Pathological crystallization of human immunoglobulins
- 30 July 2012
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 109 (33), 13359-13361
- https://doi.org/10.1073/pnas.1211723109
Abstract
Condensation of Igs has been observed in pharmaceutical formulations and in vivo in cases of cryoglobulinemia. We report a study of monoclonal IgG cryoglobulins overexpressed by two patients with multiple myeloma. These cryoglobulins form crystals, and we measured their solubility lines. Depending on the supersaturation, we observed a variety of condensate morphologies consistent with those reported in clinical investigations. Remarkably, the crystallization can occur at quite low concentrations. This suggests that, even within the regular immune response to infections, cryoprecipitation of Ig can be possible.Keywords
This publication has 26 references indexed in Scilit:
- Phase separation in solutions of monoclonal antibodies and the effect of human serum albuminProceedings of the National Academy of Sciences of the United States of America, 2011
- Crystallization and liquid‐liquid phase separation of monoclonal antibodies and fc‐fusion proteins: Screening resultsBiotechnology Progress, 2011
- Liquid-Liquid Phase Separation of a Monoclonal Antibody and Nonmonotonic Influence of Hofmeister AnionsBiophysical Journal, 2010
- Monoclonal gammopathy of undetermined significance: a consensus statementBritish Journal of Haematology, 2010
- The use of native cation-exchange chromatography to study aggregation and phase separation of monoclonal antibodiesProtein Science, 2010
- Single-Agent Bortezomib in Previously Untreated Multiple Myeloma: Efficacy, Characterization of Peripheral Neuropathy, and Molecular Correlations With Response and NeuropathyJournal of Clinical Oncology, 2009
- Review of peripheral neuropathy in plasma cell disordersHematological Oncology, 2008
- Decrease in Protein Solubility and Cataract Formation Caused by the Pro23 to Thr Mutation in Human γD-Crystallin,Biochemistry, 2005
- Enhanced crystallization of the Cys18 to ser mutant of bovine γB crystallinJournal of Molecular Biology, 2001
- Abnormal Human Serum GlobulinsScience, 1955