2017
DOI: 10.1194/jlr.m072520
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Mobility of “HSPG-bound” LPL explains how LPL is able to reach GPIHBP1 on capillaries

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Cited by 38 publications
(33 citation statements)
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“…The levels of both IDL and VLDL are increased in patients with nephrotic syndrome, primarily owing to defective LPL activity and decreased hepatic lipase activity 21 . For decades, the dogma was that LPL, which contains positively charged heparin-binding domains, binds to negatively charged heparin sulfate proteoglycans in the glycocalyx coating of blood vessels 29,30 . However, it is now established that the binding of LPL to heparan sulfate proteoglycans on endothelial cells occurs via endothelium-derived glycosylphosphatidylinositol-anchored HDL-binding protein 1 (GPIHBP1) 31 .…”
Section: Dyslipidaemia In Nephrotic Syndromementioning
confidence: 99%
“…The levels of both IDL and VLDL are increased in patients with nephrotic syndrome, primarily owing to defective LPL activity and decreased hepatic lipase activity 21 . For decades, the dogma was that LPL, which contains positively charged heparin-binding domains, binds to negatively charged heparin sulfate proteoglycans in the glycocalyx coating of blood vessels 29,30 . However, it is now established that the binding of LPL to heparan sulfate proteoglycans on endothelial cells occurs via endothelium-derived glycosylphosphatidylinositol-anchored HDL-binding protein 1 (GPIHBP1) 31 .…”
Section: Dyslipidaemia In Nephrotic Syndromementioning
confidence: 99%
“…A specific chaperone called Sel1L stabilizes the LPL-LMF1 complex 18 . Next, LPL is transported to the luminal surface of endothelial cells in conjunction with heparan sulfate proteoglycans (HSPG) 19, 20 . The glycosylphosphatidylinositol (GPI)-anchored high density lipoprotein-binding protein 1 (GPIHBP1) participates in this transport process 2123 , and also anchors LPL to the endothelial cell surface 24 .…”
Section: Overview Of Trl Metabolismmentioning
confidence: 99%
“…After secretion by parenchymal cells, LPL is retained on the cell surface through interaction with HSPGs prevalent in the ECM. Importantly, the interactions between LPL and HSPGs are dynamic (Allan et al, 2017), allowing LPL to navigate the interstitial space until captured on the basolateral surface of nearby capillary endothelial cells. SDC1 expressed on the basolateral surface of capillary endothelial cells would be positioned to capture interstitial LPL and may aid in LPL transcytosis by promoting its association with GPIHBP1, the GPI-anchored protein identified as the transcytosis receptor that shuttles LPL from the basolateral to the apical surface of capillary endothelial cells (Beigneux, 2010, Beigneux et al, 2007.…”
Section: Discussionmentioning
confidence: 99%