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1: Proc Natl Acad Sci U S A. 1990 Apr;87(7):2843-5.Click here to read Links

Fibril in senile systemic amyloidosis is derived from normal transthyretin.

Westermark P, Sletten K, Johansson B, Cornwell GG 3rd.

Department of Pathology, University of Linköping, Sweden.

The amyloid fibril in senile systemic amyloidosis (SSA), like that of familial amyloidotic polyneuropathy, is derived from transthyretin (TTR). SSA, however, is a common disease, affecting to some degree 25% of the population greater than 80 years old. In familial amyloidotic polyneuropathy, the amyloidogenesis has been considered to depend on point mutations leading to TTR variants. We show that the TTR molecule in SSA, on the other hand, has a normal primary structure. Factors other than the primary structure of TTR must therefore be important in the pathogenesis of TTR-derived amyloid.

PMID: 2320592 [PubMed - indexed for MEDLINE]

PMCID: PMC53787