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O-GlcNAcylation of Light Chain Serine 12 Mediates Rituximab Production Doubled by Thiamet G

Authors
 Hye-Yeon Kim  ;  Minseong Park  ;  Choeun Kang  ;  Woon Heo  ;  Sei Mee Yoon  ;  Jinu Lee  ;  Joo Young Kim 
Citation
 BIOPROCESS AND BIOSYSTEMS ENGINEERING, Vol.43(5) : 863-875, 2020-05 
Journal Title
 BIOPROCESS AND BIOSYSTEMS ENGINEERING 
ISSN
 1615-7591 
Issue Date
2020-05
Keywords
ADCC ; CDC ; O-GlcNAc ; Production yield ; Rituximab ; Thermal stability ; Thiamet G
Abstract
O-Glycosylation occurs in recombinant proteins produced by CHO cells, but this phenomenon has not been studied extensively. Here, we report that rituximab is an O-linked N-acetyl-glucosaminylated (O-GlcNAcylated) protein and the production of rituximab is increased by thiamet G, an inhibitor of O-GlcNAcase. The production of rituximab doubled with OGA inhibition and decreased with O-GlcNAc transferase inhibition. O-GlcNAc-specific antibody and metabolic labelling with azidO-GlcNAc confirmed the increased O-GlcNAcylation with thiamet G. Protein mass analysis revealed that serine 7, 12, and 14 of the rituximab light chain were O-GlcNAcylated. S12A mutation of the light chain decreased rituximab stability and failed to increase the production with thiamet G without any significant changes of mRNA level. Cytotoxicity and thermal stability assays confirmed that there were no differences in the biological and physical properties of rituximab produced by thiamet G treatment. Therefore, thiamet G treatment improves the production of rituximab without significantly altering its function.
Full Text
https://link.springer.com/article/10.1007/s00449-020-02282-z
DOI
10.1007/s00449-020-02282-z
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Pharmacology (약리학교실) > 1. Journal Papers
Yonsei Authors
Kim, Joo Young(김주영) ORCID logo https://orcid.org/0000-0003-2623-1491
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/176105
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