2011
DOI: 10.1016/j.antiviral.2011.01.004
|View full text |Cite
|
Sign up to set email alerts
|

Preparation of CHO cell-derived rhIFN-ω-Fc with improved pharmacokinetics

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

0
3
0

Year Published

2014
2014
2018
2018

Publication Types

Select...
4

Relationship

0
4

Authors

Journals

citations
Cited by 4 publications
(3 citation statements)
references
References 26 publications
0
3
0
Order By: Relevance
“…Some studies showed that compared with rHuIFN-ω expressed in yeast with a specific activity of 7 × 10 7 IU/mg, rHuIFN-ω-Fc had a lower activity of 1.6 × 10 7 IU/mg when it was expressed in Chinese hamster ovary cells. Furthermore, the terminal half-life of rHuIFN-ω-Fc was 35-fold higher than that of rHuIFN-ω, and it exhibited better pharmacokinetics characteristics [40]. Perhaps rHuIFN-ω-Fc will become a new alternative antiviral drug for the treatment of chronic viral infections.…”
Section: Strategies To Improve the Antiviral Efficiency Of Ifn-ωmentioning
confidence: 99%
“…Some studies showed that compared with rHuIFN-ω expressed in yeast with a specific activity of 7 × 10 7 IU/mg, rHuIFN-ω-Fc had a lower activity of 1.6 × 10 7 IU/mg when it was expressed in Chinese hamster ovary cells. Furthermore, the terminal half-life of rHuIFN-ω-Fc was 35-fold higher than that of rHuIFN-ω, and it exhibited better pharmacokinetics characteristics [40]. Perhaps rHuIFN-ω-Fc will become a new alternative antiviral drug for the treatment of chronic viral infections.…”
Section: Strategies To Improve the Antiviral Efficiency Of Ifn-ωmentioning
confidence: 99%
“…These TFs are sterol regulatory element binding transcription factor, activating enhancer binding protein 2-like YY1 site, interferon conserved sequence-binding protein, erythroid Kruppel-like factor gene, homeotic gene forkhead of Drosophila 8/hepatocyte nuclear factor 3/mouse forkhead lung protein, HNF-1A, interferon consensus sequence binding protein, and lymphocyte-enriched DNA binding protein LyF [129]. When expressed in yeast, recombinant human IFN-ω-Fc fusion protein (rhIFN-ω-Fc) has more specific activity than when expressed in a Chinese hamster ovary cell line; its terminal half-life is 35 times higher than rhIFN-ω [130]. However, an obvious drawback of IFN-ω is that it requires daily subcutaneous administration, which might influence patients’ compliance and impair its effectiveness.…”
Section: Hepatitismentioning
confidence: 99%
“…Peg-IFN-λ1 is currently undergoing clinical development for the treatment of viral hepatitis (Duong et al, 2014). Recombinant human IFN-ω-Fc fusion protein represents a useful and promising and alternative antiviral agent especially for the treatment of chronic viral disease, such as hepatitis C virus infection (Li et al, 2011). Accordingly to our results, the IFN-ω should be suitable as antiviral agent against some avian strains and IFN-λ1s should be used against human infl uenza viruses.…”
Section: Discussionmentioning
confidence: 67%