ArticleCytotechnology1996
Genetic engineering of α2,6-sialyltransferase in recombinant CHO cells and its effects on the sialylation of recombinant interferon-γ.
Article in Cytotechnology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed, 44 citations in OpenAlex.
- Engineering of CHO cells for the production of vertebrate recombinant sialyltransferases.PeerJ · 2019Article
- Improving Immunotherapy Through Glycodesign.Frontiers in immunology · 2018Review
- Contribution of vascular endothelial growth factor receptor-2 sialylation to the process of angiogenesis.Oncogene · 2017Article
- Efficient generation of influenza virus with a mouse RNA polymerase I-driven all-in-one plasmid.Virology journal · 2015Article
- Related effects of cell adaptation to serum-free conditions on murine EPO production and glycosylation by CHO cells.Cytotechnology · 2006Article
- Application of a reversible immortalization system for the generation of proliferation-controlled cell lines.Cytotechnology · 2004Article
- Genetic engineering of CHO cells producing human interferon-gamma by transfection of sialyltransferases.Glycoconjugate journal · 2000Article
- Na-butyrate increases the production and alpha2,6-sialylation of recombinant interferon-gamma expressed by alpha2,6- sialyltransferase engineered CHO cells.Cytotechnology · 1999Article
- Chinese hamster ovary (CHO) host cell engineering to increase sialylation of recombinant therapeutic proteins by modulating sialyltransferase expression.Biotechnology progressArticle
- Recombinant interferon-gamma secreted by Chinese hamster ovary-320 cells cultivated in suspension in protein-free media is protected against extracellular proteolysis by the expression of natural protease inhibitors and by the addition of plant protein hydrolysates to the culture medium.In vitro cellular & developmental biology. AnimalArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The CHO cell line has achieved considerable commercial importance as a vehicle for the production of human therapeutic proteins, but is known to lack a functional copy of the gene coding for α2,6-sialyltransferase (EC 2.4.99.1). The cDNA for rat α2,6-ST was expressed in a recombinant CHO cell line making interferon-γ, using a novel in vitro amplification vector. The enzyme was expressed efficiently, and resulted in up to 60% of the total sialic acids on interferon-γ being linked in the α2,6-conformation. This sialic acid linkage distribution was more akin to that seen in natural human glycoproteins. In the most successful cell clones, expression of α2,6-sialyltransferase improved the overall level of sialylation by up to 56%, and had no adverse effects on cell growth, IFN-γ productivity or other aspects of IFN-γ glycosylation. These experiments demonstrate how the glycosylation machinery of rodent cells can be genetically manipulated to replicate human tissues.
Identifiers
What OpenQuestion holds
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.