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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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Published in: | International Journal of Cell Biology 2013, Vol.2013 (2013), p.611-619 |
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container_title | International Journal of Cell Biology |
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creator | Hansen, Rosa E. Otsu, Mieko Braakman, Ineke Winther, Jakob R. |
description | 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. |
doi_str_mv | 10.1155/2013/898563 |
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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.</description><identifier>ISSN: 1687-8876</identifier><identifier>EISSN: 1687-8884</identifier><identifier>DOI: 10.1155/2013/898563</identifier><identifier>PMID: 24223594</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Limiteds</publisher><subject>Antibodies ; B cells ; Cell interaction ; Cell research ; Chemical bonds ; Endoplasmic reticulum ; Enzymes ; Health aspects ; Molecular weight ; Plasma ; Protein folding ; Rodents ; Thiols ; Viral antibodies</subject><ispartof>International Journal of Cell Biology, 2013, Vol.2013 (2013), p.611-619</ispartof><rights>Copyright © 2013 Rosa E. Hansen et al.</rights><rights>COPYRIGHT 2013 John Wiley & Sons, Inc.</rights><rights>Copyright © 2013 Rosa E. Hansen et al. Rosa E. Hansen et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</rights><rights>Copyright © 2013 Rosa E. 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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.</description><subject>Antibodies</subject><subject>B cells</subject><subject>Cell interaction</subject><subject>Cell research</subject><subject>Chemical bonds</subject><subject>Endoplasmic reticulum</subject><subject>Enzymes</subject><subject>Health aspects</subject><subject>Molecular weight</subject><subject>Plasma</subject><subject>Protein folding</subject><subject>Rodents</subject><subject>Thiols</subject><subject>Viral antibodies</subject><issn>1687-8876</issn><issn>1687-8884</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNqFkktv1DAQgCMEoqVw4gyKxAWB0tqx48cFadnyqLQSRS1na-LYu15l49ZOQHvkn-NsypZFSCix7Hi--aIZTZY9x-gU46o6KxEmZ0KKipEH2TFmghdCCPpwf-bsKHsS4xohJrGUj7OjkpYlqSQ9zn5-HaDrnd26bpnPV9AtTcxdl_crk89N2w4thPx65XxbnLs4tNY1Jr_qoR9i3gxhzDp31ppgkgV657vc2_z9LncU9T6fpUjtm21xZXQw_Zhy2ULcwAQ9zR5ZaKN5drefZN8-friefy4WXz5dzGeLAipBSMFKTq3UNalQUyKOSqS5SK-RAEA04xQoliWTQliEMasqxGuqDTM1lxpTcpJdTN7Gw1rdBLeBsFUenNpd-LBUEHqnW6MwwzVh1jBBS0opCMq0tIAtqzEmjCfXu8l1M9Qb0-hUfID2QHoY6dxKLf13RQRClcBJ8PpOEPztYGKvNi7q1A7ojB-iwrQSFWKpyoS--gtd-yF0qVWJoqRkQnJ5Ty0hFeA669N_9ShVM8IpIYSVJFGn_6DS05iN074z1qX7g4S3U4IOPsZg7L5GjNQ4fWqcPjVNX6Jf_tmWPft73BLwZgJWrmvgh_uP7cUEm4QYC3s4NYaKUbaY4uCC6919Wy6ThaEqLUR2RlyOG0ccU5RChx8M47Qk-QXLbf0q</recordid><startdate>2013</startdate><enddate>2013</enddate><creator>Hansen, Rosa E.</creator><creator>Otsu, Mieko</creator><creator>Braakman, Ineke</creator><creator>Winther, Jakob R.</creator><general>Hindawi Limiteds</general><general>Hindawi Puplishing Corporation</general><general>Hindawi Publishing Corporation</general><general>John Wiley & Sons, Inc</general><general>Hindawi Limited</general><scope>188</scope><scope>ADJCN</scope><scope>AHFXO</scope><scope>RHU</scope><scope>RHW</scope><scope>RHX</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>7TK</scope><scope>8FE</scope><scope>8FH</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>CWDGH</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>2013</creationdate><title>Quantifying Changes in the Cellular Thiol-Disulfide Status during Differentiation of B Cells into Antibody-Secreting Plasma Cells</title><author>Hansen, Rosa E. ; 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subjects | Antibodies B cells Cell interaction Cell research Chemical bonds Endoplasmic reticulum Enzymes Health aspects Molecular weight Plasma Protein folding Rodents Thiols Viral antibodies |
title | Quantifying Changes in the Cellular Thiol-Disulfide Status during Differentiation of B Cells into Antibody-Secreting Plasma Cells |
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