat isolated hepatocytes: putative involvement of a P‐glycoprotein transporter