ArticleThe Journal of biological chemistry2008
The acidic domain of GPIHBP1 is important for the binding of lipoprotein lipase and chylomicrons.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers, 1 of them a synthesis that pooled it.
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Who cites it
65 citing papers in PubMed, 1 synthesis or guideline pooled it, 84 citations in OpenAlex.
- Evaluation and treatment of hypertriglyceridemia: an Endocrine Society clinical practice guideline.The Journal of clinical endocrinology and metabolism · 2012Guideline
- Clinical and functional evidence supporting pathogenicity of a novel APOA5 variant in familial chylomicronemia syndrome.Archives of endocrinology and metabolism · 2026Article
- GPIHBP1 on oligodendrocytes binds lipoprotein lipase within the human brain.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Reversibly reduced lipoprotein lipase in APOA5 c.553G>T-related hypertriglyceridemia successfully treated with pemafibrate.Endocrinology, diabetes & metabolism case reports · 2026Article
- KLF13 promotes esophageal cancer progression and regulates triacylglyceride and free fatty acid metabolism through GPIHBP1.Cell death & disease · 2025Article
- Review
- Practical Approaches to Managing Dyslipidemia in Patients With Metabolic Dysfunction-Associated Steatotic Liver Disease.Journal of lipid and atherosclerosis · 2025Review
- 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 · 2024Article
- Lipoprotein lipase as a target for obesity/diabetes related cardiovascular disease.Journal of pharmacy & pharmaceutical sciences : a publication of the Canadian Society for Pharmaceutical Sciences, Societe canadienne des sciences pharmaceutiques · 2024Review
- 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 · 2023Article
- Role of glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1 in hypertriglyceridemia and diabetes.Journal of diabetes investigation · 2023Review
- 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 · 2022Article
- Lipoprotein Lipase and Its Delivery of Fatty Acids to the Heart.Biomolecules · 2021Review
- A novel NanoBiT-based assay monitors the interaction between lipoprotein lipase and GPIHBP1 in real time.Journal of lipid research · 2020Article
- GPIHBP1 and Lipoprotein Lipase, Partners in Plasma Triglyceride Metabolism.Cell metabolism · 2019Review
- Critical Role of SREBP-1c Large-VLDL Pathway in Environment-Induced Hypertriglyceridemia of Apo AV Deficiency.Arteriosclerosis, thrombosis, and vascular biology · 2019Article
- 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 · 2018Article
- Apolipoprotein C-II: New findings related to genetics, biochemistry, and role in triglyceride metabolism.Atherosclerosis · 2017Review
- Lipoprotein lipase reaches the capillary lumen in chickens despite an apparent absence of GPIHBP1.JCI insight · 2017Article
- Marked Differences of Haplotype Tagging SNP Distribution, Linkage, and Haplotype Profile of APOA5 Gene in Roma Population Samples.Pathology oncology research : POR · 2017Article
5 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
GPIHBP1, a glycosylphosphatidylinositol-anchored endothelial cell protein of the lymphocyte antigen 6 (Ly6) family, plays a key role in the lipolysis of triglyceride-rich lipoproteins (e.g. chylomicrons). GPIHBP1 is expressed along the luminal surface of endothelial cells of heart, skeletal muscle, and adipose tissue, and GPIHBP1-expressing cells bind lipoprotein lipase (LPL) and chylomicrons avidly. GPIHBP1 contains an amino-terminal acidic domain (amino acids 24-48) that is enriched in aspartate and glutamate residues, and we previously speculated that this domain might be important in binding ligands. To explore the functional importance of the acidic domain, we tested the ability of polyaspartate or polyglutamate peptides to block the binding of ligands to pgsA-745 Chinese hamster ovary cells that overexpress GPIHBP1. Both polyaspartate and polyglutamate blocked LPL and chylomicron binding to GPIHBP1. Also, a rabbit antiserum against the acidic domain of GPIHBP1 blocked LPL and chylomicron binding to GPIHBP1-expressing cells. Replacing the acidic amino acids within GPIHBP1 residues 38-48 with alanine eliminated the ability of GPIHBP1 to bind LPL and chylomicrons. Finally, mutation of the positively charged heparin-binding domains within LPL and apolipoprotein AV abolished the ability of these proteins to bind to GPIHBP1. These studies indicate that the acidic domain of GPIHBP1 is important and that electrostatic interactions play a key role in ligand binding.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.