ArticleThe Journal of biological chemistry2018
Half-life-extended recombinant coagulation factor IX-albumin fusion protein is recycled via the FcRn-mediated pathway.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Re-engineering CD154 blockade for transplantation: Fc-free design to separate thrombotic risk from therapeutic function.Clinical transplantation and research · 2026Review
- Increased gene therapy efficacy through the use of extended half-life clotting factors.Blood advances · 2026Article
- Extended Half-Life Factor Concentrates in Haemophilia Treatment.Transfusion medicine and hemotherapy : offizielles Organ der Deutschen Gesellschaft fur Transfusionsmedizin und Immunhamatologie · 2026Review
- Extravascular distribution of factor IX-review of experimental and clinical evidence, and relevance for hemophilia B replacement therapy.Research and practice in thrombosis and haemostasis · 2026Review
- HMB-002: a monovalent antibody that elevates circulating VWF and FVIII levels for treatment of von Willebrand disease.Blood advances · 2026Article
- Ozoralizumab, a trivalent anti-TNFα NANOBODYFrontiers in immunology · 2026Article
- Tailored collagen binding of albumin-fused hyperactive coagulation factor IX dictates in vivo distribution and functional properties.Nature communications · 2025Article
- Binding of therapeutic Fc-fused factor VIII to the neonatal Fc receptor at neutral pH associates with poor half-life extension.Haematologica · 2025Article
- Enhanced plasma half-life and efficacy of engineered human albumin-fused GLP-1 despite enzymatic cleavage of its C-terminal end.Communications biology · 2025Article
- An ACE2-Fc decoy produced in glycoengineered plants neutralizes ancestral and newly emerging SARS-CoV-2 variants and demonstrates therapeutic efficacy in hamsters.Scientific reports · 2025Article
- Review
- The endosomal system of primary human vascular endothelial cells and albumin-FcRn trafficking.Journal of cell science · 2023Article
- IDELVION: A Comprehensive Review of Clinical Trial and Real-World Data.Journal of clinical medicine · 2022Review
- Dynamics of intracellular neonatal Fc receptor-ligand interactions in primary macrophages using biophysical fluorescence techniques.Molecular biology of the cell · 2022Article
- Albumin-Fusion Recombinant FIX in the Management of People with Hemophilia B: An Evidence-Based Review.Drug design, development and therapy · 2022Review
- Fusion of engineered albumin with factor IX Padua extends half-life and improves coagulant activity.British journal of haematology · 2021Article
- An intact C-terminal end of albumin is required for its long half-life in humans.Communications biology · 2020Article
- Excessive breakthrough bleeding in haemophilia B patients on factor IX-albumin fusion protein prophylactic therapy: A single centre case series.Haemophilia : the official journal of the World Federation of Hemophilia · 2020Article
- The Neonatal Fc Receptor (FcRn): A Misnomer?Frontiers in immunology · 2019Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The neonatal Fc receptor (FcRn) has a pivotal role in albumin and IgG homeostasis. Internalized IgG captured by FcRn under acidic endosomal conditions is recycled to the cell surface where exocytosis and a shift to neutral pH promote extracellular IgG release. Although a similar mechanism is proposed for FcRn-mediated albumin intracellular trafficking and recycling, this pathway is less well defined but is relevant to the development of therapeutics exploiting FcRn to extend the half-life of short-lived plasma proteins. Recently, a long-acting recombinant coagulation factor IX-albumin fusion protein (rIX-FP) has been approved for the management of hemophilia B. Fusion to albumin potentially enables internalized proteins to engage FcRn and escape lysosomal degradation. In this study, we present for the first time a detailed investigation of the FcRn-mediated recycling of albumin and the albumin fusion protein rIX-FP. We demonstrate that following internalization via FcRn at low pH, rIX-FP, like albumin, is detectable within the early endosome and rapidly (within 10-15 min) traffics into the Rab11+ recycling endosomes, from where it is exported from the cell. Similarly, rIX-FP and albumin taken up by fluid-phase endocytosis at physiological pH traffics into the Rab11+ recycling compartment in FcRn-positive cells but into the lysosomal compartment in FcRn-negative cells. As expected, recombinant factor IX (without albumin fusion) and an FcRn interaction-defective albumin variant localized to the lysosomal compartments of both FcRn-expressing and nonexpressing cells. These results indicate that FcRn-mediated recycling via the albumin moiety is a mechanism for the half-life extension of rIX-FP observed in clinical studies.
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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.