ArticleThe AAPS journal2009
Role of glycosylation in conformational stability, activity, macromolecular interaction and immunogenicity of recombinant human factor VIII.
Article in The AAPS journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 50 citations in OpenAlex.
- Review
- Interpretation guidance for MHRA regulatory considerations for phage therapeutic products.Microbiology (Reading, England) · 2025Review
- The use of Bacillus subtilis as a cost-effective expression system for production of Cholera Toxin B fused factor VIII epitope regions applicable for inducing oral immune tolerance.Folia microbiologica · 2024Article
- Influence of N-glycosylation in the A and C domains on the immunogenicity of factor VIII.Blood advances · 2022Article
- Strategies for Glycoengineering Therapeutic Proteins.Frontiers in chemistry · 2022Review
- Comprehensive N- and O-glycosylation mapping of human coagulation factor V.Journal of thrombosis and haemostasis : JTH · 2020Article
- Immune Responses to Plasma-Derived Versus Recombinant FVIII Products.Frontiers in immunology · 2020Review
- The role of beta-2-glycoprotein I in health and disease associating structure with function: More than just APS.Blood reviews · 2020Review
- How Full-Length FVIII Benefits from Its Heterogeneity - Insights into the Role of the B-Domain.Pharmaceutical research · 2019Article
- Critical Evaluation of Strategies for the Production of Blood Coagulation Factors in Plant-Based Systems.Frontiers in plant science · 2019Review
- N-linked glycosylation modulates the immunogenicity of recombinant human factor VIII in hemophilia A mice.Haematologica · 2018Article
- Genetic disruption of multiple α1,2-mannosidases generates mammalian cells producing recombinant proteins with high-mannose-typeThe Journal of biological chemistry · 2018Article
- Comparative N-Glycosylation Analysis of the Fc Portions of a Chimeric Human Coagulation Factor VIII and Immunoglobulin G1.Bioengineering (Basel, Switzerland) · 2017Article
- To clear or to fear: An innate perspective on factor VIII immunity.Cellular immunology · 2016Review
- Soy phosphatidylinositol containing nanoparticle prolongs hemostatic activity of B-domain deleted factor VIII in hemophilia A mice.Journal of pharmaceutical sciences · 2015Article
- Effects of replacement of factor VIII amino acids Asp519 and Glu665 with Val on plasma survival and efficacy in vivo.The AAPS journal · 2014Article
- Recent developments in protein and peptide parenteral delivery approaches.Therapeutic delivery · 2014Article
- A new recombinant factor VIII: from genetics to clinical use.Drug design, development and therapy · 2014Review
- Native-like aggregates of factor VIII are immunogenic in von Willebrand factor deficient and hemophilia a mice.Journal of pharmaceutical sciences · 2012Article
- Delivery of therapeutic proteins.Journal of pharmaceutical sciences · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Factor VIII (FVIII) is a multi-domain glycoprotein that is an essential cofactor in the blood coagulation cascade. Its deficiency or dysfunction causes hemophilia A, a bleeding disorder. Replacement using exogenous recombinant human factor VIII (rFVIII) is the first line of therapy for hemophilia A. The role of glycosylation on the activity, stability, protein-lipid interaction, and immunogenicity of FVIII is not known. In order to investigate the role of glycosylation, a deglycosylated form of FVIII was generated by enzymatic cleavage of carbohydrate chains. The biochemical properties of fully glycosylated and completely deglycosylated forms of rFVIII (degly rFVIII) were compared using enzyme-linked immunosorbent assay, size exclusion chromatography, and clotting activity studies. The biological activity of degly FVIII decreased in comparison to the fully glycosylated protein. The ability of degly rFVIII to interact with phosphatidylserine containing membranes was partly impaired. Data suggested that glycosylation significantly influences the stability and the biologically relevant macromolecular interactions of FVIII. The effect of glycosylation on immunogenicity was investigated in a murine model of hemophilia A. Studies showed that deletion of glycosylation did not increase immunogenicity.
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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.