Quantifying changes in the cellular thiol-disulfide status during differentiation of B cells into antibody-secreting plasma cells

TY - JOUR

T1 - Quantifying changes in the cellular thiol-disulfide status during differentiation of B cells into antibody-secreting plasma cells

AU - Hansen, Rosa Rebecca Erritzøe

AU - Otsu, Mieko

AU - Braakman, Ineke

AU - Winther, Jakob R.

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

U2 - 10.1155/2013/898563

DO - 10.1155/2013/898563

M3 - Journal article

C2 - 24223594

SN - 1687-8876

VL - 2013

JO - International Journal of Cell Biology

JF - International Journal of Cell Biology

M1 - 898563

ER -