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Hansen RE, Otsu M, Braakman I, et al. Quantifying Changes in the Cellular Thiol-Disulfide Status during Differentiation of B Cells into Antibody-Secreting Plasma Cells. Int J Cell Biol. 2013;2013:898563doi: 10.1155/2013/898563.
Hansen, R. E., Otsu, M., Braakman, I., & Winther, J. R. (2013). Quantifying Changes in the Cellular Thiol-Disulfide Status during Differentiation of B Cells into Antibody-Secreting Plasma Cells. International journal of cell biology, 2013898563. https://doi.org/10.1155/2013/898563
Hansen, Rosa E, et al. "Quantifying Changes in the Cellular Thiol-Disulfide Status during Differentiation of B Cells into Antibody-Secreting Plasma Cells." International journal of cell biology vol. 2013 (2013): 898563. doi: https://doi.org/10.1155/2013/898563
Hansen RE, Otsu M, Braakman I, Winther JR. Quantifying Changes in the Cellular Thiol-Disulfide Status during Differentiation of B Cells into Antibody-Secreting Plasma Cells. Int J Cell Biol. 2013;2013:898563. doi: 10.1155/2013/898563. Epub 2013 Sep 24. PMID: 24223594; PMCID: PMC3800581.
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Int J Cell Biol. 2013;2013:898563. doi: 10.1155/2013/898563. Epub 2013 Sep 24.

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

International journal of cell biology

Rosa E Hansen, Mieko Otsu, Ineke Braakman, Jakob R Winther

Affiliations

  1. Section for Biomolecular Sciences, Department of Biology, University of Copenhagen, Ole Maaloes Vej 5, 2200 Copenhagen, Denmark ; Novo Nordisk A/S, 2760 Maaloev, Denmark.

PMID: 24223594 PMCID: PMC3800581 DOI: 10.1155/2013/898563

Abstract

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.

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