Affinage

GPIHBP1

Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 · UniProt Q8IV16

Length
184 aa
Mass
19.9 kDa
Annotated
2026-06-10
100 papers in source corpus 39 papers cited in narrative 38 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

GPIHBP1 is a GPI-anchored protein of capillary endothelial cells that functions as the dedicated platform and transporter for lipoprotein lipase (LPL), enabling intravascular triglyceride lipolysis (PMID:17620854, PMID:18845532). It is built from two functional modules: an intrinsically disordered, acidic (Asp/Glu-rich) N-terminal domain that engages LPL through electrostatic interactions, and a three-fingered Ly6/LU domain that forms a stable, longer-lived contact with LPL's C-terminal lipid-binding domain (residues 298–448) (PMID:18713736, PMID:21518912, PMID:25873395). The acidic domain accelerates LPL capture by electrostatic steering—an effect enhanced by O-sulfation of a conserved tyrosine that raises the LPL association rate constant >250-fold—and it sheathes LPL's basic patch so that LPL–GPIHBP1 complexes can cross the endothelial cell rather than being trapped by abluminal heparan sulfate proteoglycans (PMID:29899144, PMID:36037340). GPIHBP1 picks up LPL released from interstitial HSPGs and shuttles it bidirectionally across the endothelium in dynamin-dependent vesicles to the capillary lumen, where GPIHBP1-bound LPL drives margination and lipolysis of triglyceride-rich lipoproteins, and from which LPL can transfer into the glycocalyx (PMID:21478160, PMID:24726386, PMID:23008484, PMID:27811232, PMID:37871217). Binding requires a structurally intact Ly6 domain: conserved cysteines, N-glycosylation at Asn-76, and the monomeric state of GPIHBP1 are all essential, and mutations that disrupt these (or autoantibodies against the Ly6 domain) abolish LPL binding (PMID:18340083, PMID:19726683, PMID:25387803, PMID:28402248). Beyond capture and transport, GPIHBP1 stabilizes LPL's catalytic domain against spontaneous and ANGPTL4-catalyzed unfolding, protecting enzyme activity (PMID:26725083, PMID:27929370). A crystal structure shows the LU domain binding LPL's C-terminal domain through hydrophobic contacts, with LPL active as a 1:1 monomer (PMID:30559189, PMID:31072929). Loss-of-function mutations, gene deletion, and neutralizing autoantibodies all strand LPL in the interstitium and cause severe chylomicronemia in humans (PMID:19304573, PMID:22008945, PMID:28402248).

Mechanistic history

Synthesis pass · year-by-year structured walk · 17 steps
  1. 2002 Medium

    GPIHBP1 was first identified as a GPI-anchored cell-surface protein with high-affinity HDL binding and lipid-uptake activity, establishing it as a lipid-handling membrane protein before its LPL role was known.

    Evidence Expression cloning with fluorescent HDL, lipid uptake assays, and PIPL-C sensitivity in a single lab

    PMID:12496272

    Open questions at the time
    • HDL binding role not reconciled with later LPL-centric function
    • physiological ligand and tissue context not yet defined
  2. 2007 High

    Knockout mice and binding assays established GPIHBP1 as a luminal endothelial platform for LPL-mediated lipolysis, answering whether it has an essential role in triglyceride metabolism.

    Evidence Gpihbp1 knockout mouse phenotype with severe chylomicronemia, plus cell-transfection LPL/chylomicron binding assays

    PMID:17620854

    Open questions at the time
    • which GPIHBP1 domain mediates LPL binding not yet mapped
    • mechanism of chylomicron capture unresolved
  3. 2008 High

    Domain dissection assigned LPL/apoAV/chylomicron binding to the acidic N-terminal domain via electrostatic interactions and showed N-glycosylation and surface trafficking are prerequisites for any binding.

    Evidence Alanine scanning and polyanion blocking of the acidic domain; glycosylation-site mutagenesis with ER-retention and binding readouts

    PMID:18340083 PMID:18713736

    Open questions at the time
    • role of the Ly6 domain in binding not yet defined
    • structural basis of the electrostatic interface unknown
  4. 2008 High

    In vivo heparin-release kinetics demonstrated GPIHBP1 is a major physiological LPL-binding site, and PPARγ was identified as a transcriptional regulator of its tissue expression.

    Evidence Heparin and Intralipid release kinetics in Gpihbp1−/− vs control mice; luciferase reporter and endothelial PPARγ conditional knockout

    PMID:18787041 PMID:18845532

    Open questions at the time
    • mechanism of LPL release into plasma not detailed
    • additional regulatory inputs beyond PPARγ unexplored
  5. 2009 High

    Human disease mutations and Ly6-domain cysteine/Q115 mutagenesis established that a structurally intact Ly6 domain is essential for LPL binding, mechanistically linking GPIHBP1 to familial chylomicronemia.

    Evidence Patient genetics (Q115P, C65S/C68G) with cell-based and cell-free LPL binding assays and adipose LPL activity measurements

    PMID:19304573 PMID:19726683 PMID:20026666

    Open questions at the time
    • structural consequence of cysteine loss not yet defined
    • transport versus binding defect not separated
  6. 2009 High

    GPIHBP1 was shown to stabilize LPL activity and protect it from ANGPTL3/ANGPTL4 inhibition, with genetic epistasis confirming physiological relevance.

    Evidence In vitro LPL activity assays and Angptl4−/−/Gpihbp1−/− double-knockout mice with antibody rescue

    PMID:19542565

    Open questions at the time
    • molecular mechanism of protection not yet defined
    • whether protection occurs on the cell surface unclear
  7. 2010 High

    Specificity and ligand studies established that GPIHBP1 binds only LPL among lipases, binds apoAV via the acidic domain, and captures chylomicrons solely through bound LPL, and PET imaging revealed broader tissue distribution including lung and liver.

    Evidence Comparative binding assays with lipase family members and domain mutants; PET imaging with anti-GPIHBP1 antibodies and tissue LPL quantification

    PMID:20124439 PMID:20889497 PMID:20966398

    Open questions at the time
    • why some tissues capture LPL produced elsewhere not fully explained
    • functional consequence of lung/liver GPIHBP1 unresolved
  8. 2011 High

    GPIHBP1 was shown to transport LPL across endothelial cells, the minimal LPL binding element was mapped to the C-terminal domain, and finger-2 residues of the Ly6 domain were identified as the LPL interface required for transcytosis.

