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Your search keyword '"Chan, Kah Fai"' showing total 19 results
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19 results on '"Chan, Kah Fai"'

14. Highly sialylated recombinant human erythropoietin production in large-scale perfusion bioreactor utilizing CHO-gmt4 (JW152) with restored GnT I function

Author

Goh, John S. Y., primary, Liu, Yingwei, additional, Liu, Haifeng, additional, Chan, Kah Fai, additional, Wan, Corrine, additional, Teo, Gavin, additional, Zhou, Xiangshan, additional, Xie, Fusheng, additional, Zhang, Peiqing, additional, Zhang, Yuanxing, additional, and Song, Zhiwei, additional

Published
2013
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19. RCA-I-resistant CHO mutant cells have dysfunctional GnT I and expression of normal GnT I in these mutants enhances sialylation of recombinant erythropoietin.

Author

Goh JS, Zhang P, Chan KF, Lee MM, Lim SF, and Song Z

Subjects
Animals, CHO Cells, Cricetinae, Cricetulus, Glycosylation, Point Mutation, Recombinant Proteins, Erythropoietin metabolism, N-Acetylglucosaminyltransferases genetics, N-Acetylneuraminic Acid metabolism, Plant Lectins pharmacology
Abstract

A large number of CHO glycosylation mutants were isolated by Ricinus communis agglutinin-I (RCA-I). Complementation tests revealed that all these mutant lines possessed a dysfunctional N-acetylglucosaminyltransferase I (GnT I) gene. Sequencing analyses on the GnT I cDNAs isolated from 16 mutant lines led to the identification of nine different single base pair mutations. Some mutations result in a premature stop codon whereas others cause a single amino acid substitution in the GnT I protein. Interestingly, expression of the normal GnT I cDNA in mutant cells resulted in enhanced sialylation of N-glycans. The sialylation of recombinant erythropoietin (EPO) produced in mutant cells that were co-transfected with GnT I was enhanced compared to that of EPO produced in wild type CHO cells. The enhanced sialylation of EPO produced by JW152 cells in the presence of GnT I over CHO-K1 cells is a result of increased sialylated glycan structures with higher antennary branching. These findings represent a new strategy that may be utilized by the biotechnology industry to produce highly sialylated therapeutic glycoproteins., (Copyright 2010 Elsevier Inc. All rights reserved.)

Published
2010
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