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The transthyretin cDNA sequence is normal in transthyretin-derived senile systemic amyloidosis.
Department of Pathology, University of Uppsala, Sweden.
A variety of mutations leading to amino acid substitutions have been described in the transthyretin gene in association with different familial amyloidoses and have been implicated to be involved in the pathogenesis of amyloid deposits. However, there has been disagreement whether or not a transthyretin mutation is present in the most common form of transthyretin-derived amyloid, namely senile systemic amyloidosis. Therefore, the cDNA sequence of liver transthyretin was determined in a 91-year-old patient with typical senile systemic amyloidosis. This sequence was completely normal and lacked any variation. We conclude that in senile systemic amyloidosis factors other than the presence of a sequentially variant transthyretin must determine the amyloid fibril formation.
PMID: 2015890 [PubMed - indexed for MEDLINE]
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Cited by 5 PubMed Central articles
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A new isoleucine substitution of Val-20 in transthyretin tetramers selectively impairs dimer-dimer contacts and causes systemic amyloidosis.
Jenne DE, Denzel K, Blätzinger P, Winter P, Obermaier B, Linke RP, Altland K.
Proc Natl Acad Sci U S A. 1996 Jun 25; 93(13):6302-7.
[Proc Natl Acad Sci U S A. 1996]
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ReviewThe age related amyloids: a growing family of unique biochemical substances.
Cornwell GG 3rd, Johnson KH, Westermark P.
J Clin Pathol. 1995 Nov; 48(11):984-9.
[J Clin Pathol. 1995]
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Structure of Met30 variant of transthyretin and its amyloidogenic implications.
Terry CJ, Damas AM, Oliveira P, Saraiva MJ, Alves IL, Costa PP, Matias PM, Sakaki Y, Blake CC.
EMBO J. 1993 Feb; 12(2):735-41.
[EMBO J. 1993]
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