familial amyloidosis
The familial amyloidoses constitute a group of autosomal dominant diseases in which a mutant protein forms amyloid fibrils beginning in midlife.
The most common form is caused by mutant transthyretin (TTR); however, mutations of apolipoprotein A-I, gelsolin (GSN), fibrinogen A , and lysozyme (LYZ) also lead to amyloidosis.
Types
familial visceral amyloidosis (amyloidosis type 8) (MIM.105200)
Etiology
transthyretin-associated amyloidosis (TTR-associated amyloidosis)
APOA1-associated amyloidosis (apolipoprotein A-I)
gelsolin-associated amyloidosis (GSN)-associated amyloidosis
fibrinogen A-associated amyloidosis
lysozyme-associated amyloidosis (LYZ-associated amyloidosis or amyloidosis type 8) (MIM.105200)
Lysozyme (LYZ) consists of a single polypeptide with a predominantly helical structure. Four pathogenic variants of lysozyme have been reported; a fifth variant, Thr70Asn, is apparently not pathogenic.
See also
amyloidoses