Tracheobronchial amyloidosis: A surgical disease with long-term consequences

Abstract

Amyloidosis results from abnormal protein deposition and accumulation in extracellular spaces. The multiple distinct forms of this disease have heterogeneous clinical manifestations and variable patterns of organ involvement. Amyloidosis might be hereditary or acquired, localized, or systemic and can range from an incidental asymptomatic finding to a lethal disorder. The diseases are distinguished on a molecular level by the type of peptide subunits that compose abnormally accumulated protein fibrils. Although these peptide fibrils differ, all amyloid fibrils adopt a similar ultrastructure rich in -sheet content. The fibril deposits also have a common association with certain glycosaminoglycans (GAGs), notably heparin and dermatan sulphate. Normal plasma proteins, such as serum amyloid P (SAP), function to stabilize the amyloid fibril. We present a case of severe tracheobronchial amyloidosis (TBA) with the results of our evaluation and management strategies.