A new transthyretin variant from a patient with familial amyloidotic polyneuropathy has asparagine substituted for histidine at position 90
| Autor: | Aubrey Milunsky, Martha Skinner, Jeff M. Milunsky, James Skare, Ilze B. Skare, Alan S. Cohen |
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| Rok vydání: | 2008 |
| Předmět: |
Molecular Sequence Data
Cleavage (embryo) Polymerase Chain Reaction Exon Genetics medicine Humans Prealbumin Histidine Amino Acid Sequence Asparagine Hereditary Sensory and Autonomic Neuropathies Genetics (clinical) Base Sequence biology Binding protein Nucleic acid sequence nutritional and metabolic diseases Amyloidosis medicine.disease Ion Exchange Transthyretin Biochemistry Mutation biology.protein Female Polyneuropathy |
| Zdroj: | Clinical Genetics. 39:6-12 |
| ISSN: | 1399-0004 0009-9163 |
| DOI: | 10.1111/j.1399-0004.1991.tb02979.x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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