Quantifying changes in the cellular thiol-disulfide status during differentiation of B cells into antibody-secreting plasma cells
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Quantifying changes in the cellular thiol-disulfide status during differentiation of B cells into antibody-secreting plasma cells. / Hansen, Rosa Rebecca Erritzøe; Otsu, Mieko; Braakman, Ineke; Winther, Jakob R.
I: International Journal of Cell Biology, Bind 2013, 898563, 2013.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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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
VL - 2013
JO - International Journal of Cell Biology
JF - International Journal of Cell Biology
SN - 1687-8876
M1 - 898563
ER -
ID: 93948448