A novel variant of transthyretin (Glu42Asp) associated with sporadic late-onset cardiac amyloidosis.
A sixty-three year old French man presented with isolated late-onset amyloid cardiomyopathy proven by endomyocardial biopsy. There was no known family history of amyloidosis. Immunohistochemistry of cardiac deposits suggested that amyloi fibrils were derived from transthyretin. DNA sequencing revealed a point mutation in exon 2 of the transthyretin gene responsible for a novel amyloidogenic variant Asp42.
Laboratoire de Biochimie Génétique, Hôpital Cochin, Paris, France.
O
O
Dupuy
O
O
Blétry
A S
AS
Blanc
D
D
Droz
M
M
Viémont
M
M
Delpech
G
G
Grateau
D017668:Age of Onset; D019943:Amino Acid Substitution; D000686:Amyloidosis / Q000235:genetics*; D001224:Aspartic Acid / Q000235:genetics*; D001483:Base Sequence; D004247:DNA; D018698:Glutamic Acid / Q000235:genetics*; D006331:Heart Diseases / Q000235:genetics*; D006801:Humans; D007150:Immunohistochemistry; D008297:Male; D008875:Middle Aged; D016133:Polymerase Chain Reaction; D011228:Prealbumin / Q000737:chemistry / Q000235:genetics*
D011228:Prealbumin; D001224:Aspartic Acid; D018698:Glutamic Acid; D004247:DNA