What condition results from abnormal protein folding leading to aggregation in cells?

Prion disease is characterized by abnormal protein folding that leads to the aggregation of proteins, forming insoluble fibrils that accumulate in neural tissue. These misfolded proteins, known as prions, induce normal proteins to misfold as well, resulting in a cascade effect that ultimately harms neuronal function and leads to neurodegeneration. This mechanism is central to several diseases, such as Creutzfeldt-Jakob disease and bovine spongiform encephalopathy, commonly known as mad cow disease.

In contrast, autosomal dominant disorders generally arise from specific mutations that affect gene function but do not primarily involve protein misfolding and aggregation as their pathological mechanism. Metabolic syndromes are related to a cluster of conditions affecting metabolism, and while they might involve protein abnormalities, they are not characterized by abnormal protein folding and aggregation. X-linked disorders stem from mutations in genes located on the X chromosome, which do not specifically involve protein misfolding leading to aggregation. Thus, prion disease stands out as the condition most directly associated with the consequences of abnormal protein folding.