ArticleGlycobiology2008
Analysis of the N-glycans of recombinant human Factor IX purified from transgenic pig milk.
Article in Glycobiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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.
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Who cites it
17 citing papers in PubMed, 36 citations in OpenAlex.
- Coagulation factor IX analysis in bioreactor cell culture supernatant predicts quality of the purified product.Communications biology · 2021Article
- Identification of novel glycosylation events on human serum-derived factor IX.Glycoconjugate journal · 2020Article
- Article
- Expression of Active Fluorophore Proteins in the Milk of Transgenic Pigs Bypassing the Secretory Pathway.Scientific reports · 2016Article
- New developments in the management of moderate-to-severe hemophilia B.Journal of blood medicine · 2016Review
- Characterization of IXINITY® (Trenonacog Alfa), a Recombinant Factor IX with Primary Sequence Corresponding to the Threonine-148 Polymorph.Advances in hematology · 2016Article
- Engineering protein processing of the mammary gland to produce abundant hemophilia B therapy in milk.Scientific reports · 2015Article
- Production of pigs expressing a transgene under the control of a tetracycline-inducible system.PloS one · 2014Article
- Recombinant human factor IX produced from transgenic porcine milk.BioMed research international · 2014Article
- N-/O-glycosylation analysis of human FVIIa produced in the milk of transgenic rabbits.Glycobiology · 2013Article
- Blood Clotting Factor VIII: From Evolution to Therapy.Acta naturae · 2013Article
- Use of transgenic animals in biotechnology: prospects and problems.Acta naturae · 2013Article
- Coagulation Factor IX for Hemophilia B Therapy.Acta naturae · 2012Article
- Functional factor VIII made with von Willebrand factor at high levels in transgenic milk.Journal of thrombosis and haemostasis : JTH · 2011Article
- Site-specific enzymatic polysialylation of therapeutic proteins using bacterial enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- High throughput quantification of N-glycans using one-pot sialic acid modification and matrix assisted laser desorption ionization time-of-flight mass spectrometry.Analytical chemistry · 2010Article
- N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C.Proteomics · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Glycosylation of recombinant proteins is of particular importance because it can play significant roles in the clinical properties of the glycoprotein. In this work, the N-glycan structures of recombinant human Factor IX (tg-FIX) produced in the transgenic pig mammary gland were determined. The majority of the N-glycans of transgenic pig-derived Factor IX (tg-FIX) are complex, bi-antennary with one or two terminal N-acetylneuraminic acid (Neu5Ac) moieties. We also found that the N-glycan structures of tg-FIX produced in the porcine mammary epithelial cells differed with respect to N-glycans from glycoproteins produced in other porcine tissues. tg-FIX contains no detectable Neu5Gc, the sialic acid commonly found in porcine glycoproteins produced in other tissues. Additionally, we were unable to detect glycans in tg-FIX that have a terminal Galalpha(1,3)Gal disaccharide sequence, which is strongly antigenic in humans. The N-glycan structures of tg-FIX are also compared to the published N-glycan structures of recombinant human glycoproteins produced in other transgenic animal species. While tg-FIX contains only complex structures, antithrombin III (goat), C1 inhibitor (rabbit), and lactoferrin (cow) have both high mannose and complex structures. Collectively, these data represent a beginning point for the future investigation of species-specific and tissue/cell-specific differences in N-glycan structures among animals used for transgenic animal bioreactors.
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Registered trials
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