    Evidence LPL deletion/mutagenesis with cell-free binding; comprehensive Ly6 alanine scanning with basolateral-to-apical transport assays; human GPIHBP1 deletion patients with heparin-release studies

    PMID:21478160 PMID:21518912 PMID:22008945

    Open questions at the time
    • vesicular machinery of transport not yet identified
    • directionality and regulation of transport unresolved
  9. 2012 High

    Imaging and pharmacology established that GPIHBP1-bound LPL is the primary determinant of TRL margination and that GPIHBP1–LPL move bidirectionally in dynamin-dependent, caveolin-1-independent vesicles.

    Evidence Quantitative margination assays and EM tomography in Gpihbp1−/− and rescue mice; live-cell transport with dynasore/genistein and caveolin-1 knockout

    PMID:22493000 PMID:23008484 PMID:24726386

    Open questions at the time
    • identity of the transport vesicle pathway not pinned down
    • regulation of transport rate unknown
  10. 2014 High

    The monomeric state of GPIHBP1 was established as a requirement for LPL binding, explaining a class of disease mutations that drive aberrant disulfide-linked multimerization.

    Evidence Non-reducing Western blots and binding assays across multiple expression systems; W109 and S107C mutagenesis with patient data

    PMID:24847059 PMID:25387803

    Open questions at the time
    • in vivo relevance of multimerization later complicated by C63Y mouse data
    • direct role of W109 versus structural integrity not fully separated
  11. 2015 High

    SPR kinetics resolved two distinct LPL binding sites on GPIHBP1—a fast, salt-sensitive acidic-domain complex and a slow, heparin-resistant Ly6 complex—and showed ANGPTL4 inactivates GPIHBP1-bound LPL, after which LPL dissociates irreversibly.

    Evidence Surface plasmon resonance with domain fragments and Q114P mutant; cell-based ANGPTL4 inactivation assays with domain constructs

    PMID:25809481 PMID:25873395

    Open questions at the time
    • how the two binding modes hand off LPL not fully defined
    • ANGPTL4 mechanism at molecular level not yet resolved
  12. 2016 High

    HDX-MS revealed the mechanism of LPL stabilization—the acidic domain prevents global unfolding of LPL's catalytic domain and renders it refractory to ANGPTL4-catalyzed unfolding—and showed interstitial HSPG-bound LPL can transfer to GPIHBP1.

    Evidence HDX-MS, SPR, and cross-linking with activity assays; in vitro and in vivo LPL transfer from HSPGs to GPIHBP1 with Ly6 (W109S) and acidic-domain mutants

    PMID:26725083 PMID:27811232 PMID:27875259 PMID:27929370

    Open questions at the time
    • physical route of LPL handoff from HSPG to GPIHBP1 not fully mapped
    • in vivo balance of stabilization versus capture functions unclear
  13. 2017 High

    GPIHBP1 autoantibodies were identified as an acquired cause of chylomicronemia by blocking LPL binding, apoC-III was shown to inhibit lipolysis preferentially on GPIHBP1-bound LPL, and an in vivo C63Y mouse confirmed cysteine requirement.

    Evidence Patient autoantibody ELISA/blocking assays including neonatal transfer; GPIHBP1-bound LPL lipolysis assays with apoC-III variants; C63Y knock-in mouse

    PMID:28402248 PMID:28476858 PMID:28694296

    Open questions at the time
    • mechanism of apoC-III inhibition on the complex not molecularly resolved
    • discrepancy between cell-culture multimerization and monomeric mutant in vivo unexplained
  14. 2018 High

    The LPL–GPIHBP1 crystal structure and identification of acidic-domain tyrosine sulfation provided the structural and biochemical basis for hydrophobic Ly6–LPL contacts, monomeric active LPL, and electrostatic-steering-driven binding kinetics.

    Evidence X-ray crystallography of the LPL–GPIHBP1–LMF1 complex; mass spectrometry of sulfotyrosine with SPR kon/koff and LPL protection assays; CRISPR enhancer deletion in mice

    PMID:29899144 PMID:30559189 PMID:30598475

    Open questions at the time
    • structure of the disordered acidic domain not captured crystallographically
    • enhancer deletion did not produce hypertriglyceridemia, leaving threshold effects unclear
  15. 2019 Medium

    GPIHBP1 was shown to be ectopically expressed in glioma capillaries where it captures LPL and delivers TRL-derived lipid to tumor cells, and VEGF–Notch signaling was identified as an inducer of GPIHBP1 in the diabetic heart.

    Evidence NanoSIMS imaging and margination assays in glioma models; high-glucose EC culture with heparanase, VEGF neutralization, and Notch inhibition

    PMID:26586663 PMID:31169500

    Open questions at the time
    • therapeutic relevance of tumor GPIHBP1 not established
    • VEGF–Notch axis confirmed in a single lab
  16. 2022 High

    The three integrated functions of the acidic domain were experimentally consolidated: electrostatic steering of binding, prevention of catalytic-domain unfolding, and shielding of LPL's basic patch to permit transcytosis past abluminal HSPGs.

    Evidence Biophysical binding/activity assays and in vivo studies with acidic-domain-mutant GPIHBP1 and HSPG interaction analysis

    PMID:36037340

    Open questions at the time
    • relative contribution of each acidic-domain function in vivo not quantified
  17. 2023 High

    A post-GPIHBP1 step was defined in which luminal LPL detaches from GPIHBP1 and relocates into the endothelial glycocalyx, where it mediates TRL margination and lipid delivery.

    Evidence GPIHBP1-binding-blocking antibody (88B8), confocal and immunogold EM, NanoSIMS, and in vivo lipid delivery assays

    PMID:37871217

    Open questions at the time
    • trigger for LPL detachment into glycocalyx not defined
    • fate and turnover of glycocalyx LPL unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • The molecular machinery and regulation of vesicular GPIHBP1–LPL transcytosis, and the trigger that releases LPL from GPIHBP1 into the glycocalyx, remain unresolved.
  • identity of the transcytosis vesicle pathway unknown
  • signal governing luminal LPL handoff to glycocalyx undefined
  • regulation of GPIHBP1 surface levels across tissues incompletely mapped

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0098772 molecular function regulator activity 3 GO:0140096 catalytic activity, acting on a protein 2 GO:0140313 molecular sequestering activity 2
Localization
GO:0005886 plasma membrane 3 GO:0030312 external encapsulating structure 1 GO:0031410 cytoplasmic vesicle 1
Pathway
R-HSA-1430728 Metabolism 3 R-HSA-1643685 Disease 3 R-HSA-9609507 Protein localization 3
Partners
ANGPTL3ANGPTL4APOA5APOC3LMF1LPL
Complex memberships
LPL–GPIHBP1 complex

