The presence of methionine at codon 129 is distinct for FFI compared to valine at the same position in familial Creutzfeldt-Jakob disease (fCJD). The disease-causing mutation consists of substitution from the normal aspartic acid (Asp) to asparagine (Asn). The cause of FFI has been identified as an autosomal dominant mutation at the codon 178 of the PRNP gene, located on the short (p) arm of chromosome 20 at position p13 responsible for making the prion protein PrPC. et al., followed by subsequent studies, further describing its pathophysiology, etiology, and clinical course. The disease was formally identified and clinically described in 1986 by Lugaresi E. The earliest description of the disease dates back to 1765 with a report of an Italian man with symptoms suggestive of FFI. The disease is currently incurable and has a mean course of 18 months, ultimately leading to death. Aggressively progressive insomnia, with subsequent autonomic (tachycardia, hyperhidrosis, hypertension), cognitive (short-term memory and attentional deficits), motor system (balance problems), and endocrine dysfunction are a hallmark of the disease. The mode of inheritance of this disease is autosomal dominant and involves a mutation of the prion protein (PRNP) gene.
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