Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells[S]
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...
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Elsevier
2012-12-01
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| Series: | Journal of Lipid Research |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520418036 |
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doaj-39ccf5f8d4b84b0184c04c6d5c9a68312021-04-28T06:05:12ZengElsevierJournal of Lipid Research0022-22752012-12-01531226902697Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells[S]Brandon S.J. Davies0Chris N. Goulbourne1Richard H. Barnes, II2Kirsten A. Turlo3Peter Gin4Sue Vaughan5David J. Vaux6André Bensadoun7Anne P. Beigneux8Loren G. Fong9Stephen G. Young10To whom correspondence should be addressed. e-mail: Brandon-davies@uiowa.edu (B.S.J.D); sgyoung@mednet.ucla.edu (S.G.Y).; Department of Medicine and University of California, Los Angeles, CA 90095; To whom correspondence should be addressed. e-mail: Brandon-davies@uiowa.edu (B.S.J.D); sgyoung@mednet.ucla.edu (S.G.Y).Department of Medicine and University of California, Los Angeles, CA 90095Department of Medicine and University of California, Los Angeles, CA 90095Department of Medicine and University of California, Los Angeles, CA 90095Department of Medicine and University of California, Los Angeles, CA 90095School of Life Sciences, Oxford Brookes University, Oxford, OX3 0BP, United KingdomSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United KingdomDivision of Nutritional Sciences, Cornell University, Ithaca, NY 14853Department of Medicine and University of California, Los Angeles, CA 90095Department of Medicine and University of California, Los Angeles, CA 90095To whom correspondence should be addressed. e-mail: Brandon-davies@uiowa.edu (B.S.J.D); sgyoung@mednet.ucla.edu (S.G.Y).; Department of Medicine and University of California, Los Angeles, CA 90095; Department of Human Genetics, University of California, Los Angeles, CA 90095; To whom correspondence should be addressed. e-mail: Brandon-davies@uiowa.edu (B.S.J.D); sgyoung@mednet.ucla.edu (S.G.Y).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.http://www.sciencedirect.com/science/article/pii/S0022227520418036transcytosistriglyceridescaveolaechylomicronslipid metabolism |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
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 |
| spellingShingle |
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 Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells[S] Journal of Lipid Research transcytosis triglycerides caveolae chylomicrons lipid metabolism |
| author_facet |
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 |
| author_sort |
Brandon S.J. Davies |
| title |
Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells[S] |
| title_short |
Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells[S] |
| title_full |
Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells[S] |
| title_fullStr |
Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells[S] |
| title_full_unstemmed |
Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells[S] |
| title_sort |
assessing mechanisms of gpihbp1 and lipoprotein lipase movement across endothelial cells[s] |
| publisher |
Elsevier |
| series |
Journal of Lipid Research |
| issn |
0022-2275 |
| publishDate |
2012-12-01 |
| description |
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. |
| topic |
transcytosis triglycerides caveolae chylomicrons lipid metabolism |
| url |
http://www.sciencedirect.com/science/article/pii/S0022227520418036 |
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