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Dietary fats are packaged by intestine into triglyceride-rich lipoproteins called chylomicrons. Additionally we are shipping GPIHBP1 Kits (7) and GPIHBP1 Proteins (5) and many more products for this protein.
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GPIHBP1 mutations should be considered in neonates with chylomicronemia negative for mutations in LPL (show LCP1 Antibodies) gene
the two domains of GPIHBP1 interact independently with LPL (show LCP1 Antibodies) and the functionality of LPL (show LCP1 Antibodies) depends on its localization on GPIHBP1
No GPIHBP1 mutations were identified in a cohort of patients with diabetic lipemia.
GPIHBP1 missense mutations leading to protein multimerization prevent lipoprotein lipase (show LPL Antibodies) binding.
Homozygosity for a deletion of exons 3 and 4 of GPIHBP1 results in Type 1 hyperlipoproteinemia.
an extra cysteine in the GPIHBP1 Ly6 motif results in multimerization of GPIHBP1, defective LPL (show LCP1 Antibodies) binding, and severe hypertriglyceridemia.
Wild-type lipoprotein lipase (LPL (show LPL Antibodies)) and a mutated (S447X-LPL (show LCP1 Antibodies)) protein bind to the endothelial cell LPL (show LCP1 Antibodies) transporter GPIHBP1 with equal efficiency.
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 (show LCP1 Antibodies) defective alleles.
Mutations in GPIHBP1 are rare but the associated clinical phenotype of hypertriglyceridaemia is severe.
analysis of a neonate with complete GPIHBP1 deficiency due to homozygosity for a deletion of GPIHBP1 [case report]
Laminin regulates PDGFRbeta cell differentiation, fate determination, cell stemness and muscle development via gpihbp1.
the two domains of GPIHBP1 interact independently with LPL (show LPL Antibodies) and the functionality of LPL (show LPL Antibodies) depends on its localization on GPIHBP1
TRL margination depends on LPL (show LPL Antibodies) bound to GPIHBP1.
In adipose tissue, Gpihbp1 levels increases rapidly during fasting, when lipoprotein lipase (show LPL Antibodies) activity decreases.
Neither a high fat diet nor fasting/re-feeding markedly altered the distribution pattern of LPL (show LPL Antibodies) or GPIHBP1 in mouse pancreas.
The GPIHBP1 and LPL (show LPL Antibodies) move bidirectionally across endothelial cells in vesicles and that transport is efficient even when caveolin-1 (show CAV1 Antibodies) is absent.
analysis of glycosylphosphatidylinositol-anchored HDL-binding protein (show HDLBP Antibodies) 1 (GPIHBP1) expression in mouse tissues revealed by positron emission tomography scanning
Intravenously injected apoA-V (show APOA5 Antibodies) rHDL significantly lowers plasma TG in an apoA-V (show APOA5 Antibodies) deficient mouse model and requires gpihbp1.
GPIHBP1 is located at the basolateral surface of capillary endothelial cells and actively transports LPL (show LPL Antibodies) across endothelial cells.
Like ANGPTL4 (show ANGPTL4 Antibodies), ANGPTL3 (show ANGPTL3 Antibodies) inhibited nonstabilized LPL (show LPL Antibodies) but not GPIHBP1-stabilized LPL (show LPL Antibodies)
Dietary fats are packaged by intestine into triglyceride-rich lipoproteins called chylomicrons. The triglycerides in chylomicrons are hydrolyzed by lipoprotein lipase (LPL: MIM 609708) along the luminal surface of capillaries, mainly in heart, skeletal muscle, and adipose tissue. GPIHBP1 is a capillary endothelial cell protein that provides a platform for LPL-mediated processing of chylomicrons (Beigneux et al., 2007
glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
, GPI-anchored HDL-binding protein 1
, glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1
, GPI anchored high density lipoprotein binding protein 1
, high density lipoprotein-binding protein 1