ArticleJournal of biomedicine & biotechnology2010
Enhancement of human prolactin synthesis by sodium butyrate addition to serum-free CHO cell culture.
Article in Journal of biomedicine & biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 23 citations in OpenAlex.
- A novel dual-epigenetic inhibitor enhances recombinant monoclonal antibody expression in CHO cells.Applied microbiology and biotechnology · 2024Article
- Enhancement of recombinant human IL-24 (rhIL-24) protein production from site-specific integrated engineered CHO cells by sodium butyrate treatment.Bioprocess and biosystems engineering · 2022Article
- Rational development of a serum-free medium and fed-batch process for a GS-CHO cell line expressing recombinant antibody.Cytotechnology · 2013Article
- Overexpression of tissue factor pathway inhibitor in CHO-K1 cells results in increased activation of NF-κB and apoptosis mediated by a caspase-3 independent pathway.Molecular biology reports · 2012Article
- Production of functional soluble Dectin-1 glycoprotein using an IRES-linked destabilized-dihydrofolate reductase expression vector.PloS one · 2012Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sodium butyrate (NaBu) has been used as a productivity enhancer for the synthesis of recombinant proteins in Chinese hamster ovary (CHO) cells. Thus, the influence of NaBu on the production of recombinant human prolactin (hPRL) from CHO cells was investigated for the first time. CHO cell cultures were submitted to a treatment with different concentrations of NaBu (0.25 to 4 mM). Quantitative and qualitative analyses by reverse-phase high-performance liquid chromatography (RP-HPLC) and Western blot or SDS-PAGE, carried out directly on CHO-conditioned medium, showed that the highest hPRL expression was obtained with 1 mM NaBu. In vitro biological assays based on noble rat lymphoma (Nb2) and mouse pro-B lymphoma (Ba/F3-LLP) cells were carried out on purified hPRL. Its bioactivity in the presence of NaBu was not apparently different from that of the First International Reference Reagent of recombinant hPRL (WHO 97/714). Our results show that NaBu increased the synthesis of recombinant hPRL in CHO cells, apparently without compromising either its structure or function.
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