Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz

Logo MUG-Forschungsportal

Gewählte Publikation:

SHR Neuro Krebs Kardio Lipid

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. [OPEN ACCESS]
Web of Science PubMed FullText FullText_MUG


Autor/innen der Med Uni Graz:
Hammer Astrid
Malle Ernst
Panzenboeck Ute
Sattler Wolfgang

Dimensions Citations:

Plum Analytics:
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
scavenger receptor class B type 1
vitamin E
© Med Uni Graz Impressum