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Glycosylphosphatidylinositol‐anchored high‐density lipoprotein‐binding protein 1 and the intravascular processing of triglyceride‐rich lipoproteins
Author(s) -
Adeyo O.,
Goulbourne C. N.,
Bensadoun A.,
Beigneux A. P.,
Fong L. G.,
Young S. G.
Publication year - 2012
Publication title -
journal of internal medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.625
H-Index - 160
eISSN - 1365-2796
pISSN - 0954-6820
DOI - 10.1111/joim.12003
Subject(s) - lipoprotein lipase , lipoprotein , triglyceride , very low density lipoprotein , interstitial space , medicine , microbiology and biotechnology , endocrinology , biochemistry , chemistry , biology , cholesterol , adipose tissue
Lipoprotein lipase ( LPL ) is produced by parenchymal cells, mainly adipocytes and myocytes, but is involved in hydrolysing triglycerides in plasma lipoproteins at the capillary lumen. For decades, the mechanism by which LPL reaches its site of action in capillaries was unclear, but this mystery was recently solved. Glycosylphosphatidylinositol‐anchored high‐density lipoprotein‐binding protein 1 ( GPIHBP 1), a glycosylphosphatidylinositol‐anchored protein of capillary endothelial cells, ‘picks up’ LPL from the interstitial spaces and shuttles it across endothelial cells to the capillary lumen. When GPIHBP 1 is absent, LPL is mislocalized to the interstitial spaces, leading to severe hypertriglyceridaemia. Some cases of hypertriglyceridaemia in humans are caused by GPIHBP 1 mutations that interfere with the ability of GPIHBP 1 to bind to LPL , and some are caused by LPL mutations that impair the ability of LPL to bind to GPIHBP 1. Here, we review recent progress in understanding the role of GPIHBP 1 in health and disease and discuss some of the remaining unresolved issues regarding the processing of triglyceride‐rich lipoproteins.