Systemic amyloidosis is caused by conversion of peptides or proteins from their soluble functional states into highly organized amyloid fibrillar aggregates resulting in the dysfunction of vital organs. The process of amyloid formation, organ targeting, and damage is complex and only partially understood. Because of the progressive nature of the disease, early diagnosis is vital to prevent irreversible organ damage. Polyneuropathy is the hallmark of hereditary transthyretin amyloidosis, and is present in approximately 15% of patients with immunoglobulin light chain amyloidosis (AL), which is the most common type of systemic amyloidosis. The polyneuropathy is typically nerve length-dependent that starts in the feet with loss of temperature and pain sensations, along with life-threatening autonomic dysfunction. The development of novel sensitive biomarkers and imaging technologies for the detection and quantification of organ involvement and damage are facilitating earlier diagnosis and enhanced evaluation of the efficacy of new and existing therapies. In AL amyloidosis, several new classes of drugs, such as proteasome inhibitors and immunomodulatory drugs, along with high-dose chemotherapy and autologous haematopoietic stem cell transplantation, have led to rapid and deep suppression of the amyloid precursor in the majority of patients. Passive immunotherapies directly accelerating removal of amyloid deposits promise to further improve the overall outlook of this increasingly treatable disease.
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