Amyloid and Pro501Thr-mutated beta ig-h3 gene product colocalize in lattice corneal dystrophy type IIIA

Authors
Kawasaki, S Nishida, K Quantock, AJ Dota, A Bennett, K Kinoshita, S
Citation
S. Kawasaki et al., Amyloid and Pro501Thr-mutated beta ig-h3 gene product colocalize in lattice corneal dystrophy type IIIA, AM J OPHTH, 127(4), 1999, pp. 456-458
Citations number
5
Categorie Soggetti
Optalmology,"da verificare
Journal title
AMERICAN JOURNAL OF OPHTHALMOLOGY
ISSN journal
00029394 → ACNP
Volume
127
Issue
4
Year of publication
1999
Pages
456 - 458
Database
ISI
SICI code
0002-9394(199904)127:4<456:AAPBIG>2.0.ZU;2-Q
Abstract
PURPOSE: To assess the relative distribution in the cornea of amyloid and b eta ig-h3 gene product in lattice corneal dystrophy type IIIA (LCD-IIIA), METHODS: Serial sections from the cornea of a patient with LCD-IIIA were su bjected to either Congo red staining or immunohistochemistry employing an a ntibody to beta ig-h3, Also, genomic DNA was isolated from peripheral blood and used as a template for polymerase chain reaction to amplify all exons of beta ig-h3, RESULTS: Exon 11 of beta ig-h3 was mutated (Pro501Thr), Subepithelial and i ntrastromal congophilic deposits exhibited a birefringency characteristic o f amyloid, These regions of the tissue were also highly immunoreactive with the antibody to the beta ig-h3 gene product. CONCLUSION: Amyloid and Pro501Thr-mutated beta ig-h3 protein accumulate and colocalize in LCD-IIIA. (Am J Ophthalmol 1999;127:456-458. (C) 1999 by Els evier Science Inc. All rights reserved.).