ArticleCytotechnology1994
Changes of monosaccharide availability of human hybridoma lead to alteration of biological properties of human monoclonal antibody.
Article in Cytotechnology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 48 citations in OpenAlex.
- On-tissue spatially resolved glycoproteomics guided by N-glycan imaging reveal global dysregulation of canine glioma glycoproteomic landscape.Cell chemical biology · 2022Article
- Efficient production of recombinant IgG by metabolic control and co-expression with GLUT5 in a fructose-based medium.Cytotechnology · 2010Article
- The effect of nitrogen source on yield and glycosylation of a human cystatin C mutant expressed in Pichia pastoris.Journal of industrial microbiology & biotechnology · 2004Article
- Building high affinity human antibodies by altering the glycosylation on the light chain variable region in N-acetylglucosamine-supplemented hybridoma cultures.Cytotechnology · 1997Article
- Mannose corrects altered N-glycosylation in carbohydrate-deficient glycoprotein syndrome fibroblasts.The Journal of clinical investigation · 1996Article
- Modified antigen-binding of human antibodies with glycosylation variations of the light chains produced in sugar-limited human hybridoma cultures.In vitro cellular & developmental biology. Animal · 1996Article
- Glycosylation of antibody in a lectin-resistant human hybridoma is insensitive to glucose.In vitro cellular & developmental biology. Animal · 1995Article
Corrections and comments
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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
The effect of glucose and other monosaccharide availability in culture medium on production of antibody by human hybridomas has been studied. Human hybridoma cells C5TN produce an anti lung cancer human monoclonal antibody, and the light chain is N-glycosylated at the variable region. When the cell line was grown in the presence of various concentrations of glucose, the antibodies produced changed their antigen-binding activities. Analysis of the light chains produced under these condition revealed that four molecular-mass variant light chains ranging from about 26 to 32 kDa were secreted. The twenty six-kDa species, which corresponds to a non-glycosylated form of the light chain, was recovered after enzymatic removal of all N-linked carbohydrate chains, indicating that the source of the heterogeneity of the light chain is due to the varied glycosylation. When the C5TN cells were cultured in medium containing either fructose, mannose or galactose instead of glucose, galactose elevated the antigen binding activity of the antibody more than the other sugars. These results suggest that change of glucose availability affects the antigen-binding activity of the antibody via the alteration of the glycosylation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.