Evidence

Reading pass · 38 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 GPIHBP1 (GPI-HBP1) was identified as a novel GPI-anchored protein that binds HDL with high affinity (Kd = 2–3 µg/mL) and mediates selective lipid uptake but not HDL protein uptake, and lacks HDL-dependent cholesterol efflux activity. It is susceptible to phosphatidylinositol-specific phospholipase C treatment, confirming GPI anchorage. Highest expression was found in the heart. Expression cloning with fluorescent-labeled HDL; lipid uptake assays; PIPL-C treatment; in situ hybridization The Journal of biological chemistry Medium 12496272
2007 GPIHBP1-deficient mice develop severe chylomicronemia (plasma TG up to ~5000 mg/dL even on low-fat diet). GPIHBP1 is expressed on the luminal surface of capillary endothelial cells in heart, skeletal muscle, and adipose tissue. Cells transfected with GPIHBP1 bind both LPL and chylomicrons avidly, establishing GPIHBP1 as a platform for LPL-mediated lipolysis. GPIHBP1 knockout mouse model; fluorescence microscopy; cell transfection binding assays Current opinion in lipidology High 17620854
2008 The acidic domain of GPIHBP1 (amino acids 38–48, enriched in Asp/Glu) is required for binding LPL and chylomicrons. Polyaspartate and polyglutamate peptides block LPL and chylomicron binding; alanine substitution of acidic residues 38–48 eliminates binding. Electrostatic interactions are key: mutation of positively charged heparin-binding domains in LPL and apoAV abolished their binding to GPIHBP1. Cell-based binding assays with CHO cells overexpressing GPIHBP1; blocking experiments with polyaspartate/polyglutamate peptides; alanine scanning mutagenesis; anti-acidic domain antiserum blocking The Journal of biological chemistry High 18713736
2008 N-glycosylation of GPIHBP1 at Asn-76 within the Ly6 domain is critical for trafficking GPIHBP1 to the cell surface. Mutation of the N-glycosylation site causes GPIHBP1 to accumulate in the ER and markedly reduces cell-surface expression; cells expressing non-glycosylated GPIHBP1 lack the ability to bind LPL or chylomicrons. N-glycosidase F / endoglycosidase H/F digestion; site-directed mutagenesis of glycosylation site; immunofluorescence and cell-based LPL/chylomicron binding assays Journal of lipid research High 18340083
2008 In GPIHBP1-deficient mice, post-heparin plasma LPL levels peak very slowly (over 15 min) rather than rapidly (within 1 min as in wild-type), and plasma triglycerides fall negligibly within the first 15 min after heparin. Intralipid injection releases LPL in wild-type but not GPIHBP1-deficient mice, despite similar tissue LPL stores. These findings establish that GPIHBP1 represents an important LPL-binding site in vivo. Heparin injection kinetics; plasma LPL measurement; Intralipid injection; comparison of Gpihbp1−/− vs. control mice The Journal of biological chemistry High 18845532
2008 GPIHBP1 expression in heart, adipose tissue, and skeletal muscle is upregulated by fasting and by PPARγ agonists (but not PPARα or PPARδ agonists). A PPARγ binding site upstream of exon 1 exhibits activity in a luciferase reporter assay. Conditional knockout of endothelial PPARγ reduces Gpihbp1 expression in adipose tissue in vivo. Quantitative RT-PCR; luciferase reporter assay; PPARγ agonist treatment; endothelial-specific PPARγ knockout mice Molecular endocrinology Medium 18787041
2009 A homozygous Q115P missense mutation in GPIHBP1 identified in a chylomicronemia patient abolishes the ability of GPIHBP1 to bind LPL and chylomicrons without affecting cell-surface expression. The corresponding mouse mutation (Q114P) also cannot bind LPL, establishing this residue as critical for LPL binding. Patient genetic sequencing; cell-based binding assays in CHO cells expressing wild-type vs. Q115P GPIHBP1; mouse GPIHBP1 Q114P mutagenesis Arteriosclerosis, thrombosis, and vascular biology High 19304573
2009 Conserved cysteines in the Ly6 domain of GPIHBP1 (C65, C68 in humans; C65S, C68G mutations found in chylomicronemia patients) are essential for LPL binding. Cysteine mutants reach the cell surface but are defective in LPL binding in both cell-based and cell-free binding assays, demonstrating that a structurally intact Ly6 domain is required. Site-directed mutagenesis; cell-based LPL binding assay; cell-free LPL binding assay using GPIHBP1 immobilized on antibody-coated agarose beads; PIPL-C cell-surface release assay The Journal of biological chemistry High 19726683
2009 Compound heterozygous cysteine mutations in GPIHBP1 Ly6 domain (C65S and C68G) identified in familial chylomicronemia. Mutant GPIHBP1 proteins reach the cell surface but fail to bind LPL in cell-based and cell-free assays. LPL mass and activity in adipose tissue biopsies appear normal, consistent with defective LPL transport rather than synthesis. Family genetics; cell-based and cell-free LPL binding assays; adipose tissue biopsy LPL activity; [35S]methionine incorporation Journal of lipid research High 20026666
2009 GPIHBP1 stabilizes LPL activity and protects it from inhibition by ANGPTL4 and ANGPTL3 in vitro. ANGPTL4 potently inhibits non-stabilized LPL and heparin-stabilized LPL but not GPIHBP1-stabilized LPL. In vivo, Angptl4−/−/Gpihbp1−/− double knockout mice had lower plasma TG than Gpihbp1−/− mice, approaching wild-type levels, confirming the physiological relevance of this protection. In vitro LPL activity assay with GPIHBP1, ANGPTL3, ANGPTL4; double-knockout mouse models; ANGPTL-neutralizing antibody treatment in Gpihbp1−/− mice Journal of lipid research High 19542565
