Modified antigen-binding of human antibodies with glycosylation variations of the light chains produced in sugar-limited human hybridoma cultures

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Abstract

We have characterized the effects of serum and N-acetylglucosamine in a glucose-deprived condition on the glycosylation of antibody light chains, as well as the resulting biological properties of those antibodies. We have chosen for our investigation the human hybridoma lines producing monoclonal antibodies reactive to lung adenocarcinoma. Each antibody possess a N- glycosylated carbohydrate chain in the hypervariable region of the light chains. When the cell lines were grown in the absence of glucose, variant light chains with varying molecular masses were found to be secreted. Analysis of these light chains produced in a glucose-deprived condition revealed that the changed molecular-mass of the variant light chains is due to different glycosylation. Addition of N-acetylglucosamine or fetal calf serum to the glucose-free medium led to the creation of other light chains that exhibit increased antigen binding activity.

Original languageEnglish
Pages (from-to)178-183
Number of pages6
JournalIn Vitro Cellular and Developmental Biology - Animal
Volume32
Issue number3
DOIs
Publication statusPublished - Jan 1 1996

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Hybridomas
Glycosylation
Light
Antigens
Antibodies
Glucose
Acetylglucosamine
Serum
Monoclonal Antibodies
Carbohydrates
Cell Line

All Science Journal Classification (ASJC) codes

  • Developmental Biology
  • Cell Biology

Cite this

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abstract = "We have characterized the effects of serum and N-acetylglucosamine in a glucose-deprived condition on the glycosylation of antibody light chains, as well as the resulting biological properties of those antibodies. We have chosen for our investigation the human hybridoma lines producing monoclonal antibodies reactive to lung adenocarcinoma. Each antibody possess a N- glycosylated carbohydrate chain in the hypervariable region of the light chains. When the cell lines were grown in the absence of glucose, variant light chains with varying molecular masses were found to be secreted. Analysis of these light chains produced in a glucose-deprived condition revealed that the changed molecular-mass of the variant light chains is due to different glycosylation. Addition of N-acetylglucosamine or fetal calf serum to the glucose-free medium led to the creation of other light chains that exhibit increased antigen binding activity.",
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