Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin.
Familial amyloidosis in different kindreds is associated with a variety of point mutations in the prealbumin gene, resulting in prealbumin variants which are believed to be amyloidogenic, i.e. prone to form amyloid fibrils. In the most common amyloid-associated variant, there is a methionine for valine substitution in position 30. We have studied the prealbumin-derived amyloid protein ASc1 in the common age-related senile systemic amyloidosis. Evidence is presented that there is no abnormality in the primary structure of prealbumin in this disease and that, in addition to complete prealbumin, fibrils contain prealbumin fragments lacking a significant part of the N-terminus.
D000368:Aged; D000369:Aged, 80 and over; D000595:Amino Acid Sequence; D000686:Amyloidosis / Q000378:metabolism*; D006801:Humans; D005779:Immunodiffusion; D008969:Molecular Sequence Data; D009206:Myocardium / Q000032:analysis; D011228:Prealbumin / Q000032:analysis*; D000685:Serum Amyloid A Protein / Q000032:analysis*
D011228:Prealbumin; D000685:Serum Amyloid A Protein