2010 GPIHBP1 binds LPL but does not bind other members of the lipase family (endothelial lipase, hepatic lipase, pancreatic lipase). GPIHBP1 binds apoAV (dependent on the acidic domain, independent of the Ly6 domain). The ability of GPIHBP1-expressing cells to bind chylomicrons is entirely mediated by LPL captured from the medium; GPIHBP1 does not bind chylomicrons directly in the absence of LPL. Cell-based and cell-free binding assays; antibody blocking; cells expressing GPIHBP1 with acidic domain mutations Arteriosclerosis, thrombosis, and vascular biology High 20966398
2010 Homozygous GPIHBP1 C65Y mutation causes chylomicronemia; the mutant protein reaches the cell surface but cannot bind LPL. Patients with homozygous C65Y or Q115P mutations have very low LPL in post-heparin plasma, demonstrating that GPIHBP1 is required for efficient LPL entry into plasma after heparin, consistent with its role in LPL transport. Patient clinical studies; cell-surface expression assays; cell-based LPL binding assay; post-heparin LPL measurement; prolonged heparin infusion in Q115P patient Circulation. Cardiovascular genetics High 20124439
2010 PET scanning with radiolabeled GPIHBP1-specific antibodies revealed that GPIHBP1 is expressed at unexpectedly high levels in lung and liver capillary endothelium, not only in heart/skeletal muscle/adipose tissue. LPL protein was detected in lung despite very low Lpl transcript levels, suggesting GPIHBP1 in the lung captures LPL produced elsewhere. Lung LPL levels were lower in Gpihbp1−/− mice. PET imaging with radiolabeled anti-GPIHBP1 antibodies; immunofluorescence microscopy; tissue LPL quantification in knockout mice; Lpl−/− mice expressing human LPL only in muscle The Journal of biological chemistry High 20889497
2011 GPIHBP1 transports LPL from the subendothelial space across endothelial cells to the capillary lumen. LPL binding to GPIHBP1 requires only LPL's C-terminal domain (residues 298–448); the C-terminal fragment binds GPIHBP1 avidly independent of the N-terminal catalytic domain or full-length homodimer formation. C418Y and E421K mutations in LPL eliminate GPIHBP1 binding without affecting catalytic activity. Cell-based and cell-free LPL-GPIHBP1 binding assays; LPL deletion mutants; furin cleavage mapping; alanine scanning of LPL C-terminal residues Proceedings of the National Academy of Sciences of the United States of America High 21518912
2011 Within the Ly6 domain three-fingered structure of GPIHBP1, alanine scanning identified 12 residues (aside from conserved cysteines) required for LPL binding, with 9 clustered in finger 2. Mutant GPIHBP1 proteins that cannot bind LPL also lack the ability to transport LPL from the basolateral to the apical surface of endothelial cells. Comprehensive alanine-scanning mutagenesis; immunofluorescence cell-surface expression assay; Western blot LPL binding assay; endothelial transcytosis assay The Journal of biological chemistry High 21478160
2011 Homozygous GPIHBP1 deletion (17.5 kb) causes complete GPIHBP1 deficiency and severe chylomicronemia. Intravenous heparin failed to raise LPL in plasma of GPIHBP1-deficient patients (unlike controls), demonstrating that GPIHBP1 is required for heparin-releasable LPL in the human vascular compartment. Array-based copy number analysis; Sanger sequencing; heparin bolus LPL release in GPIHBP1-null patients vs. controls Journal of inherited metabolic disease High 22008945
2012 TRL margination along heart capillaries depends on GPIHBP1 and specifically on LPL bound to GPIHBP1. In Gpihbp1−/− mice, TRLs do not marginate along capillaries. Expression of LPL by endothelial cells (binding to HSPGs) in Gpihbp1−/− mice does not restore TRL margination, demonstrating that GPIHBP1-bound LPL is the primary determinant of TRL margination. Fluorescence microscopy; infrared-dye-labeled lipoprotein quantitative margination assays; EM tomography; cell-culture and in vivo studies with Gpihbp1−/− mice expressing endothelial LPL Cell metabolism High 24726386
2012 GPIHBP1 and LPL move bidirectionally across capillary endothelial cells in vesicles. Transport of LPL across endothelial cells is inhibited by dynasore and genistein (dynamin inhibitor/vesicular transport blockers). EM and dual-axis EM tomography show GPIHBP1 and LPL in membrane invaginations and vesicles. Transport is efficient in the absence of caveolin-1. Live-cell bidirectional transport assays; dynasore/genistein pharmacological inhibition; transmission EM and dual-axis EM tomography; caveolin-1 knockout endothelial cells and in vivo studies Journal of lipid research High 23008484
2012 LPL's C-terminal domain (residues 298–448) is sufficient for GPIHBP1 binding; the N-terminal catalytic domain is dispensable. Full-length homodimers are not required for GPIHBP1 binding. C-terminal fragments of LPL with C418Y or E421K mutations cannot bind GPIHBP1. After denaturation, the C-terminal fragment refolds and restores GPIHBP1 binding. LPL truncation/deletion constructs; furin cleavage mapping; cell-based and cell-free GPIHBP1 binding assays; denaturation/refolding experiment Human molecular genetics High 22493000
2014 Many GPIHBP1 Ly6 domain missense mutations (including disease-causing mutations) cause GPIHBP1 to form disulfide-linked dimers and multimers. Only GPIHBP1 monomers—not dimers or multimers—are capable of binding LPL. W109S mutation abolishes LPL binding without promoting multimerization, suggesting W109 plays a direct role in LPL binding rather than only through structural integrity. Expression in CHO, rat and human endothelial cells, and Drosophila S2 cells; Western blot under non-reducing conditions; cell-based and cell-free LPL binding assays; systematic W109 mutagenesis to 8 other amino acids Circulation research High 25387803
