A Novel Mutation in the M1S1 Gene Responsible for Gelatinous Droplike Corneal Dystrophy

To identify the genetic defect in the M1S1 gene causing gelatinous droplike corneal dystrophy (GDLD) in an Estonian family. DNA was extracted from members of a GDLD-affected family and control persons. Polymerase chain reaction followed by direct sequencing was used to detect mutations in the M1S1 g...

Full description

Saved in:
Bibliographic Details
Published inInvestigative ophthalmology & visual science Vol. 42; no. 12; pp. 2762 - 2764
Main Authors Tasa, Gunnar, Kals, Jaak, Muru, Kai, Juronen, Erkki, Piirsoo, Andres, Veromann, Siiri, Janes, Silvi, Mikelsaar, Aavo-Valdur, Lang, Aavo
Format Journal Article
LanguageEnglish
Published Rockville, MD ARVO 01.11.2001
Association for Research in Vision and Ophtalmology
Subjects
Antigens, Neoplasm - genetics
Biological and medical sciences
CD3 Complex - genetics
Cell Adhesion Molecules - genetics
Corneal Dystrophies, Hereditary - genetics
Diseases of cornea, anterior segment and sclera
DNA Mutational Analysis
Epithelial Cell Adhesion Molecule
Estonia
Female
Humans
Male
Medical sciences
Mutation
Ophthalmology
Pedigree
Polymerase Chain Reaction
Polymorphism, Genetic
Human
Eye disease
Gene
Family study
Droplet corneal dystrophy
Keratopathy
Mutation
Genetic determinism
Gelatinous corneal dystrophy
Genetic disease
Online AccessGet full text

Cover

More Information
Summary:To identify the genetic defect in the M1S1 gene causing gelatinous droplike corneal dystrophy (GDLD) in an Estonian family. DNA was extracted from members of a GDLD-affected family and control persons. Polymerase chain reaction followed by direct sequencing was used to detect mutations in the M1S1 gene. Sequencing results were confirmed with restriction analysis. Sequencing of the M1S1 gene revealed a novel mutation and a common polymorphism. All patients with GDLD were found to be homozygous for the insertion of nucleotide C in position 520 in M1S1. The mutation leads to formation of truncated protein. The mutation was excluded in 103 normal, unaffected individuals. Very close to the location where the mutation was identified in the M1S1 gene, a single-nucleotide polymorphism (518A/C) was found, changing aspartic acid to alanine at codon 173. The data indicate that mutation ins520C in the M1S1 gene is the primary cause of GDLD in the family studied.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0146-0404
1552-5783