Recombinant Human Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1)

1. the negatively charged IDR of GPIHBP1 traverses a vast space, facilitating capture of LPL by capillary endothelial cells and simultaneously contributing to GPIHBP1's ability to preserve LPL structure and activity. PMID: 29899144
2. The increased GPIHBP1 was significantly associated with decreased body weight. PMID: 29056530
3. apoC-III potently inhibits triglyceride hydrolysis when LPL is bound to GPIHBP1 PMID: 28694296
4. mutation of a conserved cysteine in GPIHBP1 abolishes the ability of GPIHBP1 to bind LPL PMID: 28476858
5. One of 33 patients with unexplained chylomicronemia had the GPIHBP1 autoantibody syndrome PMID: 28666713
6. Triglyceride-raising variant alleles of the GPIHBP1, encoding glycosylphosphatidylinositol-anchored HDL-binding protein 1,associated with clinical Cardiovascular endpoints. PMID: 28534127
7. The s now show: (1) that ANGPTL4 inactivates LPL by catalyzing the unfolding of its hydrolase domain; (2) that binding to GPIHBP1 renders LPL largely refractory to this inhibition; and (3) that both the LU domain and the intrinsically disordered acidic domain of GPIHBP1 are required for this protective effect. PMID: 27929370
8. familial chylomicronemia due to mutations in GPIHBP1 gene PMID: 27578123
9. mAbs RE3 and RG3 bound with reduced affinity to a mutant GPIHBP1 containing an Ly6 domain mutation (W109S) that abolishes LPL binding. Immunohistochemistry studies with the GPIHBP1 mAbs revealed that human GPIHBP1 is expressed only in capillary endothelial cells. Finally, we created an ELISA that detects GPIHBP1 in human plasma. PMID: 27875259
10. The binding of both antibody 88B8 and GPIHBP1 to LPL depends on large segments of LPL's carboxyl-terminal domain. PMID: 27494936
11. An LPL structural model suggests that the LPL S447X truncation exposes residues implicated in LPL binding to lipoprotein binding uptake receptors, such as GPIHBP1. PMID: 27984852
12. The acidic domain of GPIHBP1 stabilizes LPL catalytic activity by mitigating the global unfolding of LPL's catalytic domain. PMID: 26725083
13. 2 novel GPIHBP1 missense mutations in 2 unrelated patients as the cause of their severe hypertriglyceridemia PMID: 26892125
14. GPIHBP1 mutations should be considered in neonates with chylomicronemia negative for mutations in LPL gene PMID: 25911085
15. the two domains of GPIHBP1 interact independently with LPL and the functionality of LPL depends on its localization on GPIHBP1 PMID: 25873395
16. No GPIHBP1 mutations were identified in a cohort of patients with diabetic lipemia. PMID: 25131724
17. patient with type I hyperlipoproteinemia harbored homozygous mutation in case series PMID: 24793350
18. GPIHBP1 missense mutations leading to protein multimerization prevent lipoprotein lipase binding. PMID: 25387803
19. Homozygosity for a deletion of exons 3 and 4 of GPIHBP1 results in Type 1 hyperlipoproteinemia. PMID: 24589565
20. an extra cysteine in the GPIHBP1 Ly6 motif results in multimerization of GPIHBP1, defective LPL binding, and severe hypertriglyceridemia. PMID: 24847059
21. Wild-type lipoprotein lipase (LPL) and a mutated (S447X-LPL) protein bind to the endothelial cell LPL transporter GPIHBP1 with equal efficiency. PMID: 24704550
22. A polymorphism in the GPIHBP1 gene promoter was associated with an increased risk of hypertriglyceridemia and had an additive effect on the risk conferred by LPL defective alleles. PMID: 21978733
23. Mutations in GPIHBP1 are rare but the associated clinical phenotype of hypertriglyceridaemia is severe. PMID: 22239554
24. analysis of a neonate with complete GPIHBP1 deficiency due to homozygosity for a deletion of GPIHBP1 [case report] PMID: 22008945
25. Expression of glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1 tended to be higher in young healthy subjects than in subjects with type 2 diabetes mellitus or Colder control subjects PMID: 22078753
26. function and genetics of GPIHBP1 in lipoprotein lipase transport PMID: 21844202
27. we first report a mutation of the hydrophobic C-terminal domain that impairs GPIHBP1 membrane targeting PMID: 21816778
28. Findings provide further evidence that GPIHBP1 is involved in the catabolism of triglyceride-rich lipoproteins and plays a role in childhood-onset chylomicronaemia. PMID: 21314738
29. the Ly6 domain of GPIHBP1 is important for the ability of GPIHBP1 to bind and transport LPL. PMID: 21478160
30. report that two LPL missense mutations initially identified in patients with chylomicronemia, C418Y and E421K, abolish LPL's ability to bind to GPIHBP1 without interfering with LPL catalytic activity or binding to heparin PMID: 21518912
31. GPIHBP1 binds lipoprotein lipase but does not bind other lipase family members. GPIHBP1 binds apoAV but does not bind apoAI or high-density lipoprotein. GPIHBP1 binding to chylomicrons is mediated by lipoprotein lipase. PMID: 20966398
32. The conserved cysteines in the Ly6 domain are crucial for GPIHBP1 function. PMID: 20026666
33. Observational study of gene-disease association. (HuGE Navigator) PMID: 20237496
34. GPIHBP1 functions as an LPL stabilizer PMID: 19542565
35. a very rare GPIHBP1 missense mutation appears to be associated with severe hypertriglyceridemia and chylomicronemia. PMID: 17883852
36. Data show that the G56R substitution did not affect the ability of GPIHBP1 to reach the cell surface, nor did the amino acid substitution have any discernible effect on the binding of lipoprotein lipase, chylomicrons, or apo-AV. PMID: 17997385
37. the acidic domain of GPIHBP1 is important and electrostatic interactions play a key role in ligand binding PMID: 18713736
38. Case Report: Chylomicronemia with a mutant GPIHBP1 (Q115P) that cannot bind lipoprotein lipase. PMID: 19304573

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HGNC: 24945

OMIM: 612757

KEGG: hsa:338328

STRING: 9606.ENSP00000329266

UniGene: Hs.426410