2014 GPIHBP1-S107C mutation (serine-to-cysteine substitution creating an extra cysteine) causes nearly all cell-surface GPIHBP1 to form disulfide-linked dimers and multimers, abolishing LPL binding. Functional studies confirmed only GPIHBP1 monomers bind LPL. Three homozygous patients with this mutation have very low preheparin plasma LPL. Patient genetic analysis; cell-based and insect-cell expression; non-reducing Western blot; cell-based and cell-free LPL binding assays The Journal of biological chemistry High 24847059
2015 ANGPTL4 can bind and inactivate LPL when LPL is complexed with GPIHBP1 on endothelial cell surfaces. Once inactivated by ANGPTL4, LPL dissociates from GPIHBP1. ANGPTL4-inactivated LPL is incapable of re-binding GPIHBP1. The N-terminal coiled-coil domain of ANGPTL4 alone is more potent in inactivating GPIHBP1-bound LPL than full-length ANGPTL4. Cell-based LPL binding and inactivation assays using endothelial cells; ANGPTL4 domain constructs; temperature-dependent binding experiments (4°C vs. 37°C) The Journal of biological chemistry Medium 25809481
2015 GPIHBP1 has two distinct binding sites for LPL: the acidic N-terminal domain forms a tight but short-lived complex (fast on/off rates, salt-sensitive, heparin-displaceable), while the Ly6 domain forms a slower but longer-lasting complex (heparin-resistant). LPL bound to the acidic domain retains affinity for the Ly6 domain and retains capacity to interact with lipoproteins, whereas LPL bound to the Ly6 domain does not. Surface plasmon resonance (SPR); comparative binding studies with isolated N-terminal peptide, Ly6 domain, full-length GPIHBP1, and Q114P mutant; salt and heparin competition assays The Journal of biological chemistry High 25873395
2016 GPIHBP1's intrinsically disordered acidic N-terminal domain stabilizes LPL catalytic activity by mitigating global unfolding of LPL's catalytic domain. Biophysical studies using hydrogen-deuterium exchange/mass spectrometry (HDX-MS) demonstrated that the acidic domain reduces spontaneous unfolding of LPL's hydrolase domain. The LU domain and acidic domain serve distinct roles: the LU domain mediates binding kinetics while the acidic domain prevents unfolding. Hydrogen-deuterium exchange/mass spectrometry (HDX-MS); surface plasmon resonance (SPR); zero-length cross-linking; LPL catalytic activity assays eLife High 26725083
2016 ANGPTL4 inactivates LPL by catalyzing the unfolding of its hydrolase domain (not simply by binding). Binding of LPL to GPIHBP1 renders LPL largely refractory to ANGPTL4-catalyzed inactivation. Both the LU domain and the intrinsically disordered acidic domain of GPIHBP1 are required for this protective effect. A common ANGPTL4 polymorphic variant (associated with lower plasma TG) is less efficient at catalyzing LPL unfolding and its substitution destabilizes its N-terminal α-helix. HDX-MS measuring unfolding of LPL hydrolase domain; LPL activity assays in presence of ANGPTL4 with/without GPIHBP1; GPIHBP1 domain mutants; biophysical analysis of ANGPTL4 variant eLife High 27929370
2016 LPL bound to HSPGs in interstitial spaces is mobile and can detach to move to GPIHBP1 on capillaries. LPL moves from HSPGs on cultured cells to: soluble GPIHBP1 in medium; GPIHBP1-coated agarose beads; and nearby GPIHBP1-expressing cells. Movement requires an intact GPIHBP1 Ly6 domain (W109S mutation blocks transfer) but is largely independent of the acidic domain. In vivo, LPL moves rapidly from adipocyte HSPGs to GPIHBP1-coated beads injected into adipose tissue of Gpihbp1−/− mice. Cell culture LPL transfer assays; GPIHBP1-coated bead capture; in vivo bead injection into brown adipose tissue of Gpihbp1−/− mice; Ly6 domain mutant (W109S) and acidic domain mutant GPIHBP1 Journal of lipid research High 27811232
2016 Monoclonal antibodies targeting GPIHBP1's Ly6 domain (RE3 and RG3) abolish LPL binding, whereas an antibody against the acidic domain (RF4) does not. Both RE3 and RG3 bind with reduced affinity to GPIHBP1-W109S (an Ly6 mutant that abolishes LPL binding), linking the W109 region to the LPL binding interface. Immunohistochemistry confirmed that human GPIHBP1 is expressed exclusively in capillary endothelial cells. Monoclonal antibody development; cell-based LPL binding blocking assays; affinity measurements with Ly6 domain mutants; immunohistochemistry of human tissues Journal of lipid research Medium 27875259
2017 GPIHBP1 autoantibodies (identified in 6 patients with chylomicronemia) block the binding of LPL to GPIHBP1, thereby preventing LPL transport into capillaries, reducing plasma LPL levels, and causing severe hypertriglyceridemia. The autoantibody-mediated chylomicronemia phenotype mirrors genetic GPIHBP1 deficiency. Maternal autoantibodies transferred to a neonate caused transient chylomicronemia. ELISA; Western blot; immunocytochemistry; LPL-GPIHBP1 binding blocking assay with patient plasma The New England journal of medicine High 28402248
2017 ApoC-III potently inhibits triglyceride hydrolysis specifically when LPL is bound to GPIHBP1. TRLs from APOC3 transgenic mice bind normally to GPIHBP1-bound LPL on cells and in vivo, but triglycerides are hydrolyzed more slowly. The inhibitory effect of apoC-III is greater when LPL is bound to GPIHBP1 compared to free LPL. A loss-of-function apoC-III variant (A23T) associated with low plasma TG shows reduced capacity to inhibit both free and GPIHBP1-bound LPL. Cell-based lipolysis assays using GPIHBP1-bound LPL; GPIHBP1-coated agarose bead lipolysis assay; in vivo margination assay in mice; recombinant apoC-III variants Journal of lipid research High 28694296
