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Amyloid fibril composition is related to the phenotype of hereditary transthyretin V30M amyloidosis
The Journal of Pathology, 09/02/08

Ihse E et al. - Variations in clinical appearance of familial ATTR amyloidosis are associated with specific structural differences in the amyloid fibrils, and therefore may have a molecular cause.

Methods

Aim was to see whether the morphological and biochemical variations in amyloid fibrils have clinical implications
Subcutaneous adipose tissue biopsies from 33 pts with Val30Met FAP were examined by microscopy, electrophoresis and western blot
Clinical data included age, sex, duration of disease and echocardiographic determination of the interventricular septum (IVS) thickness

Results

Fibrils composed of only full-length transthyretin were associated with early age of onset, no clinical cardiac involvement and a strong affinity for Congo red
Presence of transthyretin fragments in the amyloid was associated with late age of onset, signs of cardiac involvement and weak Congo red staining
For each individual, the same molecular type of amyloid was found in different organs

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