Purpose. Transthyretin (prealbumin) functions as a transport protein for thyroxine and retinal binding protein. Mutations in the coding sequence of the gene for this protein are responsible for amyloid (mutant transthyretin) deposition in familial amyloidotic polyneuropathy. Vitreous amyloidosis is a common finding in types I and II familial amyloidosis, and to date transthyretin mutations have been identified in all cases of vitreous amyloidosis that have been examined at the molecular level. In order to investigate the role of this gene in isolated cases of amyloidosis, we analyzed the transthyretin gene in a patient with bilateral vitreous amyloidosis without systemic or familial involvement. Methods. The patient is a 71 year-old otherwise healthy woman who presented with complaints of visually significant floaters in each eye. Ophthalmic examination revealed white vitreous deposits many of which were on strands as well as several yellowish deposits deep to the retina. She underwent vitreous biopsy and pars plana vitrectomy in each eye. Histopathology was performed on the surgical specimen. To identify an amyloidogenic mutation of the transthyretin gene, direct genomic sequencing of the entire coding region of the transthyretin gene was carried out on her leucocyte DNA. Results. Histopathology of the vitreous biopsy yielded Congophilic, birefringent round lobules, diagnostic of amyloic. Direct genomic sequencing of two separate blood samples revealed no transthyretin mutation in the leukocyte DNA. Conclusions. This patient with both clinical and biopsy-proven vitreous amyloidosis represents the first reported case of vitreous amyloidosis without a transthyretin mutation.
|Original language||English (US)|
|Journal||Investigative Ophthalmology and Visual Science|
|State||Published - Feb 15 1996|
ASJC Scopus subject areas
- Sensory Systems
- Cellular and Molecular Neuroscience