Amyloidosis is a collective term for diseases in which protein fibers, known as amyloid fibrils, are deposited in the body. Normally, proteins are soluble and degradable, but in amyloidosis, they become misfolded, making them insoluble and causing them to accumulate in organs and tissues. Without treatment, this can cause organs to swell and stiffen, eventually leading to death.
In systemic amyloidosis, these amyloid fibrils can be deposited in various organs and tissues, such as the heart, liver, kidneys, nerves, and gastrointestinal tract, causing symptoms to vary per patient. This variability makes diagnosis challenging, while an early diagnosis is essential to prevent further damage.
The availability of effective new drugs in the fight against systemic amyloidosis has drastically changed the field. Early recognition, accurate typing and correct risk stratification are now more critical than ever. This enables physicians to select and initiate treatment as early as possible, preventing or delaying further damage and improving prognosis. Since prognosis and treatment tolerance mainly depend on the extent of amyloid deposition and the number of vital organs affected, this thesis of Anne Floor Brunger investigates different markers that can be used for determining the extent of organ and/or tissue involvement in systemic amyloidosis: serum neurofilament light chain as marker for polyneuropathy, and liver stiffness to establish liver involvement. In AA amyloidosis another key factor in prognosis and treatment selection is identifying the underlying cause. Therefore, this thesis also studies the causality between different chronic inflammatory diseases and AA amyloidosis.
