In the prototypic Portuguese (autosomal dominant) familial amyloid polyneuropathy, transthyretin (prealbumin) variants have been found to constitute the amyloid. This molecule circulates as a 55 kDa tetramer composed of 4 identical 127 amino acid monomers. This molecule is a carrier of thyroxine and of retinol binding protein. It also acts as a negative acute phase reactant. It is determined by one gene located on chromosome 18. The most common abnormality is the substitution of methionine for valine at position 30 in families of Portuguese, Swedish,

Japanese, Italian, and Greek origin. Substitutions in the families with other phenotypic expression occur at over 50 other positions. Several different mutations may be present at one position (i.e. 30, 33, 35, 45, 47, 50, 58, 84). Hereditary amyloid composed of variant apolipoprotein Al, of the proteins gelsolin, fibrinogen Aa, lysozyme and of (3 protein have also been described, each in a different clinical syndrome.

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