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In vitro co-expression of human amyloidogenic immunoglobulin light and heavy chain proteins: a relevant cell-based model of AL amyloidosis
Open accessAbstract
Immunoglobulin (Ig) light chain (LC) amyloidosis (AL) is characterized by the overproduction and tissue deposition of monoclonal LC in various organs and tissues. The plasma circulating monoclonal LC is believed to be the precursor of the deposited protein and in vitro studies aimed at understanding AL pathobiology have mainly focused on LC and its variable domain. While 33% of patients have free circulating monoclonal LC, ∼40% feature LC complexed to heavy chain (HC) forming a monoclonal intact Ig; the significance of free vs. bound LC in the amyloid forming pathway is unknown. To address this issue, we developed a cell-based model using stable mouse plasmacytoma Sp2/0 cells that co-express patient-derived amyloidogenic LC and HC proteins. The system was designed using amyloidogenic kappa and lambda LC, and gamma HC sequences; stable production and secretion of either free LC and/or intact Ig were accomplished by varying the LC to HC ratios. This novel cell-based system provides a relevant tool to systematically investigate LC and HC interactions, and the molecular events leading to the development of AL amyloidosis.
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“In other disease areas, including organ fibrosis, several examples exist in which a mutation at one site can affect PTM profiles elsewhere on the protein 53-55 .”
From How many human proteoforms are there? (2018) · cites this paper as [54]
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How many human proteoforms are there?
Aebersold, R., Agar, J. N., Amster, I. J., Baker, M. S., Bertozzi, C. R., Boja, E. S., Costello, C. E., Cravatt, B. F., Fenselau, C., Garcia, B. A., et al. (2018) · Nature Chemical Biology · doi:10.1038/nchembio.2576 · Cited by 907
Metadata
- Authors
- Klimtchuk, E. S., Prokaeva, T. B., Spencer, B. H., Gursky, O., & Connors, L. H.
- Affiliations
- Boston University (US)
- Corresponding author
- Klimtchuk, Elena S.
- Venue
- Amyloid
- Publisher
- Informa UK Limited
- Published
- 2017-04-03
- Volume
- 24
- Issue
- 2
- Pages
- 115-122
- ISSN
- 1350-6129 (ISSN-L)
- 1744-2818
- PMC
- PMC5580339
- OpenAlex
- W2681602274
- Cited by
- 10
- References
- 22
- Citations by year
- 2025: 5 · 2024: 1 · 2023: 1 · 2022: 1 · 2020: 1 · 2018: 1
- FWCI
- 0.22
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Amyloid (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Wildflower Foundation
- Gruss Foundation
- Stewart Amyloidosis Research Endowment Fund
- National Institutes of Health (GM067260)
- Topics
- Health Sciences › Medicine › Internal Medicine › Amyloidosis: Diagnosis, Treatment, Outcomes
- Health Sciences › Medicine › Hematology › Multiple Myeloma Research and Treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Keywords
- AL amyloidosis, immunoglobulin light chain amyloidosis, monoclonal immunoglobulin light chains, immunoglobulin heavy chain, free light chains, amyloidogenic light chains, kappa light chain, lambda light chain, gamma heavy chain, cell-based models, amyloid deposition
- MeSH terms
- Immunoglobulin Light-chain Amyloidosis, Aged, Amyloid, Animals, Female, Humans, Immunoglobulin Variable Region, Immunoglobulin Heavy Chains, Immunoglobulin Light Chains, Male, Models, Biological, Mice
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