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-Î 1/4, 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.

Francesca Mossuto, M., Ami, D., Anelli, T., Fagioli, C., Maria Doglia, S., Sitia, R. (2015). Biochemical nature of Russell Bodies. SCIENTIFIC REPORTS, 5 [10.1038/srep12585].

Biochemical nature of Russell Bodies

AMI, DILETTA
Secondo
;
2015

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-Î 1/4, 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.
Articolo in rivista - Articolo scientifico
HEK293 Cells; HeLa Cells; Humans; Immunoglobulin mu-Chains; Microscopy, Confocal; Mutation; Spectrophotometry, Infrared; Multidisciplinary
English
2015
5
12585
none
Francesca Mossuto, M., Ami, D., Anelli, T., Fagioli, C., Maria Doglia, S., Sitia, R. (2015). Biochemical nature of Russell Bodies. SCIENTIFIC REPORTS, 5 [10.1038/srep12585].
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/134649
Citazioni
  • Scopus 9
  • ???jsp.display-item.citation.isi??? 7
Social impact