A new mutant transthyretin (Arg 10) associated with familial amyloid polyneuropathy. Issue 12 (December 1992)

• Record Type: Journal Article
• Authors: Uemichi, T; Murrell, J R; Zeldenrust, S; Benson, M D
• Is Part Of: Journal of medical genetics. Volume 29:Issue 12(1992)
• Page Start: 888
• Page End: 891
• Publication Date: 1992-12
• Subjects: Medical genetics -- Periodicals; 616.042
• DOI: 10.1136/jmg.29.12.888
• Languages: English
• ISSNs: 1468-6244

Abstract

Abstract : We report a new kindred with systemic amyloidosis presenting as peripheral neuropathy in the sixth and seventh decades of life. Polymorphism in exon 2 of the transthyretin (TTR) gene was suggested by single strand conformation polymorphism analysis and determined by direct DNA sequencing. We also developed restriction fragment length polymorphism analysis by polymerase chain reaction using a primer with an induced mutation. The point mutation (cytosine for thymine at position 1038 of the TTR gene) is responsible for substitution of arginine for cysteine at position 10 of the TTR molecule. It is hypothesised that the TTR molecules which have no cysteine have a unique structure in heterozygous TTR polymers and are responsible for amyloid fibril formation.