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- Title
Mutations in specific structural regions of immunoglobulin light chains are associated with free light chain levels in patients with AL amyloidosis.
- Authors
Poshusta, Tanya L; Sikkink, Laura A; Leung, Nelson; Clark, Raynell J; Dispenzieri, Angela; Ramirez-Alvarado, Marina
- Abstract
The amyloidoses are protein misfolding diseases characterized by the deposition of amyloid that leads to cell death and tissue degeneration. In immunoglobulin light chain amyloidosis (AL), each patient has a unique monoclonal immunoglobulin light chain (LC) that forms amyloid deposits. Somatic mutations in AL LCs make these proteins less thermodynamically stable than their non-amyloidogenic counterparts, leading to misfolding and ultimately the formation of amyloid fibrils. We hypothesize that location rather than number of non-conservative mutations determines the amyloidogenicity of light chains.
- Publication
PloS one, 2009, Vol 4, Issue 4, pe5169
- ISSN
1932-6203
- Publication type
Journal Article
- DOI
10.1371/journal.pone.0005169