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Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Balazs, Z; Panzenboeck, U; Hammer, A; Sovic, A; Quehenberger, O; Malle, E; Sattler, W.
Uptake and transport of high-density lipoprotein (HDL) and HDL-associated alpha-tocopherol by an in vitro blood-brain barrier model.
J NEUROCHEM. 2004; 89(4): 939-950.
Doi: 10.1111/j.1471-4159.2004.02373.x
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- Führende Autor*innen der Med Uni Graz
- Sattler Wolfgang
- Co-Autor*innen der Med Uni Graz
- Hammer Astrid
- Malle Ernst
- Panzenboeck Ute
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- Abstract:
- The present study aimed to investigate pathways that contribute to uptake and transcytosis of high-density lipoproteins (HDLs) and HDL-associated alpha-tocopherol (alpha TocH) across an in vitro model of the blood-brain barrier (BBB). In primary porcine brain capillary endothelial cells HDL-associated alpha TocH was taken up in 10-fold excess of HDL holoparticles, indicating efficient selective uptake, a pathway mediated by scavenger receptor class B, type I (SR-BI). SR-BI was present in caveolae of brain capillary endothelial cells and expressed almost exclusively at the apical membrane. Disruption of caveolae with methyl-beta-cyclodextrin (CDX) resulted in (mis)sorting of SR-BI to the basolateral membrane. Immunohistochemistry of porcine brain cryosections revealed SR-BI expression on brain capillary endothelial cells and presumably astrocytic endfeet. HDL-associated [(14)C]alpha TocH taken up by brain capillary endothelial cells was recovered in sucrose gradient fractions containing the majority of cellular caveolin-1, the major caveolae-associated protein. During mass transfer studies using alpha TocH-enriched HDL, approximately 50% of cellular alpha TocH was recovered with the bulk of cellular caveolin-1 and SR-BI. Efflux experiments revealed that a substantial amount of cell-associated [(14)C]alpha TocH could be mobilized into the culture medium. In addition, apical-to-basolateral transport of HDL holoparticles and HDL-associated alpha TocH was saturable. Results from the present study suggest that part of cerebral apolipoprotein A-I and alpha TocH originates from plasma HDL transcytosed across the BBB and that caveolae-located SR-BI facilitates selective uptake of HDL-associated alpha TocH at the BBB.
- Find related publications in this database (using NLM MeSH Indexing)
- Animals -
- Antigens, CD36 -
- Apolipoprotein A-I - metabolism
- Biological Transport - physiology
- Biotinylation - physiology
- Blood-Brain Barrier - cytology
- Brain - cytology
- Brain Chemistry - cytology
- Capillaries - cytology
- Caveolae - chemistry
- Caveolin 1 - chemistry
- Caveolins - chemistry
- Cell Membrane - chemistry
- Cells, Cultured - chemistry
- Cyclodextrins - chemistry
- Endothelial Cells - metabolism
- Lipoproteins, HDL - chemistry
- Models, Biological - chemistry
- Receptors, Immunologic - metabolism
- Receptors, Scavenger - metabolism
- Scavenger Receptors, Class B - metabolism
- Subcellular Fractions - chemistry
- Swine - chemistry
- alpha-Tocopherol - chemistry
- beta-Cyclodextrins - chemistry
- Find related publications in this database (Keywords)
- brain capillary endothelial cells
- caveolin-1
- scavenger receptor class B type 1
- transcytosis
- vitamin E