June 2015
Volume 56, Issue 7
ARVO Annual Meeting Abstract  |   June 2015
A novel transthyretin mutation (Gly87Arg) in a Caucasian kindred with vitreous amyloidosis.
Author Affiliations & Notes
  • Camille Estelle M. Van Mierlo
    Dept of Ophthalmology, University Hospitals of Leuven, Leuven, Belgium
  • Rita Van Ginderdeuren
    Dept of Ophthalmology, University Hospitals of Leuven, Leuven, Belgium
  • Bart Peter Leroy
    Dept of Ophthalmology & Ctr for Medical Genetics, Ghent University Hospital & Ghent University, Ghent, Belgium
    Div of Ophthalmology & Ctr for Molecular & Cellular Therapeutics, Children's Hospital of Philadelphia, Philadelphia, PA
  • Joachim Van Calster
    Dept of Ophthalmology, University Hospitals of Leuven, Leuven, Belgium
  • Footnotes
    Commercial Relationships Camille Van Mierlo, None; Rita Van Ginderdeuren, None; Bart Leroy, None; Joachim Van Calster, Allergan (C), Allergan (R), Bausch&Lomb (F), Bayer (C), Bayer (R), DORC (C), DORC (R), MSD (C), Novartis (C), Novartis (F), Novartis (R)
  • Footnotes
    Support None
Investigative Ophthalmology & Visual Science June 2015, Vol.56, 788. doi:
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      Camille Estelle M. Van Mierlo, Rita Van Ginderdeuren, Bart Peter Leroy, Joachim Van Calster; A novel transthyretin mutation (Gly87Arg) in a Caucasian kindred with vitreous amyloidosis.. Invest. Ophthalmol. Vis. Sci. 2015;56(7 ):788.

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      © ARVO (1962-2015); The Authors (2016-present)

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Purpose: To report a case-series from a Caucasian kindred with vitreous amyloidosis associated with the novel Gly87Arg mutation in the transthyretin (TTR) gene.

Methods: We report a Caucasian family with vitreous amyloidosis, consisting of four symptomatic siblings: 3 women and 1 man, 53-59 yo. All underwent an extensive ocular evaluation. A diagnostic-therapeutic 23-gauge sutureless pars plana vitrectomy was performed in all patients. Histopathology of vitreous samples was performed. DNA was extracted from peripheral blood cells and subjected to amplification, followed by sequencing of the four exons and exon-intron boundaries of the TTR gene. In silico analysis with SIFT and MutationTaster was used to predict potential pathogenicity of the mutation. One other unaffected sister (56 yo) was also examined.

Results: Clinical examination showed a typical ocular phenotype of amyloidosis, with multiple vitreous densities without cellular infiltration in the four symptomatic siblings, and was normal in the asymptomatic sibling. Histopathology of vitreous samples (6 eyes) revealed amyloid deposits (staining with Congo red and/or Toluidine blue). A heterozygous mutation c.259 G>C (p.Gly87Arg) in exon 3 of the TTR gene (with a highly conserved glycine residue at position 87) was identified in the three affected sisters, whereas this mutation was not present in the unaffected sister. The affected brother died of a cardiovascular accident (after embolization of a cerebellar arteriovenous malformation) before genetic testing was performed. In silico analysis of the mutation predicted pathogenicity. General history and examination revealed a hereditary heterozygous factor V Leiden mutation in the siblings, transient ischemic attacks in the two affected sisters and brother and an early onset dementia in one affected sister.

Conclusions: Our findings strongly suggest an association between the heterozygous Gly87Arg mutation in the TTR gene and familial vitreous amyloidosis. This pathogenic variant has not been previously described in the literature.


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