FIBRIL IN SENILE SYSTEMIC AMYLOIDOSIS IS DERIVED FROM NORMAL TRANSTHYRETIN
FIBRIL IN SENILE SYSTEMIC AMYLOIDOSIS IS DERIVED FROM NORMAL TRANSTHYRETIN
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DOI：
10.1073/pnas.87.7.2843
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发表时间：
1990-04-01
影响因子：
11.1
通讯作者：
CORNWELL, GG
中科院分区：
文献类型：
--
作者：
WESTERMARK, P;SLETTEN, K;CORNWELL, GG
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 > 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.
