Amylozy

Amylozy, commonly referred to as amyloidosis in English, denotes a group of diseases characterized by extracellular deposition of amyloid, misfolded protein aggregates, in tissues and organs. Amyloid fibrils are formed when normally soluble proteins misfold and assemble into stable, β-pleated sheets that resist normal degradation and accumulate over time, impairing organ function.

Clinical presentation varies by affected organ but often includes kidney involvement with proteinuria, heart involvement causing restrictive cardiomyopathy or heart failure, liver enlargement, neuropathy, and gastrointestinal symptoms. Because signs are diverse, amylozy is often suspected after abnormal protein studies or imaging, followed by tissue biopsy to confirm amyloid deposition and determine subtype.

Main forms include AL (light-chain) amyloidosis, usually associated with plasma cell disorders; AA (serum amyloid A) amyloidosis linked to chronic inflammatory disease; ATTR amyloidosis due to transthyretin, which can be hereditary or age-related; and dialysis-related β2-microglobulin amyloidosis. Less common hereditary forms arise from variants in other proteins such as fibrinogen or apolipoprotein.

Diagnosis relies on tissue Congo red staining with apple-green birefringence under polarized light and analysis of the amyloid subtype by proteomic methods or targeted blood and urine tests (for light chains) and imaging. Specific noninvasive scans can help distinguish ATTR from other forms, such as nuclear medicine ATTR scans. Management focuses on treating the underlying cause, relieving symptoms, and supporting organ function.

Prognosis and therapy depend on the type and extent of organ involvement. AL amyloidosis requires systemic therapy and sometimes stem cell transplantation; ATTR forms may respond to transthyretin stabilizers or gene-silencing therapies. Amylozy remains a rare disease with improving outcomes due to advancing diagnostics and targeted treatments.