Highly conserved cysteines within the Ly6 domain of GPIHBP1 are crucial for the binding of lipoprotein lipase.
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Chylomicronemia with low postheparin lipoprotein lipase levels in the setting of GPIHBP1 defectsGPIHBP1 is responsible for the entry of lipoprotein lipase into capillariesGlycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 and the intravascular processing of triglyceride-rich lipoproteinsPalmoplantar keratoderma along with neuromuscular and metabolic phenotypes in Slurp1-deficient miceUnexpected expression pattern for glycosylphosphatidylinositol-anchored HDL-binding protein 1 (GPIHBP1) in mouse tissues revealed by positron emission tomography scanning.Deletion of the basement membrane heparan sulfate proteoglycan type XVIII collagen causes hypertriglyceridemia in mice and humansMultimerization of glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) and familial chylomicronemia from a serine-to-cysteine substitution in GPIHBP1 Ly6 domainMutation of conserved cysteines in the Ly6 domain of GPIHBP1 in familial chylomicronemia.GPIHBP1 and the processing of triglyceride-rich lipoproteinsGPIHBP1, an endothelial cell transporter for lipoprotein lipase.High-resolution imaging of dietary lipids in cells and tissues by NanoSIMS analysis.Binding preferences for GPIHBP1, a glycosylphosphatidylinositol-anchored protein of capillary endothelial cellsEquivalent binding of wild-type lipoprotein lipase (LPL) and S447X-LPL to GPIHBP1, the endothelial cell LPL transporter.Mutations in lipoprotein lipase that block binding to the endothelial cell transporter GPIHBP1Assessing the role of the glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) three-finger domain in binding lipoprotein lipaseIdentification and quantitative mRNA analysis of a novel splice variant of GPIHBP1 in dairy cattle.Evidence for Two Distinct Binding Sites for Lipoprotein Lipase on Glycosylphosphatidylinositol-anchored High Density Lipoprotein-binding Protein 1 (GPIHBP1).Deletion of GPIHBP1 causing severe chylomicronemiaChylomicronemia mutations yield new insights into interactions between lipoprotein lipase and GPIHBP1New wrinkles in lipoprotein lipase biology.Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells.Biochemistry and pathophysiology of intravascular and intracellular lipolysis.The metabolism of triglyceride-rich lipoproteins revisited: new players, new insight.Mutations in LPL, APOC2, APOA5, GPIHBP1 and LMF1 in patients with severe hypertriglyceridaemiaMonoclonal antibodies that bind to the Ly6 domain of GPIHBP1 abolish the binding of LPL.Mobility of "HSPG-bound" LPL explains how LPL is able to reach GPIHBP1 on capillaries.An LPL-specific monoclonal antibody, 88B8, that abolishes the binding of LPL to GPIHBP1.GPIHBP1 and Plasma Triglyceride Metabolism.Angiopoietin-like 4 Modifies the Interactions between Lipoprotein Lipase and Its Endothelial Cell Transporter GPIHBP1.GPIHBP1 missense mutations often cause multimerization of GPIHBP1 and thereby prevent lipoprotein lipase binding.A new monoclonal antibody, 4-1a, that binds to the amino terminus of human lipoprotein lipase.ANGPTL8 promotes the ability of ANGPTL3 to bind and inhibit lipoprotein lipase.GPIHBP1: two get tangled.Mutating a conserved cysteine in GPIHBP1 reduces amounts of GPIHBP1 in capillaries and abolishes LPL binding.Apolipoprotein C-III inhibits triglyceride hydrolysis by GPIHBP1-bound LPL.GPIHBP1 autoantibodies in a patient with unexplained chylomicronemia.
P2860
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P2860
Highly conserved cysteines within the Ly6 domain of GPIHBP1 are crucial for the binding of lipoprotein lipase.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 02 September 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Highly conserved cysteines wit ...... binding of lipoprotein lipase.
@en
Highly conserved cysteines wit ...... binding of lipoprotein lipase.
@nl
type
label
Highly conserved cysteines wit ...... binding of lipoprotein lipase.
@en
Highly conserved cysteines wit ...... binding of lipoprotein lipase.
@nl
prefLabel
Highly conserved cysteines wit ...... binding of lipoprotein lipase.
@en
Highly conserved cysteines wit ...... binding of lipoprotein lipase.
@nl
P2093
P2860
P356
P1476
Highly conserved cysteines wit ...... binding of lipoprotein lipase
@en
P2093
André Bensadoun
Anne P Beigneux
Loren G Fong
Michael M Weinstein
P2860
P304
30240-30247
P356
10.1074/JBC.M109.046391
P407
P577
2009-09-02T00:00:00Z