Document Type
Article
Publication Date
4-1990
Publication Title
Proceedings of the National Academy of Sciences of the United States of America
Department
Geisel School of Medicine
Abstract
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.
Original Citation
Westermark P, Sletten K, Johansson B, Cornwell GG 3rd. Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proc Natl Acad Sci U S A. 1990;87(7):2843-2845. doi:10.1073/pnas.87.7.2843
Dartmouth Digital Commons Citation
Westermark, Per; Sletten, Knut; Johansson, Bjorn; and Cornwell, Gibbons G., "Fibril in Senile Systemic Amyloidosis is Derived from Normal Transthyretin." (1990). Dartmouth Scholarship. 1371.
https://digitalcommons.dartmouth.edu/facoa/1371
