Evidence for vesicles that mediate long-chain fatty acid uptake by human microvascular endothelial cells

Ring, Axel; Pohl, Jürgen; Völkl, Alfred; Stremmel, Wolfgang

doi:10.1194/jlr.m200285-jlr200

Cited by 24 publications

(20 citation statements)

References 45 publications

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“…These data are consistent with the fact that HMEC-1 cells have a high capacity for vesicle transport mediated by caveolae and clathrin [49] . It is known that both types of transport are essential in inward and outward cellular cholesterol traffic [50] .…”

Section: Discussionsupporting

confidence: 80%

“…These results suggest that the antiviral activity of LOV cannot be completely explained by the reduction of cholesterol or inhibition of prenylation of Rho (which is usually geranylgeranylated) and Ras proteins (which are often farnesylated). However, LOV viral inhibition could be due to its inhibition of the prenylation of other proteins, such as Rab, that are involved at several steps of the DENV replicative cycle [48][49][50][51][52][53] .…”

Section: Discussionmentioning

confidence: 99%

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Statins Reduce Dengue Virus Production via Decreased Virion Assembly

2011

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Background: Most of the effects of statins can be explained by pleiotropic effects independent of their lowering of serum cholesterol; in some cases, these effects have been shown to be a result of the role of statins in the prenylation of cellular proteins, some of which are involved in the life cycle of animal viruses. This study evaluated the potential antiviral activity of lovastatin (LOV) against dengue virus (DENV) infection of epithelial and endothelial cells (VERO cells, epithelial cells derived from African green monkey kidney, and HMEC-1 cells, human dermal microvascular endothelial cells). Methods: To evaluate its potential antiviral effects, LOV was used before, during and after inoculation of cell cultures with DENV. Results: Before and after viral inoculation, LOV caused a reduction in virus yield (80% for HMECs and 25% for VERO cells). However, with LOV treatment after inoculation induced a marked increase (2- to 9-fold) in viral-positive RNA while the amount of viral protein increased only by 13–23%. A moderate reduction (1 log unit) in viral titer occurred concurrent with the increase in DENV genomic RNA and protein within the cells. Conclusions: According to our results, LOV appears to have a greater effect on viral assembly than on replication, resulting in the cellular presence of viral genomic RNA and proteins that fail to take the normal assembly pathway.

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Section: Discussionsupporting

confidence: 80%

Section: Discussionmentioning

confidence: 99%

Statins Reduce Dengue Virus Production via Decreased Virion Assembly

2011

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“…First, caveolin-1 in adipocytes was shown to be a fatty acid binding protein itself (25). It has also been suggested that caveolae are involved in endocytosis of fatty acids (26). Alternatively, plasma membrane caveolae may regulate the function of fatty acid transporters such as FAT/CD36.…”

Section: Discussionmentioning

confidence: 99%

Sarcolemmal FAT/CD36 in human skeletal muscle colocalizes with caveolin-3 and is more abundant in type 1 than in type 2 fibers

Vistisen

Roepstorff

et al. 2004

Journal of Lipid Research

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FAT/CD36 is a transmembrane protein that is thought to facilitate cellular long-chain fatty acid uptake. However, surprisingly little is known about the localization of FAT/CD36 in human skeletal muscle. By confocal immunofluorescence microscopy, we demonstrate high FAT/CD36 expression in endothelial cells and weaker but significant FAT/CD36 expression in sarcolemma in human skeletal muscle. No apparent intracellular staining was observed in the muscle cells. There are indications in the literature that caveolae may be involved in the uptake of fatty acids, possibly as regulators of FAT/CD36 or other fatty acid transporters. We show that in sarcolemma, FAT/CD36 colocalizes with the muscle-specific caveolae marker protein caveolin-3, suggesting that caveolae may regulate cellular fatty acid uptake by FAT/CD36. Furthermore, we provide evidence that FAT/ CD36 expression is significantly higher in type 1 compared with type 2 fibers, whereas caveolin-3 expression is significantly higher in type 2 fibers than in type 1 fibers. -Vistisen, B., K. Roepstorff, C. Roepstorff, A. Bonen, B. van Deurs, and B. Kiens. Sarcolemmal FAT/CD36 in human skeletal muscle colocalizes with caveolin-3 and is more abundant in type 1 than in type 2 fibers. J. Lipid Res. 2004. 45: 603-609.

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“…The findings that a major protein associated with fatty acid uptake, FAT/CD36 (Abumrad et al 1993), is preferentially located in the caveolae at the plasma membrane level (Kolleck et al 2002), and that caveolin-1 binding with fatty acids is saturable (Trigatti et al 1999) stimulated interest in the possibility that caveolae might have a function in lipid transport. Indeed, in previous studies Ring et al 2002) it was shown that caveolae are associated with the overall process of cellular uptake of LCFA. When caveolin-1-green fluorescence protein was expressed in HepG2 cells and exposed to the fluorescent LCFA derivative 12-(N-methyl)-N-[(7-nitrobenz-2-oxa-1, 3-diazol-4-yl)amino] stearate, there was marked co-localization of 12-(N-methyl)-N-[(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino] stearate with green fluorescence protein.…”

Section: The Fatty Acid Transport Protein Familymentioning

confidence: 99%

New concepts of cellular fatty acid uptake: role of fatty acid transport proteins and of caveolae

et al. 2004

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Efficient uptake and channelling of long-chain fatty acids (LCFA) are critical cell functions. Evidence is emerging that proteins are important mediators of LCFA-trafficking into cells and various proteins have been suggested to be involved in this process. Amongst these proteins is a family of membrane-associated proteins termed fatty acid transport proteins (FATP). So far six members of this family, designated FATP 1–6, have been characterized. FATP 1, 2 and 6 show a highly-conserved AMP-binding region that participates in the activation of very-long-chain fatty acids (VLCFA) to form their acyl-CoA derivatives. The mechanisms by which FATP mediate LCFA uptake are not well understood, but several studies provide evidence that uptake of LCFA across cellular membranes is closely linked to acyl-CoA synthetase activity. It is proposed that FATP indirectly enhance LCFA uptake by activating VLCFA to their CoA esters, which are required to maintain the typical structure of lipid rafts in cellular membranes. Recent work has shown that the structural integrity of lipid rafts is essential for cellular LCFA uptake. This effect might be exerted by proteins, e.g. caveolin-1 and FAT/CD36, that use lipid rafts as platforms and bind or transport LCFA. The proposed molecular mechanisms await further experimental investigation.

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Evidence for vesicles that mediate long-chain fatty acid uptake by human microvascular endothelial cells

Cited by 24 publications

References 45 publications

Statins Reduce Dengue Virus Production via Decreased Virion Assembly

Statins Reduce Dengue Virus Production via Decreased Virion Assembly

Sarcolemmal FAT/CD36 in human skeletal muscle colocalizes with caveolin-3 and is more abundant in type 1 than in type 2 fibers

New concepts of cellular fatty acid uptake: role of fatty acid transport proteins and of caveolae

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