Source:http://linkedlifedata.com/resource/pubmed/id/21169054
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2011-2-25
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pubmed:abstractText |
The specific productivity of tumor necrosis factor receptor-immunoglobulin G1 Fc fusion (TNFR-Fc) (q(TNFR-Fc)) in Chinese hamster ovary (CHO) cells at 30°C was approximately 5-fold higher than that at 37°C. To investigate reasons for increased q(TNFR-Fc) at low culture temperature, TNFR-Fc mRNA levels were determined by real-time PCR. It was found that like q(TNFR-Fc), the relative TNFR-Fc mRNA level was increased by lowering culture temperature, and more importantly, the kinetics of the increase in TNFR-Fc mRNA levels were in accordance with the changes in q(TNFR-Fc). The results demonstrated that the increased transcriptional level of TNFR-Fc was responsible for the increased q(TNFR-Fc) at low culture temperature. Enhanced levels of mRNA could derive from increased gene copy number, improved mRNA stability, or enhanced transcriptional rate. There was not a big change of gene copy number by lowering culture temperature. The transcriptional rate of TNFR-Fc was slightly decreased at 30°C, compared to 37°C. However, mRNA stability of TNFR-Fc was significantly improved by lowering culture temperature. The half-life of TNFR-Fc mRNA was 5.55 h at 30°C, whereas that was 3.69h at 37°C. Taken together, the reasons for the increased q(TNFR-Fc) in CHO cells at low culture temperature were mainly the enhanced TNFR-Fc mRNA levels, which resulted from the improved mRNA stability, rather than the changes in the gene copy number or the transcriptional rate.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TNFR-Fc fusion protein
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1347-4421
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2010 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:volume |
111
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
365-9
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pubmed:meshHeading |
pubmed-meshheading:21169054-Animals,
pubmed-meshheading:21169054-CHO Cells,
pubmed-meshheading:21169054-Cell Culture Techniques,
pubmed-meshheading:21169054-Cold Temperature,
pubmed-meshheading:21169054-Cricetinae,
pubmed-meshheading:21169054-Cricetulus,
pubmed-meshheading:21169054-Gene Dosage,
pubmed-meshheading:21169054-Immunoglobulin G,
pubmed-meshheading:21169054-RNA, Messenger,
pubmed-meshheading:21169054-RNA Stability,
pubmed-meshheading:21169054-Receptors, Tumor Necrosis Factor,
pubmed-meshheading:21169054-Recombinant Fusion Proteins,
pubmed-meshheading:21169054-Transcription, Genetic,
pubmed-meshheading:21169054-Transfection
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pubmed:year |
2011
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pubmed:articleTitle |
Detailed understanding of enhanced specific productivity in Chinese hamster ovary cells at low culture temperature.
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pubmed:affiliation |
The State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai 200237, PR China.
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pubmed:publicationType |
Journal Article
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