Genomic and proteomic exploration of CHO and hybridoma cells under sodium butyrate treatment

Yee, JC; Gatti, MdeL; Philp, RJ; Yap, M; Hu, WeiS

HERO ID

1458426

Reference Type

Journal Article

Year

2008

Language

English

PMID

17929327

HERO ID 1458426
In Press No
Year 2008
Title Genomic and proteomic exploration of CHO and hybridoma cells under sodium butyrate treatment
Authors Yee, JC; Gatti, MdeL; Philp, RJ; Yap, M; Hu, WeiS
Journal Biotechnology and Bioengineering
Volume 99
Issue 5
Page Numbers 1186-1204
Abstract Sodium butyrate has been known to increase the specific productivity of recombinant proteins in mammalian cells. In quest of physiological mechanisms leading to the increased productivity, DNA microarray and two dimensional gel electrophoresis (2DE) were used to assess the response of Chinese hamster ovary (CHO) and a mouse hybridoma cell (MAK) to butyrate treatment at the transcriptome and proteome level. The expression of the orthologous genes represented on both CHO cDNA and mouse Affymetrix microarray, as well as genes in the same ontological class were compared. Only a relatively small number of orthologs changed their expression consistently between the two cell lines, however, at a functional class level many genes involved in cell cycle and apoptosis were affected in both cell lines. Furthermore, a large number of genes involved in protein processing, secretion and redox activity were upregulated in both CHO and MAK cells. More genes showed a consistent trend of change at both transcript and protein levels than those which showed opposite trend in MAK cells. Overall the results suggested that the changes arising in the protein processing machinery may be responsible for the increased productivity upon butyrate treatment in both CHO and MAK cells.
Doi 10.1002/bit.21665
Pmid 17929327
Wosid WOS:000253925800013
Is Certified Translation No
Dupe Override No
Comments Source: Web of Science WOS:000253925800013
Is Public Yes
Language Text English
Keyword transcriptome; proteome; microarray; cell culture; protein secretion; recombinant protein