Current treatment of AL amyloidosis

Immunoglobulin light chain systemic amyloidosis(AL) is a progressive disease caused by monoclonallight chains with specific mutations that confer a unique propensity to misfold from their native structure to less stable, partially folded intermediates that self-aggregate into oligomers and then into the highly-ordered cross β-sheet structure which defines amyloid fibrils.1 At least 11 additional proteins, synthesized by different organs (liver, intestine, etc) can cause systemic amyloidoses which can be difficult to distinguish from AL amyloidosis on a clinical basis. These proteins form amyloid deposits that share the common tinctorial, green birefringence under polarized light after staining with Congo red, and ultrastructural features, rigid, non-branching fibril with a distinct diameter of 7.5 to 10 nm (Figure 1). The unequivocal identification of the protein forming the amyloid fibril is essential for the choice of