Widespread amyloidogenicity potential of multiple myeloma patient-derived immunoglobulin light chains.

Rebecca Sternke-HoffmannThomas PaulyRasmus K NorrildJan HansenFlorian TucholskiMagnus Haraldson HøiePaolo MarcatiliMathieu DupréMagalie DuchateauMartial ReyChristian MalosseSabine MetzgerAmelie BoquoiFlorian PlattenStefan U EgelhaafJulia Chamot-RookeRoland FenkLuitgard Nagel-StegerRainer HaasAlexander K Buell

Published in: BMC biology (2023)

We show that (I) in vivo aggregation behaviour is unlikely to be mechanistically linked to any single biophysical or biochemical parameter and (II) amyloidogenic potential is widespread in IgLC sequences and is not confined to those sequences that form amyloid fibrils in patients. Our findings suggest that protein sequence, environmental conditions and presence and action of proteases all determine the ability of light chains to form amyloid fibrils in patients.

Keyphrases

end stage renal disease
newly diagnosed
ejection fraction
multiple myeloma
human health
risk assessment
binding protein
protein protein