Glycosylphosphatidylinositol Anchored High Density Lipoprotein Binding Protein 1 (GPIHBP1) ELISA Kits

Cow (Bovine) Glycosylphosphatidylinositol Anchored High Density Lipoprotein Binding Protein 1 (GPIHBP1) interaction partners

1. Data indicate that lipoprotein receptor GPIHBP1 (GPIHBP1) could be a strong candidate gene for milk fat content traits.

Human Glycosylphosphatidylinositol Anchored High Density Lipoprotein Binding Protein 1 (GPIHBP1) interaction partners

1. we assessed visceral adipose tissue GPIHBP1 protein expression in type 2 diabetes Lepr db/db mouse model as well as in subjects with ranging levels of insulin resistance. We report that insulin reduces the expression of GPIHBP1 protein in HMVECs. Furthermore, GPIHBP1 protein expression in visceral adipose tissue in Lepr db/db mice is significantly reduced as is the active monomeric form of GPIHBP1 as compared to Leprdb/m

2. The LPL-GPIHBP1 structure provides insights into mutations causing chylomicronemia.

3. The GPIHBP1 gene, protein, its expression and function focus on its regulation and provides critical evidence supporting its role in triglyceride-rich lipoprotein (TRL) metabolism.

4. 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.

5. The increased GPIHBP1 was significantly associated with decreased body weight.

6. apoC-III potently inhibits triglyceride hydrolysis when LPL is bound to GPIHBP1

7. mutation of a conserved cysteine in GPIHBP1 abolishes the ability of GPIHBP1 to bind LPL

8. One of 33 patients with unexplained chylomicronemia had the GPIHBP1 autoantibody syndrome

9. Triglyceride-raising variant alleles of the GPIHBP1, encoding glycosylphosphatidylinositol-anchored HDL-binding protein 1,associated with clinical Cardiovascular endpoints.

10. The authors 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.

11. familial chylomicronemia due to mutations in GPIHBP1 gene

12. 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.

13. The binding of both antibody 88B8 and GPIHBP1 to LPL depends on large segments of LPL's carboxyl-terminal domain.

14. An LPL structural model suggests that the LPL S447X truncation exposes residues implicated in LPL binding to lipoprotein binding uptake receptors, such as GPIHBP1.

15. The acidic domain of GPIHBP1 stabilizes LPL catalytic activity by mitigating the global unfolding of LPL's catalytic domain.

16. 2 novel GPIHBP1 missense mutations in 2 unrelated patients as the cause of their severe hypertriglyceridemia

17. GPIHBP1 mutations should be considered in neonates with chylomicronemia negative for mutations in LPL gene

18. the two domains of GPIHBP1 interact independently with LPL and the functionality of LPL depends on its localization on GPIHBP1

19. No GPIHBP1 mutations were identified in a cohort of patients with diabetic lipemia.

20. patient with type I hyperlipoproteinemia harbored homozygous mutation in case series

Mouse (Murine) Glycosylphosphatidylinositol Anchored High Density Lipoprotein Binding Protein 1 (GPIHBP1) interaction partners

1. GPIHBP1-independent pathway for clearance of plasma TGs in Angptl4(-/-)Gpihbp1(-/-) mice

2. we assessed visceral adipose tissue GPIHBP1 protein expression in type 2 diabetes Lepr db/db mouse model as well as in subjects with ranging levels of insulin resistance. We report that insulin reduces the expression of GPIHBP1 protein in HMVECs. Furthermore, GPIHBP1 protein expression in visceral adipose tissue in Lepr db/db mice is significantly reduced as is the active monomeric form of GPIHBP1 as compared to Leprdb/m

3. 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.

4. mutation of a conserved cysteine in GPIHBP1 abolishes the ability of GPIHBP1 to bind LPL

5. LPL moved quickly from heparan sulfate proteoglycans (HSPGs) on adipocytes to GPIHBP1-coated beads, thereby depleting LPL stores on the surface of adipocytes. We conclude that HSPG-bound LPL in the interstitial spaces of tissues is mobile, allowing the LPL to move to GPIHBP1 on endothelial cells

6. An LPL structural model suggests that the LPL S447X truncation exposes residues implicated in LPL binding to lipoprotein binding uptake receptors, such as GPIHBP1.

7. Laminin regulates PDGFRbeta cell differentiation, fate determination, cell stemness and muscle development via gpihbp1.

8. the two domains of GPIHBP1 interact independently with LPL and the functionality of LPL depends on its localization on GPIHBP1

9. TRL margination depends on LPL bound to GPIHBP1.

10. In adipose tissue, Gpihbp1 levels increases rapidly during fasting, when lipoprotein lipase activity decreases.

11. Neither a high fat diet nor fasting/re-feeding markedly altered the distribution pattern of LPL or GPIHBP1 in mouse pancreas.

12. The GPIHBP1 and LPL move bidirectionally across endothelial cells in vesicles and that transport is efficient even when caveolin-1 is absent.

13. analysis of glycosylphosphatidylinositol-anchored HDL-binding protein 1 (GPIHBP1) expression in mouse tissues revealed by positron emission tomography scanning

14. Intravenously injected apoA-V rHDL significantly lowers plasma TG in an apoA-V deficient mouse model and requires gpihbp1.

15. GPIHBP1 is located at the basolateral surface of capillary endothelial cells and actively transports LPL across endothelial cells.

16. Like ANGPTL4, ANGPTL3 inhibited nonstabilized LPL but not GPIHBP1-stabilized LPL

17. GPIHBP1 is required for the lipolytic processing of both apo-B48- and apo-B100-containing lipoproteins

18. GPIHBP1 is an important platform for the LpL-mediated processing of chylomicrons in capillaries.

19. Eliminating the N-glycosylation site in a truncated soluble version of GPIHBP1 causes a modest reduction in the secretion of the protein. These studies demonstrate that N-glycosylation of GPIHBP1 is important for the trafficking of GPIHBP1 to cell surface

20. the acidic domain of GPIHBP1 is important and electrostatic interactions play a key role in ligand binding