Quantifying Changes in the Cellular Thiol-Disulfide Status during Differentiation of B Cells into Antibody-Secreting Plasma Cells

Plasma cells produce and secrete massive amounts of disulfide-containing antibodies. To accommodate this load on the secretory machinery, the differentiation of resting B cells into antibody-secreting plasma cells is accompanied by a preferential expansion of the secretory compartments of the cells...

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Bibliographic Details
Published in:International Journal of Cell Biology 2013, Vol.2013 (2013), p.611-619
Main Authors: Hansen, Rosa E., Otsu, Mieko, Braakman, Ineke, Winther, Jakob R.
Format: Article
Language:English
Subjects:
Antibodies
B cells
Cell interaction
Cell research
Chemical bonds
Endoplasmic reticulum
Enzymes
Health aspects
Molecular weight
Plasma
Protein folding
Rodents
Thiols
Viral antibodies
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Summary:Plasma cells produce and secrete massive amounts of disulfide-containing antibodies. To accommodate this load on the secretory machinery, the differentiation of resting B cells into antibody-secreting plasma cells is accompanied by a preferential expansion of the secretory compartments of the cells and by an up-regulation of enzymes involved in redox regulation and protein folding. We have quantified the absolute levels of protein thiols, protein disulfides, and glutathionylated proteins in whole cells. The results show that while the global thiol-disulfide state is affected to some extent by the differentiation, steady-state levels of glutathionylated protein thiols are less than 0.3% of the total protein cysteines, even in fully differentiated cells, and the overall protein redox state is not affected until late in differentiation, when large-scale IgM production is ongoing. A general expansion of the ER does not affect global protein redox status until an extensive production of cargo proteins has started.
ISSN:1687-8876
1687-8884
DOI:10.1155/2013/898563