2017 Mutating a conserved cysteine in mouse GPIHBP1 (C63Y) abolishes LPL binding and causes severe chylomicronemia in vivo, with ~70% reduction in GPIHBP1 levels at the endothelial cell surface. The mutant GPIHBP1 is predominantly monomeric, contrasting with cell culture studies where cysteine mutations cause multimerization. Knock-in mouse model (CRISPR/Cas9 was not stated explicitly but mice harboring C63Y were created); immunohistochemistry; plasma TG measurement; LPL localization Journal of lipid research High 28476858
2018 X-ray crystal structure of the LPL-GPIHBP1 complex was solved at 2.5–3.0 Å. GPIHBP1's LU domain binds to LPL's C-terminal lipid-binding domain largely through hydrophobic interactions. LPL contains a large basic patch spanning its N- and C-terminal domains, positioned to interact with GPIHBP1's acidic domain. In the complex, LPL can be active as a 1:1 monomer rather than requiring a homodimer. X-ray crystallography; co-expression of LPL, soluble GPIHBP1, and LMF1; inhibitor-bound structure resolving LPL lid region; biochemical activity assays Proceedings of the National Academy of Sciences of the United States of America High 30559189 31072929
2018 A conserved tyrosine in the middle of GPIHBP1's intrinsically disordered acidic domain undergoes posttranslational O-sulfation. This tyrosine sulfation increases the affinity of GPIHBP1-LPL interactions and enhances GPIHBP1's ability to protect LPL against ANGPTL4-catalyzed unfolding. The acidic IDR also increases the probability of GPIHBP1-LPL encounters via electrostatic steering, increasing the association rate constant (kon) for LPL binding by >250-fold. Mass spectrometry identification of sulfotyrosine; surface plasmon resonance (kon/koff measurements); LPL activity protection assays; biophysical characterization of IDR conformation Proceedings of the National Academy of Sciences of the United States of America High 29899144
2018 An upstream enhancer element located ~3.6 kb upstream from exon 1 of mouse Gpihbp1 regulates tissue-specific Gpihbp1 expression. Deletion of this enhancer (CRISPR/Cas9) reduced Gpihbp1 expression by >90% in liver and ~50% in heart/brown adipose tissue. Reduced GPIHBP1 caused partial LPL mislocalization (increased LPL in interstitial spaces) in compound heterozygotes, but did not cause hypertriglyceridemia. CRISPR/Cas9 enhancer deletion; quantitative RT-PCR; immunofluorescence microscopy for LPL localization; plasma TG measurement Journal of lipid research Medium 30598475
2019 GPIHBP1 is expressed in glioma capillaries (unlike normal brain capillaries, which lack GPIHBP1) and captures locally produced LPL. GPIHBP1 in glioma capillaries enables margination of TRLs along glioma capillaries, and NanoSIMS imaging confirmed uptake of TRL-derived lipid nutrients by surrounding glioma cells, providing a source of lipid energy for tumors. Immunohistochemistry of mouse and human glioma; NanoSIMS isotope imaging; TRL margination assay in glioma-bearing mice; LPL capture by GPIHBP1 in glioma capillaries eLife Medium 31169500
2020 In a NanoBiT split-luciferase assay monitoring LPL-GPIHBP1 binding on endothelial cells in real time, ANGPTL4 and ANGPTL3-ANGPTL8 complexes disrupt LPL-GPIHBP1 interactions. Chylomicrons can dissociate LPL from GPIHBP1, and this dissociation is mediated in part by fatty acids produced during lipolysis. Exogenous inhibitors (tyloxapol, poloxamer-407, tetrahydrolipstatin) did not disrupt LPL-GPIHBP1 binding. NanoBiT split-luciferase real-time binding assay on endothelial cells; ANGPTL4, ANGPTL3-8 complex, and chylomicron addition assays; fatty acid competition Journal of lipid research Medium 32029511
2022 GPIHBP1's acidic domain (AD) serves three distinct functions established experimentally: (1) it accelerates LPL binding kinetics via electrostatic steering; (2) it preserves LPL catalytic activity by preventing unfolding of LPL's catalytic domain; and (3) by sheathing LPL's basic patch, the AD enables LPL-GPIHBP1 complexes to move across endothelial cells to the capillary lumen—without the AD, GPIHBP1-bound LPL is trapped by interactions with heparan sulfate proteoglycans on the abluminal surface. Biophysical binding assays; LPL activity measurements; in vivo mouse studies with AD-mutant GPIHBP1; HSPG interaction studies Proceedings of the National Academy of Sciences of the United States of America High 36037340
2023 LPL transported into capillaries by GPIHBP1 can detach from GPIHBP1 and move into the endothelial glycocalyx. By confocal microscopy, immunogold EM, and NanoSIMS, LPL detected by a GPIHBP1-binding-blocking antibody (88B8, which cannot detect GPIHBP1-bound LPL) is located in the glycocalyx, distant from GPIHBP1 on the plasma membrane. This glycocalyx-localized LPL mediates TRL margination and is active in TRL processing, delivering lipids to adjacent parenchymal cells. Monoclonal antibody 88B8 (GPIHBP1-binding-blocking epitope); confocal microscopy; immunogold electron microscopy; NanoSIMS imaging; in vivo functional lipid delivery assays Proceedings of the National Academy of Sciences of the United States of America High 37871217
2015 VEGF, secreted by cardiomyocytes in response to hyperglycemia-triggered heparanase release, induces GPIHBP1 expression in endothelial cells via Notch signaling (Delta-like ligand 4 augmentation and nuclear translocation of the Notch intracellular domain), thereby increasing LPL shuttling across endothelial cells in the diabetic heart. High-glucose EC culture; heparanase treatment; VEGF neutralizing antibody; Notch pathway inhibition; cardiomyocyte-EC co-culture; in vivo severely diabetic animal model with VEGF attenuation Arteriosclerosis, thrombosis, and vascular biology Medium 26586663

