transthyretinamyloidoosi

Transthyretin amyloidoosi is a rare, progressive, and often underdiagnosed condition. It is characterized by the buildup of abnormal amyloid fibrils in various organs and tissues throughout the body. These fibrils are composed of misfolded transthyretin protein, which is normally involved in transporting thyroxine and retinol. When transthyretin misfolds, it can aggregate and deposit in areas such as the heart, nerves, kidneys, and eyes.

There are two main types of transthyretin amyloidoosi: hereditary (ATTRv) and wild-type (ATTRwt). Hereditary transthyretin amyloidoosi is caused by a mutation in the TTR gene, leading to the production of unstable transthyretin that readily misfolds. This type typically manifests earlier in life and can have a more severe progression. Wild-type transthyretin amyloidoosi, also known as senile systemic amyloidosis, occurs in older individuals without a genetic mutation and is associated with aging.

The symptoms of transthyretin amyloidoosi vary depending on the location and extent of amyloid deposition. Cardiac involvement can lead to restrictive cardiomyopathy, characterized by thickening of the heart walls, arrhythmias, and heart failure. Neurological symptoms may include peripheral neuropathy, causing numbness, tingling, and pain in the extremities, as well as autonomic dysfunction, affecting functions like blood pressure regulation and digestion. Other potential symptoms include carpal tunnel syndrome, edema, and kidney dysfunction. Diagnosis often involves a combination of clinical evaluation, imaging studies such as echocardiography, and tissue biopsy. Genetic testing is crucial for identifying hereditary forms. Treatment strategies aim to slow disease progression, manage symptoms, and improve quality of life. These can include medications that stabilize transthyretin, reduce its production, or manage specific organ dysfunction.