Amyloidosis is caused by protein that is deposited as insoluble fibrils, mainly in the extracellular spaces of organs and tissues, as a result of changes in protein folding. Over 30 human proteins have been associated with different types of amyloidosis (Sipe et al., 2014; pubmed:25263598); intracellular protein inclusions are not typically included in this category (although they may be described as amyloid-like). Visceral amyloidoses involve organs other than the central nervous system, especially kidneys and heart. Diagnosis requires tissue biopsy to confirm the presence of amyloid deposits.
In flies, one of the three genes implicated in familial visceral amyloidosis has been used to model the human disease: see the report for amyloidosis, familial visceral, LYZ-related (FBhh0000350).
[updated Jul. 2016 by FlyBase; FBrf0222196]
A hereditary generalized amyloidosis in which viscera are particularly affected; there is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash. (UniProt:P61626; 2016.07.29)
Familial visceral amyloidosis exhibits autosomal dominant inheritance. [from MIM:105200; 2017.06.05]
Systemic nonneuropathic amyloidosis can be the result of mutation in the apolipoprotein A1 gene (APOA1), the fibrinogen alpha-chain gene (FGA), or the lysozyme gene (LYZ).[from MIM:105200; 2016.07.29]