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2012 Mutations in LPL, APOC2, APOA5, GPIHBP1 and LMF1 in patients with severe hypertriglyceridaemia. Journal of internal medicine 204 22239554
2014 The GPIHBP1-LPL complex is responsible for the margination of triglyceride-rich lipoproteins in capillaries. Cell metabolism 130 24726386
2009 Chylomicronemia with a mutant GPIHBP1 (Q115P) that cannot bind lipoprotein lipase. Arteriosclerosis, thrombosis, and vascular biology 128 19304573
2017 Autoantibodies against GPIHBP1 as a Cause of Hypertriglyceridemia. The New England journal of medicine 126 28402248
2019 GPIHBP1 and Lipoprotein Lipase, Partners in Plasma Triglyceride Metabolism. Cell metabolism 113 31269429
2016 The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding. eLife 111 27929370
2009 GPIHBP1 stabilizes lipoprotein lipase and prevents its inhibition by angiopoietin-like 3 and angiopoietin-like 4. Journal of lipid research 105 19542565
2009 Mutation of conserved cysteines in the Ly6 domain of GPIHBP1 in familial chylomicronemia. Journal of lipid research 102 20026666
2016 The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain. eLife 93 26725083
2010 Chylomicronemia with low postheparin lipoprotein lipase levels in the setting of GPIHBP1 defects. Circulation. Cardiovascular genetics 92 20124439
2011 GPIHBP1, an endothelial cell transporter for lipoprotein lipase. Journal of lipid research 86 21844202
2018 Structure of the lipoprotein lipase-GPIHBP1 complex that mediates plasma triglyceride hydrolysis. Proceedings of the National Academy of Sciences of the United States of America 82 30559189
2002 Expression cloning and characterization of a novel glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein, GPI-HBP1. The Journal of biological chemistry 82 12496272
2011 Deletion of GPIHBP1 causing severe chylomicronemia. Journal of inherited metabolic disease 81 22008945
2008 The acidic domain of GPIHBP1 is important for the binding of lipoprotein lipase and chylomicrons. The Journal of biological chemistry 79 18713736
2016 GPIHBP1 and Plasma Triglyceride Metabolism. Trends in endocrinology and metabolism: TEM 68 27185325
2009 Highly conserved cysteines within the Ly6 domain of GPIHBP1 are crucial for the binding of lipoprotein lipase. The Journal of biological chemistry 68 19726683
2012 Linking nutritional regulation of Angptl4, Gpihbp1, and Lmf1 to lipoprotein lipase activity in rodent adipose tissue. BMC physiology 67 23176178
2007 GPIHBP1: an endothelial cell molecule important for the lipolytic processing of chylomicrons. Current opinion in lipidology 67 17620854
2008 Abnormal patterns of lipoprotein lipase release into the plasma in GPIHBP1-deficient mice. The Journal of biological chemistry 65 18845532
2012 Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells. Journal of lipid research 64 23008484
2007 Homozygous missense mutation (G56R) in glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPI-HBP1) in two siblings with fasting chylomicronemia (MIM 144650). Lipids in health and disease 62 17883852
2010 Modulation of plasma TG lipolysis by Angiopoietin-like proteins and GPIHBP1. Biochimica et biophysica acta 61 20056168
2015 Angiopoietin-like 4 Modifies the Interactions between Lipoprotein Lipase and Its Endothelial Cell Transporter GPIHBP1. The Journal of biological chemistry 58 25809481
2018 A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase. Proceedings of the National Academy of Sciences of the United States of America 56 29899144
2011 Childhood-onset chylomicronaemia with reduced plasma lipoprotein lipase activity and mass: identification of a novel GPIHBP1 mutation. Journal of internal medicine 56 21314738
2011 GPIHBP1 C89F neomutation and hydrophobic C-terminal domain G175R mutation in two pedigrees with severe hyperchylomicronemia. The Journal of clinical endocrinology and metabolism 54 21816778
2019 Structure of lipoprotein lipase in complex with GPIHBP1. Proceedings of the National Academy of Sciences of the United States of America 52 31072929
2011 Mutations in lipoprotein lipase that block binding to the endothelial cell transporter GPIHBP1. Proceedings of the National Academy of Sciences of the United States of America 51 21518912
2011 Assessing the role of the glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) three-finger domain in binding lipoprotein lipase. The Journal of biological chemistry 50 21478160
2008 The expression of GPIHBP1, an endothelial cell binding site for lipoprotein lipase and chylomicrons, is induced by peroxisome proliferator-activated receptor-gamma. Molecular endocrinology (Baltimore, Md.) 50 18787041
2014 GPIHBP1 missense mutations often cause multimerization of GPIHBP1 and thereby prevent lipoprotein lipase binding. Circulation research 49 25387803
2008 GPIHBP1, a GPI-anchored protein required for the lipolytic processing of triglyceride-rich lipoproteins. Journal of lipid research 48 18854402
2017 Apolipoprotein C-III inhibits triglyceride hydrolysis by GPIHBP1-bound LPL. Journal of lipid research 47 28694296
2014 Multimerization of glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) and familial chylomicronemia from a serine-to-cysteine substitution in GPIHBP1 Ly6 domain. The Journal of biological chemistry 47 24847059
2020 Chylomicronemia from GPIHBP1 autoantibodies. Journal of lipid research 43 32948662
2011 Lipoprotein lipase deficiency in chronic kidney disease is accompanied by down-regulation of endothelial GPIHBP1 expression. Clinical and experimental nephrology 43 22009636
2010 Binding preferences for GPIHBP1, a glycosylphosphatidylinositol-anchored protein of capillary endothelial cells. Arteriosclerosis, thrombosis, and vascular biology 43 20966398
2016 Mobility of "HSPG-bound" LPL explains how LPL is able to reach GPIHBP1 on capillaries. Journal of lipid research 37 27811232
2007 Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution. Biochimica et biophysica acta 36 17997385
2015 Cardiomyocyte VEGF Regulates Endothelial Cell GPIHBP1 to Relocate Lipoprotein Lipase to the Coronary Lumen During Diabetes Mellitus. Arteriosclerosis, thrombosis, and vascular biology 33 26586663
2010 Unexpected expression pattern for glycosylphosphatidylinositol-anchored HDL-binding protein 1 (GPIHBP1) in mouse tissues revealed by positron emission tomography scanning. The Journal of biological chemistry 33 20889497
2014 Familial chylomicronemia syndrome and response to medium-chain triglyceride therapy in an infant with novel mutations in GPIHBP1. Journal of clinical lipidology 32 25499947
2017 GPIHBP1 autoantibodies in a patient with unexplained chylomicronemia. Journal of clinical lipidology 30 28666713
2021 GPIHBP1 and ANGPTL4 Utilize Protein Disorder to Orchestrate Order in Plasma Triglyceride Metabolism and Regulate Compartmentalization of LPL Activity. Frontiers in cell and developmental biology 29 34336854
2011 Reciprocal metabolic perturbations in the adipose tissue and liver of GPIHBP1-deficient mice. Arteriosclerosis, thrombosis, and vascular biology 28 22173228
2008 Glycosylation of Asn-76 in mouse GPIHBP1 is critical for its appearance on the cell surface and the binding of chylomicrons and lipoprotein lipase. Journal of lipid research 28 18340083
2013 Novel combined GPIHBP1 mutations in a patient with hypertriglyceridemia associated with CAD. Journal of atherosclerosis and thrombosis 27 23831619
2009 GPIHBP1 and lipolysis: an update. Current opinion in lipidology 27 19369870
2015 Novel mutations in the GPIHBP1 gene identified in 2 patients with recurrent acute pancreatitis. Journal of clinical lipidology 26 26892125
2022 A protein of capillary endothelial cells, GPIHBP1, is crucial for plasma triglyceride metabolism. Proceedings of the National Academy of Sciences of the United States of America 24 36037340
2014 A 3-day-old neonate with severe hypertriglyceridemia from novel mutations of the GPIHBP1 gene. Journal of clinical lipidology 24 25911085
