To date, seven different single amino acid mutations in the plasma protein prealbumin (transthyretin) have been found to be associated with amyloidosis and each is the result of a single nucleotide change in the prealbumin gene.
A DNA polymorphic site, 5' to the serum amyloid P component gene, has been found to be significantly associated with amyloidosis in juvenile arthritic patients.
A variant of cystatin C lacking the first NH2-terminal residues and having one amino acid substitution at position 68 forms amyloid deposits mainly in the walls of brain arteries, causing fatal strokes in Icelandic patients with familial cerebral hemorrhage secondary to a form of an autosomal dominant amyloidosis.
Overexpression of amyloid precursor protein A4 (beta-amyloid) immunoreactivity in genetically transformed cells: implications for a cellular model of Alzheimer amyloidosis.
Whereas in Down's syndrome, over-expression of the gene coding for PreA4 is likely to be responsible for the premature development of cerebral amyloidosis, a similar mechanism is yet to be demonstrated in Alzheimer's disease.
The effects of 4 proteolytic enzymes, alpha-chymotrypsin, bromeline, collagenase, and lysozyme on amyloid tissue sections from a patient with familial amyloidotic polyneuropathy (FAP) were evaluated.
Autosomal dominant amyloidosis, also known as familial amyloidotic polyneuropathy (FAP), is a late-onset disorder associated with variants of the protein prealbumin.
This is the sixth prealbumin variant implicated in amyloidosis, and adds to the accumulating evidence that the prealbuminamyloidoses are more varied and prevalent than previously thought.
AmyloidB-protein/amyloid A4 is a peptide present in the neuritic plaques, neurofibrillary tangles and cerebrovascular deposits in patients with Alzheimer's disease and Down's syndrome (trisomy 21) and may be involved in the pathogenesis of Alzheimer's disease.
These observations indicate the same methionine for valine substitution at position 30 of the transthyretin molecule in patients with vitreous amyloidosis as seen in Swedish patients with FAP as well as in patients with FAP from Japan and Portugal, and patients of Swedish descent with FAP from the United States.
Because only SAA2-derived products deposit in mouse amyloid tissues, the resistance of SJL mice to amyloidosis seems to be due to defective SAA2 gene expression.
The immunoperoxidase method, the autoclave method, and a newly developed alkaline-guanidine method were used to distinguish senile (SSA) and familial types (FAP) of prealbumin-related amyloidosis in formalin-fixed, paraffin-embedded tissue sections.
In recent years prealbumin has been shown to be a major component of two forms of systemic amyloid, senile systemic amyloid (SSA), and familial amyloidotic polyneuropathy (FAP).
Sequence analysis of the isolated peptides confirms this observation and shows that the 3 Brazilian families investigated in our study have the same prealbumin variant as individuals with amyloidosis of Swedish/American, Portuguese and Japanese origins.
By radioimmunoassay, the serum level of prealbumin was measured in 25 patients from 12 different kinships with this dominantly inherited form of amyloidosis and 56 unaffected, but at risk, relatives from two of the kinships.
Since the serum levels of the acute phase reactants, haptoglobin and amyloid-related serum protein AA, were higher in the group of patients with reactive amyloidosis than in patients with SSA, the depression of the prealbumin levels in SSA is not a result of inflammation.
Amyloid deposits in several heredofamilial forms of amyloidosis are chemically related to transthyretin (TTR, the protein usually referred to as prealbumin).