Although prior in vitro studies have shown that Apo-CII can form amyloid fibrils and that certain mutations in this protein promote amyloid fibrillogenesis, there are no reports of this type of amyloidosis in humans.
Although not described previously, elevated IOP may develop in patients with vitreous amyloidosis due to a TTR Val30Gly mutation in the transthyretin gene.
Analysis of guanidine hydrochloride solubilized protein from isolated vitreous and cardiac amyloid fibrils indicated that the amyloidTTR in both organs is highly proteolyzed with minor amounts of intact TTR present.
Although amyloidogenic transthyretin (ATTR) mutations are common in several populations, such as black Americans, the small number of diagnosed patients homozygous for TTRamyloid and the short follow up in most studies has until now prevented an analysis of their phenotype.
Alzheimer's disease (AD) is characterized by pathological lesions, such as senile plaques (SPs) and cerebral amyloid angiopathy (CAA), both predominantly consisting of a proteolytic cleavage product of the amyloid-beta precursor protein (APP), the amyloid-beta peptide (Abeta).
Though the effects of the MEFV genotypes seem clear, there are definitely other modifying factors or genes on the development of amyloidosis and on the course of the disease.
The aim of this study was to examine the controversial issue of amyloidosis susceptibility in FMF by determining the relative contributions of MEFV and numerous epidemiologic factors to the risk of renal amyloidosis.