2016 Clinical and genetic features of 3 patients with familial chylomicronemia due to mutations in GPIHBP1 gene. Journal of clinical lipidology 23 27578123
2012 Chylomicronemia mutations yield new insights into interactions between lipoprotein lipase and GPIHBP1. Human molecular genetics 23 22493000
2017 An enzyme-linked immunosorbent assay for measuring GPIHBP1 levels in human plasma or serum. Journal of clinical lipidology 22 29246728
2020 Intermittent chylomicronemia caused by intermittent GPIHBP1 autoantibodies. Journal of clinical lipidology 21 32107180
2021 A novel GPIHBP1 mutation related to familial chylomicronemia syndrome: A series of cases. Atherosclerosis 20 33706081
2014 Whole-exome sequencing reveals GPIHBP1 mutations in infantile colitis with severe hypertriglyceridemia. Journal of pediatric gastroenterology and nutrition 20 24614124
2023 The lipoprotein lipase that is shuttled into capillaries by GPIHBP1 enters the glycocalyx where it mediates lipoprotein processing. Proceedings of the National Academy of Sciences of the United States of America 19 37871217
2018 GPIHBP1 autoantibody syndrome during interferon β1a treatment. Journal of clinical lipidology 19 30514621
2011 Comparative studies of glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1: evidence for a eutherian mammalian origin for the GPIHBP1 gene from an LY6-like gene. 3 Biotech 19 22582156
2018 Lipoprotein lipase transporter GPIHBP1 and triglyceride-rich lipoprotein metabolism. Clinica chimica acta; international journal of clinical chemistry 17 30218660
2020 A novel NanoBiT-based assay monitors the interaction between lipoprotein lipase and GPIHBP1 in real time. Journal of lipid research 16 32029511
2017 Mutating a conserved cysteine in GPIHBP1 reduces amounts of GPIHBP1 in capillaries and abolishes LPL binding. Journal of lipid research 16 28476858
2016 Type 1 hyperlipoproteinemia in a child with large homozygous deletion encompassing GPIHBP1. Journal of clinical lipidology 16 27578137
2016 Monoclonal antibodies that bind to the Ly6 domain of GPIHBP1 abolish the binding of LPL. Journal of lipid research 16 27875259
2019 GPIHBP1 expression in gliomas promotes utilization of lipoprotein-derived nutrients. eLife 15 31169500
2015 Evidence for Two Distinct Binding Sites for Lipoprotein Lipase on Glycosylphosphatidylinositol-anchored High Density Lipoprotein-binding Protein 1 (GPIHBP1). The Journal of biological chemistry 15 25873395
2014 Type 1 hyperlipoproteinemia due to a novel deletion of exons 3 and 4 in the GPIHBP1 gene. Atherosclerosis 15 24589565
2014 Endothelial cells respond to hyperglycemia by increasing the LPL transporter GPIHBP1. American journal of physiology. Endocrinology and metabolism 15 24735886
2012 Localization of lipoprotein lipase and GPIHBP1 in mouse pancreas: effects of diet and leptin deficiency. BMC physiology 15 23186339
2022 GPIHBP1 autoantibody is an independent risk factor for the recurrence of hypertriglyceridemia-induced acute pancreatitis. Journal of clinical lipidology 14 36064883
2019 Gpihbp1 deficiency accelerates atherosclerosis and plaque instability in diabetic Ldlr-/- mice. Atherosclerosis 13 30721842
2020 Management of a pregnant patient with chylomicronemia from a novel mutation in GPIHBP1: a case report. BMC pregnancy and childbirth 12 32375710
2018 Impaired thermogenesis and sharp increases in plasma triglyceride levels in GPIHBP1-deficient mice during cold exposure. Journal of lipid research 12 29449313
2017 Lipoprotein lipase reaches the capillary lumen in chickens despite an apparent absence of GPIHBP1. JCI insight 12 29046479
2023 AAV-mediated hepatic LPL expression ameliorates severe hypertriglyceridemia and acute pancreatitis in Gpihbp1 deficient mice and rats. Molecular therapy : the journal of the American Society of Gene Therapy 11 37974401
2018 A novel mutation in GPIHBP1 causes familial chylomicronemia syndrome. Journal of clinical lipidology 11 29452893
2017 A 1-month-old infant with chylomicronemia due to GPIHBP1 gene mutation treated by plasmapheresis. Annals of pediatric endocrinology & metabolism 11 28443263
2017 Functional validation of GPIHBP1 and identification of a functional mutation in GPIHBP1 for milk fat traits in dairy cattle. Scientific reports 11 28819221
2016 An LPL-specific monoclonal antibody, 88B8, that abolishes the binding of LPL to GPIHBP1. Journal of lipid research 11 27494936
2014 Equivalent binding of wild-type lipoprotein lipase (LPL) and S447X-LPL to GPIHBP1, the endothelial cell LPL transporter. Biochimica et biophysica acta 11 24704550
2018 An ELISA for quantifying GPIHBP1 autoantibodies and making a diagnosis of the GPIHBP1 autoantibody syndrome. Clinica chimica acta; international journal of clinical chemistry 10 30287259
2019 Association between skeletal muscle mass and serum concentrations of lipoprotein lipase, GPIHBP1, and hepatic triglyceride lipase in young Japanese men. Lipids in health and disease 9 30947712
2019 Genetic variants in the LPL and GPIHBP1 genes, in patients with severe hypertriglyceridaemia, detected with high resolution melting analysis. Clinica chimica acta; international journal of clinical chemistry 9 31669931
2023 The GPIHBP1-LPL complex and its role in plasma triglyceride metabolism: Insights into chylomicronemia. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 7 37951027
2018 Novel GPIHBP1-independent pathway for clearance of plasma TGs in Angptl4-/-Gpihbp1-/- mice. Journal of lipid research 7 29739862
2018 An upstream enhancer regulates Gpihbp1 expression in a tissue-specific manner. Journal of lipid research 7 30598475
2009 Some things just have to be done in vivo: GPIHBP1, caloric delivery, and the generation of remnant lipoproteins. Arteriosclerosis, thrombosis, and vascular biology 7 19458350
2017 The effect of combined diet and exercise intervention on body weight and the serum GPIHBP1 concentration in overweight/obese middle-aged women. Clinica chimica acta; international journal of clinical chemistry 6 29056530
2023 Molecular genetic testing and measurement of levels of GPIHBP1 autoantibodies in patients with severe hypertriglyceridemia: The importance of identifying the underlying cause of hypertriglyceridemia. Journal of clinical lipidology 5 37981531
2022 A case of hyperchylomicronemia associated with GPIHBP1 autoantibodies and fluctuating thyroid autoimmune disease. Journal of clinical lipidology 5 36402671
2018 Decreased GPIHBP1 protein levels in visceral adipose tissue partly underlie the hypertriglyceridemic phenotype in insulin resistance. PloS one 5 30408040
2023 Severe hypertriglyceridemia caused by Gpihbp1 deficiency facilitates vascular remodeling through increasing endothelial activation and oxidative stress. Biochimica et biophysica acta. Molecular and cell biology of lipids 4 37172802
2022 Circulating GPIHBP1 levels and microvascular complications in patients with type 2 diabetes: A cross-sectional study. Journal of clinical lipidology 4 35101360
2022 A homozygous variant in the GPIHBP1 gene in a child with severe hypertriglyceridemia and a systematic literature review. Frontiers in genetics 4 36051701
2022 Biochemical, Clinical, and Genetic Characteristics of Mexican Patients with Primary Hypertriglyceridemia, Including the First Case of Hyperchylomicronemia Syndrome Due to GPIHBP1 Deficiency. International journal of molecular sciences 4 36613909
2020 The antagonic behavior of GPIHBP1 between EAT and circulation does not reflect lipolytic enzymes levels in the tissue and serum from coronary patients. Clinica chimica acta; international journal of clinical chemistry 4 32771483
2025 KLF13 promotes esophageal cancer progression and regulates triacylglyceride and free fatty acid metabolism through GPIHBP1. Cell death & disease 3 40450000
2022 Anti-GPIHBP1 Antibody-Positive Autoimmune Hyperchylomicronemia and Immune Thrombocytopenia. Journal of atherosclerosis and thrombosis 3 35185060

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