A new transthyretin variant from a patient with familial amyloidotic polyneuropathy has asparagine substituted for histidine at position 90
作者:
James C. Skare,
Jeffrey M. Milunsky,
Aubrey Milunsky,
Ilze B. Skare,
Alan S. Cohen,
Martha Skinner,
期刊:
Clinical Genetics
(WILEY Available online 1991)
卷期:
Volume 39,
issue 1
页码: 6-12
ISSN:0009-9163
年代: 1991
DOI:10.1111/j.1399-0004.1991.tb02979.x
出版商: Blackwell Publishing Ltd
关键词: amyloid;familial amyloidotic polyneuropathy;transthyretin
数据来源: WILEY
摘要:
A new transthyretin variant which lost an Sph I cleavage site within exon 3 has been characterized. A 260 bp sequence containing exon 3 was amplified using the polymerase chain reaction, and the variant was found to possess a Bsm I cleavage site not present in normal transthyretin. This led to the conclusion that the histidine at position 90 was replaced by asparagine, and amino acid analysis supported the conclusion. The discovery of this mutation suggests that intermolecular binding between hydrophobic polypeptide loops on the surface of transthyretin can lead to familial amyloidotic polyneuropathy.
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