These findings are typical for patients which develop AL amyloidosis (primary amyloidosis). A serum free light chains assay was performed, showing a marked increase of λ light chains, with a κ/λ ratio of 0.09, indicating the presence of a population of plasma cells producing clonal λ free light chains.To complete the work-up for the extension of the disease, a lower limb electromiography was performed, which showed sensitive and motor polineuropathy.
Cardiac involvment carries a worse prognosis than any other organ involvement3.
Patients with cardiac amyloidosis present with signs and symptoms of heart failure, with progressive dyspnea, peripheral edema and angina, typical or atypical, due to involvement of the small vessels of the heart by the amyloid deposition.
The dermatological manifestations of the disease include easy bruising and periorbital purpura, the latter being pathognomonic for AL amyloidosis. Blood pressure is often low, due to decreased cardiac output in conjunction with early autonomic dysfunction, and in hypertensive patients there is frequently a history of normalization of blood pressure values with the onset of amyloidosis.
Pleural effusions and hepatomegaly are frequent, both as a manifestation of congestive heart failure and as a sign of pleural or hepatic involvement of the disease3.
The laboratory workup shows elevated NT-pro BNP (2800 pg/ml) and troponin I (0.079 ng/ml), the rest was unremarkable.
Renal function was normal, and there was no proteinuria.
Echocardiography shows typical features in cardiac amyloidosis: concentric left (and sometimes right) ventricular wall thickening, infiltration of the atrial septum, dilation of the atria, often inceased echogenicity of the valves.
The myocardial texture is particular, with increased echogenicity and sometimes granular sparkling (an aspect that is not specific for amyloidosis).
Amyloidosis represents a group of diseases, characterized by the extracellular deposition of a homogenous material, the amyloid, consisting of fibrils formed by proteins folded in the beta-sheet form.
The inertness of amyloid fibrils and their resistance to proteolysis are responsible for their accumulation in tissues and their eventual interference with vital functions.