1. Biochemical nature of Russell Bodies
- Author
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Maria Francesca Mossuto, Claudio Fagioli, Diletta Ami, Silvia Maria Doglia, Roberto Sitia, Tiziana Anelli, Francesca Mossuto, M, Ami, D, Anelli, T, Fagioli, C, Maria Doglia, S, and Sitia, R
- Subjects
Spectrophotometry, Infrared ,Immunoglobulin mu-Chain ,Russell bodies ,FIS/07 - FISICA APPLICATA (A BENI CULTURALI, AMBIENTALI, BIOLOGIA E MEDICINA) ,Plasma cell ,medicine.disease_cause ,HeLa Cell ,Article ,HEK293 Cell ,medicine ,Extracellular ,Humans ,Mutation ,Microscopy, Confocal ,Multidisciplinary ,biology ,Immunoglobulin mu-Chains ,Endoplasmic reticulum ,HEK 293 cells ,Cell biology ,HEK293 Cells ,medicine.anatomical_structure ,Immunology ,biology.protein ,Antibody ,Biogenesis ,HeLa Cells ,Human - Abstract
Professional secretory cells produce and release abundant proteins. Particularly in case of mutations and/or insufficient chaperoning, these can aggregate and become toxic within or amongst cells. Immunoglobulins (Ig) are no exception. In the extracellular space, certain Ig-L chains form fibrils causing systemic amyloidosis. On the other hand, Ig variants lacking the first constant domain condense in dilated cisternae of the early secretory compartment, called Russell Bodies (RB), frequently observed in plasma cell dyscrasias, autoimmune diseases and chronic infections. RB biogenesis can be recapitulated in lymphoid and non-lymphoid cells by expressing mutant Ig-μ, providing powerful models to investigate the pathophysiology of endoplasmic reticulum storage disorders. Here we analyze the aggregation propensity and the biochemical features of the intra- and extra-cellular Ig deposits in human cells, revealing β-aggregated features for RB.
- Published
- 2015