Differential effects on light chain amyloid formation depend on mutations and type of glycosaminoglycans.

ABSTRACT: Amyloid light chain (AL) amyloidosis is a protein misfolding disease where immunoglobulin light chains sample partially folded states that lead to misfolding and amyloid formation, resulting in organ dysfunction and death. In vivo, amyloid deposits are found in the extracellular space and involve a variety of accessory molecules, such as glycosaminoglycans, one of the main components of the extracellular matrix. Glycosaminoglycans are a group of negatively charged heteropolysaccharides composed of repeating disaccharide units. In this study, we investigated the effect of glycosaminoglycans on the kinetics of amyloid fibril formation of three AL cardiac amyloidosis light chains. These proteins have similar thermodynamic stability but exhibit different kinetics of fibril formation. We also s

SUBMITTER: Blancas-Mejia LM 

PROVIDER: S-EPMC4335233 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature