Transthyretin amyloidosis associated with a novel variant (Trp41Leu) presenting with vitreous opacities.
We report a 45-year-old woman with a new transthyretin (TTR) variant, substitution of leucine for tryptophan at residue 41, who has showed vitreous opacities without any other visceral organ involvement since age of 42. Congo red staining of vitrectomy specimens revealed that the vitreous fluid contained amyloid fibrils, which were strongly positive for immunohistochemical staining using anti-human TTR antiserum. DNA analysis of the TTR gene showed a G to T transversion at the second nucleotide of codon 41, indicating a replacement of tryptophan (TGG) by leucine (TTG). These results indicate that the patient's vitreous amyloid is associated with this novel TTR mutation.
Yazaki
Masahide
M
Department of Pathology & Laboratory Medicine, Indiana University School of Medicine, 975 West Walnut Street, Indianapolis, IN 46202-5121, USA.
Connors
Lawreen H
LH
Eagle
Ralph C
RC
Leff
Steven R
SR
Skinner
Martha
M
Benson
Merrill D
MD
D000686:Amyloidosis / Q000150:complications / Q000235:genetics / Q000473:pathology*; D001483:Base Sequence; D005128:Eye Diseases / Q000150:complications*; D005260:Female; D006801:Humans; D007930:Leucine / Q000235:genetics*; D008875:Middle Aged; D009154:Mutation; D012150:Polymorphism, Restriction Fragment Length; D011228:Prealbumin / Q000737:chemistry / Q000235:genetics*; D014364:Tryptophan / Q000235:genetics*; D014822:Vitreous Body / Q000473:pathology*
D011228:Prealbumin; D014364:Tryptophan; D007930:Leucine