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PMID: 2320592 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Fibril in senile systemic amyloidosis is derived from normal transthyretin.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 87 ·No. 7 ·1990-04-00 ·Pages 2843-5

Westermark P, Sletten K, Johansson B, Cornwell GG

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.

MeSH Terms
Amino Acid Sequence Amyloid/isolation & purification Amyloidosis/metabolism,pathology Chromatography, Gel Cyanogen Bromide Humans Molecular Sequence Data Myocardium/metabolism,pathology Peptide Fragments/isolation & purification Prealbumin/metabolism
Chemicals
Amyloid Peptide Fragments Prealbumin Cyanogen Bromide
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Westermark P
Department of Pathology, University of Linköping, Sweden.
Sletten K
Johansson B
Cornwell G G
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.87.7.2843
Published
1990-04-00
Pages
2843-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC53787
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.87.7.2843 PMC Full Text View journal details
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