Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells[S]

Brandon S. J Davies; Chris N Goulbourne; Richard H Barnes II; Kirsten A Turlo; Peter Gin; Sue Vaughan; David J Vaux; André Bensadoun; Anne P Beigneux; Loren G Fong; Stephen G Young

doi:10.1194/jlr.M031559

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Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells[S]

Journal article

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Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells[S]

Brandon S. J Davies, Chris N Goulbourne, Richard H Barnes II, Kirsten A Turlo, Peter Gin, Sue Vaughan, David J Vaux, André Bensadoun, Anne P Beigneux, Loren G Fong, …

Journal of lipid research, Vol.53(12), pp.2690-2697

12/2012

DOI: 10.1194/jlr.M031559

PMCID: PMC3494248

PMID: 23008484

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Abstract

Lipoprotein lipase (LPL) is secreted into the interstitial spaces by adipocytes and myocytes but then must be transported to the capillary lumen by GPIHBP1, a glycosylphosphatidylinositol-anchored protein of capillary endothelial cells. The mechanism by which GPIHBP1 and LPL move across endothelial cells remains unclear. We asked whether the transport of GPIHBP1 and LPL across endothelial cells was uni- or bidirectional. We also asked whether GPIHBP1 and LPL are transported across cells in vesicles and whether this transport process requires caveolin-1. The movement of GPIHBP1 and LPL across cultured endothelial cells was bidirectional. Also, GPIHBP1 moved bidirectionally across capillary endothelial cells in live mice. The transport of LPL across endothelial cells was inhibited by dynasore and genistein, consistent with a vesicular transport process. Also, transmission electron microscopy (EM) and dual-axis EM tomography revealed GPIHBP1 and LPL in invaginations of the plasma membrane and in vesicles. The movement of GPIHBP1 across capillary endothelial cells was efficient in the absence of caveolin-1, and there was no defect in the internalization of LPL by caveolin-1-deficient endothelial cells in culture. Our studies show that GPIHBP1 and LPL move bidirectionally across endothelial cells in vesicles and that transport is efficient even when caveolin-1 is absent.

Lipid Metabolism

triglycerides

chylomicrons

caveolae

transcytosis

Details

Title: Subtitle: Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells[S]
Creators: Brandon S. J Davies - Department of Medicine and
Chris N Goulbourne - Department of Medicine and
Richard H Barnes II - Department of Medicine and
Kirsten A Turlo - Department of Medicine and
Peter Gin - Department of Medicine and
Sue Vaughan - School of Life Sciences
David J Vaux - Sir William Dunn School of Pathology
André Bensadoun - Division of Nutritional Sciences
Anne P Beigneux - Department of Medicine and
Loren G Fong - Department of Medicine and
Stephen G Young - Department of Medicine and
Resource Type: Journal article
Publication Details: Journal of lipid research, Vol.53(12), pp.2690-2697
DOI: 10.1194/jlr.M031559
PMID: 23008484
PMCID: PMC3494248
NLM abbreviation: J Lipid Res
ISSN: 0022-2275
eISSN: 1539-7262
Publisher: The American Society for Biochemistry and Molecular Biology
Language: English
Date published: 12/2012
Academic Unit: Fraternal Order of Eagles Diabetes Research Center; Biochemistry and Molecular Biology
Record Identifier: 9984025270602771

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