Fibril in senile systemic amyloidosis is derived from normal transthyretin.

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  • P Westermark
    Department of Pathology, University of Linköping, Sweden.
  • K Sletten
    Department of Pathology, University of Linköping, Sweden.
  • B Johansson
    Department of Pathology, University of Linköping, Sweden.
  • G G Cornwell
    Department of Pathology, University of Linköping, Sweden.

説明

<jats:p>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.</jats:p>

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